cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEK---------------- 64
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKetgenrlikhlqfttw 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  65 --------------------------------------------------------SFNIMDIVAQMREQRSGMVQTKEQ 88
Cdd:cd14596   115 pdhgtpqssdqlvkficymrkvhntgpivvhcsagigragvlicvdvllsliekdlSFNIKDIVREMRQQRYGMIQTKDQ 194

                         170
                  ....*....|...
gi 1207734434  89 YHFCYDIVLEVLR 101
Cdd:cd14596   195 YLFCYKVVLEVLQ 207

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEK---------------- 64
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKetgenrlikhlqfttw 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  65 --------------------------------------------------------SFNIMDIVAQMREQRSGMVQTKEQ 88
Cdd:cd14596   115 pdhgtpqssdqlvkficymrkvhntgpivvhcsagigragvlicvdvllsliekdlSFNIKDIVREMRQQRYGMIQTKDQ 194

                         170
                  ....*....|...
gi 1207734434  89 YHFCYDIVLEVLR 101
Cdd:cd14596   195 YLFCYKVVLEVLQ 207

Protein-tyrosine phosphatase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVV----------------- 62
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSnggseetrtvkhfhytg 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  63 ----------------------------------------------------------EKSFNIMDIVAQMREQRSGMVQ 84
Cdd:pfam00102 141 wpdhgvpespnslldllrkvrkssldgrsgpivvhcsagigrtgtfiaidialqqleaEGEVDIFQIVKELRSQRPGMVQ 220

                         170
                  ....*....|....
gi 1207734434  85 TKEQYHFCYDIVLE 98
Cdd:pfam00102 221 TLEQYIFLYDAILE 234

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEK---------------- 64
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKetgenrlikhlqfttw 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  65 --------------------------------------------------------SFNIMDIVAQMREQRSGMVQTKEQ 88
Cdd:cd14596   115 pdhgtpqssdqlvkficymrkvhntgpivvhcsagigragvlicvdvllsliekdlSFNIKDIVREMRQQRYGMIQTKDQ 194

                         170
                  ....*....|...
gi 1207734434  89 YHFCYDIVLEVLR 101
Cdd:cd14596   195 YLFCYKVVLEVLQ 207

Protein tyrosine phosphatase, catalytic domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434    1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVV------------------ 62
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTntgcsetrtvthyhytnw 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   63 --------------------------------------------------------EKSFNIMDIVAQMREQRSGMVQTK 86
Cdd:smart00194 168 pdhgvpespesildliravrksqststgpivvhcsagvgrtgtfiaidillqqleaGKEVDIFEIVKELRSQRPGMVQTE 247

                          170
                   ....*....|..
gi 1207734434   87 EQYHFCYDIVLE 98
Cdd:smart00194 248 EQYIFLYRAILE 259

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLEL-KHFRVFLENYQILQYFIIRMFQV------------------ 61
Cdd:cd14597    62 MVWEQKSTVIAMMTQEVEGGKIKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELediqtrevrhithlnfta 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  62 ----------------------VEKS--------------------------------FNIMDIVAQMREQRSGMVQTKE 87
Cdd:cd14597   142 wpdhdtpsqpeqlltfisymrhIHKSgpiithcsagigrsgtlicidvvlgliskdldFDISDIVRTMRLQRHGMVQTED 221

                         170
                  ....*....|...
gi 1207734434  88 QYHFCYDIVLEVL 100
Cdd:cd14597   222 QYIFCYQVILYVL 234

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FLENYQI-LQYFIIRMFQV----------------- 61
Cdd:cd18533    34 MIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLVSEEENdDGGFIVREFELskedgkvkkvyhiqyks 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  62 ------------------------------------------------------------------VEKSF-NIMDIVAQ 74
Cdd:cd18533   113 wpdfgvpdspedlltliklkrelndsasldppiivhcsagvgrtgtfialdslldelkrglsdsqdLEDSEdPVYEIVNQ 192

                         170       180
                  ....*....|....*....|
gi 1207734434  75 MREQRSGMVQTKEQYHFCYD 94
Cdd:cd18533   193 LRKQRMSMVQTLRQYIFLYD 212

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLENYQILQYFIIRMFQV------------------- 61
Cdd:cd14549    33 MVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLLSTEVLATYTVRTFSLknlklkkvkgrsservvyq 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  62 -------------------------------------------------------------VEKSFNIMDIVAQMREQRS 80
Cdd:cd14549   111 yhytqwpdhgvpdytlpvlsfvrkssaanppgagpivvhcsagvgrtgtyividsmlqqiqDKGTVNVFGFLKHIRTQRN 190

