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Conserved domains on  [gi|238624151|ref|NP_808288|]
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ras and Rab interactor 3 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SH2_RIN3 cd10395
Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins; RIN3, a ...
52-153 1.17e-62

Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins; RIN3, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. RIN3 stimulated the formation of GTP-bound Rab31, a Rab5-subfamily GTPase, and formed enlarged vesicles and tubular structures, where it colocalized with Rab31. Transferrin appeared to be transported partly through the RIN3-positive vesicles to early endosomes. RIN3 interacts via its Pro-rich domain with amphiphysin II, which contains SH3 domain and participates in receptor-mediated endocytosis. RIN3, a Rab5 and Rab31 GEF, plays an important role in the transport pathway from plasma membrane to early endosomes. Mutations in the region between the SH2 and RH domain of RIN3 specifically abolished its GEF action on Rab31, but not Rab5. RIN3 was also found to partially translocate the cation-dependent mannose 6-phosphate receptor from the trans-Golgi network to peripheral vesicles and that this is dependent on its Rab31-GEF activity. These data indicate that RIN3 specifically acts as a GEF for Rab31. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


:

Pssm-ID: 198258  Cd Length: 101  Bit Score: 206.93  E-value: 1.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  52 VLEKLVKTCPVWLQLGLGQAEAAKILQQEMAGMFLVCRDNNLKQLVLCVHFPSlKGSSAEVLEYPIKEEKAILYLEGSVL 131
Cdd:cd10395    1 ILEKLIKTCPVWLQLGMNQAEAARILHKEVAGMFLVRRDSNSKQMVLCVHFPS-NESSAEVLEYPIKEEKSILYLEGSVL 79
                         90       100
                 ....*....|....*....|..
gi 238624151 132 VFEDIFRLIAFYCVSRDLLPFT 153
Cdd:cd10395   80 VFEDIFKLIAFYCVSRDLLPFT 101
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
874-961 2.32e-40

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd16130:

Pssm-ID: 475130  Cd Length: 88  Bit Score: 143.33  E-value: 2.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151 874 QDFICVSYLKPEQQSRTLASRADTAAQALCAQCAEKFEVSQPQDYRLFVLVDGRCFQLADEALPHRIKGYLLRSEPKRDF 953
Cdd:cd16130    1 QDFISVSFLEPGSNTRTLAIRPDTTAEDLCKQCAEKFEVLDPENYGLFVLVDGRCLQLADDALPHHIKSDLLKSEPRKDF 80

                 ....*...
gi 238624151 954 HFVYRPQD 961
Cdd:cd16130   81 HFLYKQLS 88
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
736-839 1.12e-35

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


:

Pssm-ID: 460489  Cd Length: 104  Bit Score: 130.79  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  736 MEKILQKLTSMHKAYSPGKKISILLKTCKLIYDSMALGNPGKPYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPAL 815
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80
                          90       100
                  ....*....|....*....|....
gi 238624151  816 QLGEGSYYLTTTYGALEHIKNYDK 839
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIESLDP 104
 
Name Accession Description Interval E-value
SH2_RIN3 cd10395
Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins; RIN3, a ...
52-153 1.17e-62

Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins; RIN3, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. RIN3 stimulated the formation of GTP-bound Rab31, a Rab5-subfamily GTPase, and formed enlarged vesicles and tubular structures, where it colocalized with Rab31. Transferrin appeared to be transported partly through the RIN3-positive vesicles to early endosomes. RIN3 interacts via its Pro-rich domain with amphiphysin II, which contains SH3 domain and participates in receptor-mediated endocytosis. RIN3, a Rab5 and Rab31 GEF, plays an important role in the transport pathway from plasma membrane to early endosomes. Mutations in the region between the SH2 and RH domain of RIN3 specifically abolished its GEF action on Rab31, but not Rab5. RIN3 was also found to partially translocate the cation-dependent mannose 6-phosphate receptor from the trans-Golgi network to peripheral vesicles and that this is dependent on its Rab31-GEF activity. These data indicate that RIN3 specifically acts as a GEF for Rab31. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198258  Cd Length: 101  Bit Score: 206.93  E-value: 1.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  52 VLEKLVKTCPVWLQLGLGQAEAAKILQQEMAGMFLVCRDNNLKQLVLCVHFPSlKGSSAEVLEYPIKEEKAILYLEGSVL 131
Cdd:cd10395    1 ILEKLIKTCPVWLQLGMNQAEAARILHKEVAGMFLVRRDSNSKQMVLCVHFPS-NESSAEVLEYPIKEEKSILYLEGSVL 79
                         90       100
                 ....*....|....*....|..
gi 238624151 132 VFEDIFRLIAFYCVSRDLLPFT 153
Cdd:cd10395   80 VFEDIFKLIAFYCVSRDLLPFT 101
RA_Rin3 cd16130
Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3); Rin3, also termed Ras ...
874-961 2.32e-40

Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3); Rin3, also termed Ras interaction/interference protein 3, is a RAS effector and a RAB5-activating guanine nucleotide exchange factor (GEF) specifically for GTPase Rab31. It functions as a negative regulator of mast cell responses to Stem Cell Factor (SCF). Rin3 contains the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains.


Pssm-ID: 340547  Cd Length: 88  Bit Score: 143.33  E-value: 2.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151 874 QDFICVSYLKPEQQSRTLASRADTAAQALCAQCAEKFEVSQPQDYRLFVLVDGRCFQLADEALPHRIKGYLLRSEPKRDF 953
Cdd:cd16130    1 QDFISVSFLEPGSNTRTLAIRPDTTAEDLCKQCAEKFEVLDPENYGLFVLVDGRCLQLADDALPHHIKSDLLKSEPRKDF 80

                 ....*...
gi 238624151 954 HFVYRPQD 961
Cdd:cd16130   81 HFLYKQLS 88
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
736-839 1.12e-35

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 130.79  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  736 MEKILQKLTSMHKAYSPGKKISILLKTCKLIYDSMALGNPGKPYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPAL 815
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80
                          90       100
                  ....*....|....*....|....
gi 238624151  816 QLGEGSYYLTTTYGALEHIKNYDK 839
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIESLDP 104
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
736-852 4.40e-28

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 109.47  E-value: 4.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151   736 MEKILQKLTSMHKaySPGKKISILLKTCKLIYDSMALgNPGKPYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPAL 815
Cdd:smart00167   4 IEQIELKFLQLYK--SPSDKIKCLLRACKLIYTLLET-QSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 238624151   816 QLGEGSYYLTTTYGALEHIKNYDKITVTRQLSVEVQD 852
Cdd:smart00167  81 LTGEGGYYLTSLSAALALIKGLTEAHALPLSPEQELE 117
 
Name Accession Description Interval E-value
SH2_RIN3 cd10395
Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins; RIN3, a ...
52-153 1.17e-62

Src homology 2 (SH2) domain found in Ras and Rab interactor 3 (RIN3)-like proteins; RIN3, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. RIN3 stimulated the formation of GTP-bound Rab31, a Rab5-subfamily GTPase, and formed enlarged vesicles and tubular structures, where it colocalized with Rab31. Transferrin appeared to be transported partly through the RIN3-positive vesicles to early endosomes. RIN3 interacts via its Pro-rich domain with amphiphysin II, which contains SH3 domain and participates in receptor-mediated endocytosis. RIN3, a Rab5 and Rab31 GEF, plays an important role in the transport pathway from plasma membrane to early endosomes. Mutations in the region between the SH2 and RH domain of RIN3 specifically abolished its GEF action on Rab31, but not Rab5. RIN3 was also found to partially translocate the cation-dependent mannose 6-phosphate receptor from the trans-Golgi network to peripheral vesicles and that this is dependent on its Rab31-GEF activity. These data indicate that RIN3 specifically acts as a GEF for Rab31. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198258  Cd Length: 101  Bit Score: 206.93  E-value: 1.17e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  52 VLEKLVKTCPVWLQLGLGQAEAAKILQQEMAGMFLVCRDNNLKQLVLCVHFPSlKGSSAEVLEYPIKEEKAILYLEGSVL 131
Cdd:cd10395    1 ILEKLIKTCPVWLQLGMNQAEAARILHKEVAGMFLVRRDSNSKQMVLCVHFPS-NESSAEVLEYPIKEEKSILYLEGSVL 79
                         90       100
                 ....*....|....*....|..
gi 238624151 132 VFEDIFRLIAFYCVSRDLLPFT 153
Cdd:cd10395   80 VFEDIFKLIAFYCVSRDLLPFT 101
SH2_RIN_family cd10339
Src homology 2 (SH2) domain found in Ras and Rab interactor (RIN)-family; The RIN (AKA Ras ...
52-153 1.52e-51

