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Conserved domains on  [gi|578834651|ref|XP_006723349|]
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transmembrane gamma-carboxyglutamic acid protein 2 isoform X1 [Homo sapiens]

Protein Classification

GLA and TM_EGFR-like domain-containing protein( domain architecture ID 10637896)

GLA and TM_EGFR-like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
28-95 2.30e-27

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


:

Pssm-ID: 214503  Cd Length: 65  Bit Score: 98.54  E-value: 2.30e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578834651    28 QEVFLGPPEAQSFLSshtRIPRANHWDLELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYI 95
Cdd:smart00069   1 GSVFLSRQEANKVLR---RQRRANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
109-138 2.75e-05

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


:

Pssm-ID: 213052  Cd Length: 38  Bit Score: 39.82  E-value: 2.75e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 578834651 109 SLAVGLTGGILLIVLAGLGAFWYLRWRQHR 138
Cdd:cd12087    7 SIAAGVVGGLLVLVILGLIVFLFRRRRHIK 36
 
Name Accession Description Interval E-value
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
28-95 2.30e-27

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 98.54  E-value: 2.30e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578834651    28 QEVFLGPPEAQSFLSshtRIPRANHWDLELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYI 95
Cdd:smart00069   1 GSVFLSRQEANKVLR---RQRRANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
55-95 7.37e-22

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 83.73  E-value: 7.37e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 578834651   55 LELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYI 95
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
109-138 2.75e-05

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


Pssm-ID: 213052  Cd Length: 38  Bit Score: 39.82  E-value: 2.75e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 578834651 109 SLAVGLTGGILLIVLAGLGAFWYLRWRQHR 138
Cdd:cd12087    7 SIAAGVVGGLLVLVILGLIVFLFRRRRHIK 36
 
Name Accession Description Interval E-value
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
28-95 2.30e-27

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 98.54  E-value: 2.30e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578834651    28 QEVFLGPPEAQSFLSshtRIPRANHWDLELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYI 95
Cdd:smart00069   1 GSVFLSRQEANKVLR---RQRRANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
55-95 7.37e-22

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 83.73  E-value: 7.37e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 578834651   55 LELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYI 95
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
TM_EGFR-like cd12087
Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine ...
109-138 2.75e-05

Transmembrane domain of the Epidermal Growth Factor Receptor family of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. They are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of EGFR family RTKs have been associated with increased breast cancer risk.


Pssm-ID: 213052  Cd Length: 38  Bit Score: 39.82  E-value: 2.75e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 578834651 109 SLAVGLTGGILLIVLAGLGAFWYLRWRQHR 138
Cdd:cd12087    7 SIAAGVVGGLLVLVILGLIVFLFRRRRHIK 36
 
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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