                         170
                  ....*....|....
gi 1207734434  81 GMVQTKEQYHFCYD 94
Cdd:cd14549   191 YLVQTEEQYIFIHD 204

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQV 61
Cdd:cd14548    58 MVWEQNSHTIVMLTQCMEKGRVKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKL 117

Protein tyrosine phosphatase, catalytic domain motif;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1207734434   53 YFIIRMFQVVEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 98
Cdd:smart00404  60 DILLQQLEAEAGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWP---------------ISLKK------------------------------- 34
Cdd:cd14540    35 MVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggehdaltfgeykVSTKFsvssgcytttglrvkhtlsgqsrtvwhlqyt 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  35 -------PLELKHFRVFLENYQILQYFIIRMFQ--------VVEKS------------------------FNIMDIVAQM 75
Cdd:cd14540   115 dwpdhgcPEDVSGFLDFLEEINSVRRHTNQDVAghnrnpptLVHCSagvgrtgvviladlmlycldhneeLDIPRVLALL 194

                         170       180
                  ....*....|....*....|....*
gi 1207734434  76 REQRSGMVQTKEQYHFCYDIVLEVL 100
Cdd:cd14540   195 RHQRMLLVQTLAQYKFVYNVLIQYL 219

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWP--ISLKK------------PL------ELK----------------HFRV- 43
Cdd:cd14605    73 MVFQENSRVIVMTTKEVERGKSKCVKYWPdeYALKEygvmrvrnvkesAAhdyilrELKlskvgqgntertvwqyHFRTw 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  44 --------------FLENYQILQYFIIRMFQVV---------EKSFNIMDI-------------------VAQMREQRSG 81
Cdd:cd14605   153 pdhgvpsdpggvldFLEEVHHKQESIMDAGPVVvhcsagigrTGTFIVIDIlidiirekgvdcdidvpktIQMVRSQRSG 232

                         170
                  ....*....|..
gi 1207734434  82 MVQTKEQYHFCY 93
Cdd:cd14605   233 MVQTEAQYRFIY 244

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEK 64
Cdd:cd14619    59 MIWEQQSSTIVMLTNCMEAGRVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQV 121

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.

                          10        20
                  ....*....|....*....|....*..
gi 1207734434  67 NIMDIVAQMREQRSGMVQTKEQYHFCY 93
Cdd:cd17658   179 DLSKTVRKFRSQRIGMVQTQDQYIFCY 205

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQI-LQYFI------------------------ 55
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQArTDYFIrtlllefqnetrrlyqfhyvnwpd 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  56 ----------------IRMFQ----------------------------------VVEKSFNIMDIVAQMREQRSGMVQT 85
Cdd:cd14604   199 hdvpssfdsildmislMRKYQehedvpicihcsagcgrtgaicaidytwnllkagKIPEEFNVFNLIQEMRTQRHSAVQT 278

                         170
                  ....*....|....*....
gi 1207734434  86 KEQYHFCYDIVLEVLRKLL 104
Cdd:cd14604   279 KEQYELVHRAIAQLFEKQL 297

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207734434  61 VVEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 99
Cdd:cd14602   195 IIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFL--ENYQI----------------------LQY--- 53
Cdd:cd14600   101 VVWEQKLSLIVMLTTLTERGRTKCHQYWP-DPPDVMEYGGFRVQChsEDCTIayvfremlltntqtgeertvthLQYvaw 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  54 --------------FIIRMFQ--------VVEKSFNI------------------------MDIVAQMREQRSGMVQTKE 87
Cdd:cd14600   180 pdhgvpddssdfleFVNYVRSkrvenepvLVHCSAGIgrtgvlvtmetamclternqpvypLDIVRKMRDQRAMMVQTSS 259

                         170
                  ....*....|....*
gi 1207734434  88 QYHFCYDIVLEVLRK 102
Cdd:cd14600   260 QYKFVCEAILRVYEE 274

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWP----ISLKKPLELKH----------FRVFL-------ENYQI--LQY---- 53
Cdd:cd14541    38 MVWEQKSTLIVMLTTLVERGRVKCHQYWPdlgeTMQFGNLQITCvseevtpsfaFREFIltntntgEERHItqMQYlawp 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  54 -------------FIIRMFQ---------VVEKSFNI------------------------MDIVAQMREQRSGMVQTKE 87
Cdd:cd14541   118 dhgvpddssdfldFVKRVRQnrvgmveptVVHCSAGIgrtgvlitmetamclieanepvypLDIVRTMRDQRAMLIQTPS 197