Src homology 2 (SH2) domain found in Ras and Rab interactor (RIN)-family; The RIN (AKA Ras interaction/interference) family is composed of RIN1, RIN2 and RIN3. These proteins have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs, and RIN3 specifically functions as a Rab31-GEF. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198202  Cd Length: 101  Bit Score: 175.80  E-value: 1.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  52 VLEKLVKTCPVWLQLGLGQAEAAKILQQEMAGMFLVCRDNNLKQLVLCVHFPSlKGSSAEVLEYPIKEEKAILYLEGSVL 131
Cdd:cd10339    1 LLERLLLTRPVWLQLQLNAAEAAHMLQTEPPGTFLVRKSNTRQCQVLCMRLPE-ASGPAFVSEHYIKESPGGVSLEGSEL 79
                         90       100
                 ....*....|....*....|..
gi 238624151 132 VFEDIFRLIAFYCVSRDLLPFT 153
Cdd:cd10339   80 MFPDLFRLIAFYCHSRDILPFT 101
RA_Rin3 cd16130
Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3); Rin3, also termed Ras ...
874-961 2.32e-40

Ras-associating (RA) domain found in Ras and Rab interactor 3 (Rin3); Rin3, also termed Ras interaction/interference protein 3, is a RAS effector and a RAB5-activating guanine nucleotide exchange factor (GEF) specifically for GTPase Rab31. It functions as a negative regulator of mast cell responses to Stem Cell Factor (SCF). Rin3 contains the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains.


Pssm-ID: 340547  Cd Length: 88  Bit Score: 143.33  E-value: 2.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151 874 QDFICVSYLKPEQQSRTLASRADTAAQALCAQCAEKFEVSQPQDYRLFVLVDGRCFQLADEALPHRIKGYLLRSEPKRDF 953
Cdd:cd16130    1 QDFISVSFLEPGSNTRTLAIRPDTTAEDLCKQCAEKFEVLDPENYGLFVLVDGRCLQLADDALPHHIKSDLLKSEPRKDF 80

                 ....*...
gi 238624151 954 HFVYRPQD 961
Cdd:cd16130   81 HFLYKQLS 88
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
736-839 1.12e-35

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 130.79  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  736 MEKILQKLTSMHKAYSPGKKISILLKTCKLIYDSMALGNPGKPYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPAL 815
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80
                          90       100
                  ....*....|....*....|....
gi 238624151  816 QLGEGSYYLTTTYGALEHIKNYDK 839
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIESLDP 104
SH2_RIN2 cd10394
Src homology 2 (SH2) domain found in Ras and Rab interactor 2 (RIN2)-like proteins; RIN2, a ...
52-153 2.73e-29