                         170
                  ....*....|..
gi 1207734434  88 QYHFCYDIVLEV 99
Cdd:cd14541   198 QYRFVCEAILRV 209

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYFI---------------IRMFQVV-- 62
Cdd:cd14627   115 MLWENNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQYILrefkvtdardgqsrtVRQFQFTdw 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  63 ----------------------------------------------------------EKSFNIMDIVAQMREQRSGMVQ 84
Cdd:cd14627   193 peqgvpksgegfidfigqvhktkeqfgqdgpisvhcsagvgrtgvfitlsivlermryEGVVDIFQTVKMLRTQRPAMVQ 272

                         170
                  ....*....|....*.
gi 1207734434  85 TKEQYHFCYDIVLEVL 100
Cdd:cd14627   273 TEDEYQFCYQAALEYL 288

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQV 61
Cdd:cd14617    59 MVWEQNVHNIVMVTQCVEKGRVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKI 118

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEK---------------- 64
Cdd:cd14539    34 MVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQSVRTTPTHVERIISIQHKdtrlsrsvvhlqfttw 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  65 -------------SF-------------------------------------------------NIMDIVAQMREQRSGM 82
Cdd:cd14539   114 pelglpdspnpllRFieevhshylqqrslqtpivvhcssgvgrtgafcllyaavqeieagngipDLPQLVRKMRQQRKYM 193

                         170
                  ....*....|..
gi 1207734434  83 VQTKEQYHFCYD 94
Cdd:cd14539   194 LQEKEHLKFCYE 205

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPlELKHFRVFLENYQILQYFIIRMFQVV------------------ 62
Cdd:cd14544    71 MVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVSkldqgdpireiwhyqyls 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  63 -----------------------EKSFN------------------------IMDIVA--------------QM-REQRS 80
Cdd:cd14544   150 wpdhgvpsdpggvlnfledvnqrQESLPhagpivvhcsagigrtgtfividmLLDQIKrkgldcdidiqktiQMvRSQRS 229

                         170
                  ....*....|...
gi 1207734434  81 GMVQTKEQYHFCY 93
Cdd:cd14544   230 GMVQTEAQYKFIY 242

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.

                          10        20
                  ....*....|....*....|....*..
gi 1207734434  67 NIMDIVAQMREQRSGMVQTKEQYHFCY 93
Cdd:cd14612   215 DILGIVCQLRLDRGGMIQTSEQYQFLH 241

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKsfnimdivaqmreqR 79
Cdd:cd14629   115 MLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDA--------------R 177

                          90
                  ....*....|..
gi 1207734434  80 SGMVQTKEQYHF 91
Cdd:cd14629   178 DGQSRTIRQFQF 189

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislkKPLEL-KHFRVFLENYQILQYFIIRMFQVVEKSFNIMDIVAQ 74
Cdd:cd14631    47 MIWQEQSACIVMVTNLVEVGRVKCYKYWP----DDTEVyGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQ 117

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1207734434  67 NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 98
Cdd:cd14634   172 NIIDVfhtVKTLRNNKSNMVETLEQYKFVYEVALE 206

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1207734434  62 VEKSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 94
Cdd:cd14556   169 VENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1207734434  69 MDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRK 102
Cdd:cd14601   179 LDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLE------------------LKHFRVFLE---------NY----- 48
Cdd:cd14614    74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWPFT-EEPVAygditvemlseeeqpdwaIREFRVSYAdevqdvmhfNYtawpd 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434  49 ----------QILQYF-IIR------------------------------MFQVVEKSF-NIMDIVAQMREQRSGMVQTK 86
Cdd:cd14614   153 hgvptanaaeSILQFVqMVRqqavkskgpmiihcsagvgrtgtfialdrlLQHIRDHEFvDILGLVSEMRSYRMSMVQTE 232

                         170
                  ....*....|.
gi 1207734434  87 EQYHFCYDIVL 97
Cdd:cd14614   233 EQYIFIHQCVQ 243

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1207734434  63 EKSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 98
Cdd:cd14620   194 EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSFNimdivaQMREQRs 80
Cdd:cd14630    65 MIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIK---VTLIETEPLAEYVIRTFTVQKKGYH------EIREIR- 134

                          90
                  ....*....|.
gi 1207734434  81 gmvqtkeQYHF 91
Cdd:cd14630   135 -------QFHF 138

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734434   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSfnimdiVAQMREQRs 80
Cdd:cd14633   102 MVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRG------VHEIREIR- 171