Src homology 2 (SH2) domain found in Ras and Rab interactor 2 (RIN2)-like proteins; RIN2, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. Ras induces activation of Rab5 through RIN2, which is a direct downstream target of Ras and a direct upstream regulator of Rab5. In other words it is the binding of the GTP-bound form of Ras to the RA domain of RIN2 that enhances the GEF activity toward Rab5. It is thought that the RA domain negatively regulates the Rab5 GEF activity. In steady state, RIN2 is likely to form a closed conformation by an intramolecular interaction between the RA domain and the Vps9p-like (Rab5 GEF) domain, negatively regulating the Rab5 GEF activity. In the active state, the binding of Ras to the RA domain may reduce the intramolecular interaction and stabilize an open conformation of RIN2. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198257  Cd Length: 100  Bit Score: 112.21  E-value: 2.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  52 VLEKLVKTCPVWLQLGLGQAEAAKILQQEMAGMFLVCRDNNLKQLVLCVHFPSlkGSSAEVLEYPIKEEKAILYLEGSVL 131
Cdd:cd10394    1 ILDRLLHTHPIWLQLSLSEEEAAEVLQAQPPGIFLVRKSSKMQKKVLSLRLPC--EFGAPLKEFAIKESTYTFSLEGSGI 78
                         90       100
                 ....*....|....*....|..
gi 238624151 132 VFEDIFRLIAFYCVSRDLLPFT 153
Cdd:cd10394   79 SFADLFRLIAFYCISRDVLPFT 100
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
736-852 4.40e-28

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 109.47  E-value: 4.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151   736 MEKILQKLTSMHKaySPGKKISILLKTCKLIYDSMALgNPGKPYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPAL 815
Cdd:smart00167   4 IEQIELKFLQLYK--SPSDKIKCLLRACKLIYTLLET-QSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 238624151   816 QLGEGSYYLTTTYGALEHIKNYDKITVTRQLSVEVQD 852
Cdd:smart00167  81 LTGEGGYYLTSLSAALALIKGLTEAHALPLSPEQELE 117
RA_Rin cd01776
Ras-associating (RA) domain of Ras and Rab interactor (Rin) protein family; Family of ...
874-961 1.45e-22

Ras-associating (RA) domain of Ras and Rab interactor (Rin) protein family; Family of Ras-interaction/interference (Rin) proteins, also known as Ras and Rab interactors, is composed of Rin1, Rin2, and Rin3, which have multifunctional domains, including SH2 and proline-rich domains in the N-terminal region, and RH, VPS9, and RA domains in the C-terminal region. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domains of Rin1, Rin2, and Rin3 are well conserved and they all have Ras binding characteristics.


Pssm-ID: 340474  Cd Length: 90  Bit Score: 92.74  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151 874 QDFICVSYLKPEQ---QSRTLASRADTAAQALCAQCAEKFEVSQPQDYRLFVLVDGRCFQLADEALPHRIKGYLLRsEPK 950
Cdd:cd01776    1 QGFLRVAVPDENNgsiVSKTLPVRPSMTAREVCKMIAHKFRVTNPQDYGLFLLVDGEEIQLEDNECPQLIKGELLA-TSK 79
                         90
                 ....*....|.
gi 238624151 951 RDFHFVYRPQD 961
Cdd:cd01776   80 KPCYFAYKRID 90
SH2_RIN1 cd10393
Src homology 2 (SH2) domain found in Ras and Rab interactor 1 (RIN1)-like proteins; RIN1, a ...
52-153 3.64e-21

Src homology 2 (SH2) domain found in Ras and Rab interactor 1 (RIN1)-like proteins; RIN1, a member of the RIN (AKA Ras interaction/interference) family, have multifunctional domains including SH2 and proline-rich (PR) domains in the N-terminal region, and RIN-family homology (RH), VPS9 and Ras-association (RA) domains in the C-terminal region. RIN proteins function as Rab5-GEFs. Previous studies showed that RIN1 interacts with EGF receptors via its SH2 domain and regulates trafficking and degradation of EGF receptors via its interaction with STAM, indicating a vital role for RIN1 in regulating endosomal trafficking of receptor tyrosine kinases (RTKs). RIN1 was first identified as a Ras-binding protein that suppresses the activated RAS2 allele in S. cerevisiae. RIN1 binds to the activated Ras through its carboxyl-terminal domain and this Ras-binding domain also binds to 14-3-3 proteins as Raf-1 does. The SH2 domain of RIN1 are thought to interact with the phosphotyrosine-containing proteins, but the physiological partners for this domain are unknown. The proline-rich domain in RIN1 is similar to the consensus SH3 binding regions. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198256  Cd Length: 101  Bit Score: 89.14  E-value: 3.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  52 VLEKLVKTCPVWLQLGLGQAEAAKILQQEMAGMFLVCRDNNLKQLVLCVHFPSLKGSSAeVLEYPIKEEKAILYLEGSVL 131
Cdd:cd10393    1 LRERLLLTRPVWLQLRANAAAALHVLRTEPPGTFLVRKSNTRQCQALCVRLPEASGPSF-VSSHYIQESPGGVSLEGSEL 79
                         90       100
                 ....*....|....*....|..
gi 238624151 132 VFEDIFRLIAFYCVSRDLLPFT 153
Cdd:cd10393   80 TFPDLVQLICAYCHTRDILLLP 101
RA_Rin1 cd17215
Ras-associating (RA) domain found in Ras and Rab interactor 1 (Rin1); Rin1, also termed Ras ...
874-961 3.45e-07

Ras-associating (RA) domain found in Ras and Rab interactor 1 (Rin1); Rin1, also termed Ras inhibitor JC99, or Ras interaction/interference protein 1, is a downstream Ras effector that represents a unique class of Ras effector connected to two independent signaling pathways. The first effector pathway is the direct activation of RAB5-mediated endocytosis and the second pathway involves direct activation of ABL tyrosine kinase activity. Rin1 functions as a guanine nucleotide exchange factor (GEF) for RAB5 GTPases. The RAB5 GEF activity of Rin1 promotes early endosome fusion, an early event in transit to the lysosome. Rin1 binds the SH3 and SH2 domains of ABL proteins, ABL1 and ABL2, and activates their tyrosine kinase activity. Rin1 contains SH2 and proline-rich domains in the N-terminal region, and RH, VPS9, and RA domains in the C-terminal region. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340735  Cd Length: 88  Bit Score: 48.82  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151 874 QDFICVSYLKPEQ--QSRTLASRADTAAQALCAQCAEKFEVSQPQDYRLFVLVDGRCFQLADEALPHRIKGYLlrSEPKR 951
Cdd:cd17215    1 QNFLRVAYQDPSSgcTSKTLAVPPSATVADLNQLCATKFKVTQPETYGIFLYKEQGYQRLPPDALPQRIKAQL--KEKGS 78
                         90
                 ....*....|
gi 238624151 952 DFHFVYRPQD 961
Cdd:cd17215   79 TFYFVYQRAE 88
RA_Rin2 cd16131
Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras ...
908-958 7.63e-07

Ras-associating (RA) domain found in Ras and Rab interactor 2 (Rin2); Rin2, also termed Ras association domain family 4, or Ras inhibitor JC265, or Ras interaction/interference protein 2, is a Rab5 GDP/GTP exchange factor with the Vps9p-like guanine nucleotide exchange factor and Ras-association (RA) domains. Rin2 connects three GTPases, R-Ras, Rab5 and Rac1, to promote endothelial cell adhesion through the regulation of integrin internalization and Rac1 activation. Rin2 is involved in the regulation of Rab5-mediated early endocytosis. The deficiency of Rin2 can cause the RIN2 syndrome, an autosomal recessive connective tissue disorder.


Pssm-ID: 340548  Cd Length: 91  Bit Score: 47.93  E-value: 7.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 238624151 908 EKFEVSQPQDYRLFVLVDGRCFQLADEALPHRIKGYlLRSEPK-RDFHFVYR 958
Cdd:cd16131   38 QKFKVQDPENYSLFLLIDDTWQQLAEDTYPQKIKAE-LHSRPQpQIFHFVYK 88
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
63-143 3.53e-03

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 37.44  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624151  63 WLQLGLGQAEAAKILQQEMAGMFLV-CRDNNLKQLVLcvhfpSLKGSSAEVLEYPIK-EEKAILYLEGSVLVFEDIFRLI 140
Cdd:cd00173    2 WFHGSISREEAERLLRGKPDGTFLVrESSSEPGDYVL-----SVRSGDGKVKHYLIErNEGGYYLLGGSGRTFPSLPELV 76

                 ...
gi 238624151 141 AFY 143
Cdd:cd00173   77 EHY 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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