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Conserved domains on  [gi|1002585882|ref|XP_015671641|]
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integrin beta-1-binding protein 1 [Protobothrops mucrosquamatus]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-199 4.06e-130

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member pfam10480:

Pssm-ID: 473070  Cd Length: 200  Bit Score: 363.63  E-value: 4.06e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNSDTCAEFRVKYVGAIEKLNLDESK 80
Cdd:pfam10480   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNANSDACAEFRIKYVGAIEKLKFDEGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  81 TLEGPLDLINYIDVAQQDGKLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYLIVRMVCYDDGLGAGKSLLALKTT 160
Cdd:pfam10480  81 GLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVLHRHALYLIIRMLCYDDGLGAGKNLLALKTT 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002585882 161 DSNSEEYSLWIYQCNSLEQAQAICKVLSTAFDSVLTSEK 199
Cdd:pfam10480 161 DAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEK 199
 
Name Accession Description Interval E-value
ICAP-1_inte_bdg pfam10480
Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the ...
 1-199 4.06e-130

Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the cytoplasmic domains of beta-1 integrins in a highly specific manner, binding to a NPXY sequence motif on the beta-1 integrin. The cytoplasmic domains of integrins are essential for cell adhesion, and the fact that phosphorylation of ICAP-1 by interaction with the cell-matrix implies an important role of ICAP-1 during integrin-dependent cell adhesion. Overexpression of ICAP-1 strongly reduces the integrin-mediated cell spreading on extracellular matrix and inhibits both Cdc42 and Rac1. In addition, ICAP-1 induces release of Cdc42 from cellular membranes and prevents the dissociation of GDP from this GTPase. An additional function of ICAP-1 is to promote differentiation of osteoprogenitors by supporting their condensation through modulating the integrin high affinity state,


Pssm-ID: 119000  Cd Length: 200  Bit Score: 363.63  E-value: 4.06e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNSDTCAEFRVKYVGAIEKLNLDESK 80
Cdd:pfam10480   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNANSDACAEFRIKYVGAIEKLKFDEGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  81 TLEGPLDLINYIDVAQQDGKLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYLIVRMVCYDDGLGAGKSLLALKTT 160
Cdd:pfam10480  81 GLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVLHRHALYLIIRMLCYDDGLGAGKNLLALKTT 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002585882 161 DSNSEEYSLWIYQCNSLEQAQAICKVLSTAFDSVLTSEK 199
Cdd:pfam10480 161 DAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEK 199
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 61-191 6.23e-79

Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269985  Cd Length: 129  Bit Score: 231.57  E-value: 6.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  61 AEFRVKYVGAIEKLNlDESKTLEGPLDLINYIDVAQQDGKLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYLIVR 140
Cdd:cd13163     1 AEFRVKYVGVIENLE-GLSHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002585882 141 MVCYDDGLGaGKSLLALKTTDSNSEEYSLWIYQCNSLEQAQAICKVLSTAF 191
Cdd:cd13163    80 MVCYDDGLG-GKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF 129
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 58-200 2.18e-18

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 77.35  E-value: 2.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882   58 DTCAEFRVKYVGAIEklnLDESKTLEGPLDLINYIDVAQqdgkLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYL 137
Cdd:smart00462   1 GSGVSFRVKYLGSVE---VPEARGLQVVQEAIRKLRAAQ----GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002585882  138 IVRMVCYDDGLgagkSLLALKTTDSNSEEYSLWIYQCNSL--EQAQAICKVLSTAFDSVLTSEKS 200
Cdd:smart00462  74 ISFCAVGPDDL----DVFGYIARDPGSSRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARSE 134
 
Name Accession Description Interval E-value
ICAP-1_inte_bdg pfam10480
Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the ...
 1-199 4.06e-130

Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the cytoplasmic domains of beta-1 integrins in a highly specific manner, binding to a NPXY sequence motif on the beta-1 integrin. The cytoplasmic domains of integrins are essential for cell adhesion, and the fact that phosphorylation of ICAP-1 by interaction with the cell-matrix implies an important role of ICAP-1 during integrin-dependent cell adhesion. Overexpression of ICAP-1 strongly reduces the integrin-mediated cell spreading on extracellular matrix and inhibits both Cdc42 and Rac1. In addition, ICAP-1 induces release of Cdc42 from cellular membranes and prevents the dissociation of GDP from this GTPase. An additional function of ICAP-1 is to promote differentiation of osteoprogenitors by supporting their condensation through modulating the integrin high affinity state,


Pssm-ID: 119000  Cd Length: 200  Bit Score: 363.63  E-value: 4.06e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNSDTCAEFRVKYVGAIEKLNLDESK 80
Cdd:pfam10480   1 MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNANSDACAEFRIKYVGAIEKLKFDEGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  81 TLEGPLDLINYIDVAQQDGKLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYLIVRMVCYDDGLGAGKSLLALKTT 160
Cdd:pfam10480  81 GLEEPLDLINYIDAAQQDGKLPFVPGDEEFILGVSKYGIKVASLDQCDVLHRHALYLIIRMLCYDDGLGAGKNLLALKTT 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002585882 161 DSNSEEYSLWIYQCNSLEQAQAICKVLSTAFDSVLTSEK 199
Cdd:pfam10480 161 DAKNEECSIWVYQCNSAEHAQAICKVLSSAFDCALASEK 199
PTB_ICAP1 cd13163
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ...
 61-191 6.23e-79

Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269985  Cd Length: 129  Bit Score: 231.57  E-value: 6.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  61 AEFRVKYVGAIEKLNlDESKTLEGPLDLINYIDVAQQDGKLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYLIVR 140
Cdd:cd13163     1 AEFRVKYVGVIENLE-GLSHSLEGPLDLINAIDVAQQDGKLPFVAIEEEVILGLSKYGIKVTELNQPVVLKRHPLYSIIR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002585882 141 MVCYDDGLGaGKSLLALKTTDSNSEEYSLWIYQCNSLEQAQAICKVLSTAF 191
Cdd:cd13163    80 MVCYDDGLG-GKSLLAVKTGDPGEEVYSLLAYQCNSQEQAIEICKTLSTAF 129
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 58-200 2.18e-18

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 77.35  E-value: 2.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882   58 DTCAEFRVKYVGAIEklnLDESKTLEGPLDLINYIDVAQqdgkLPFVPGEEEFIMGVSKYGIKVTSLDQYDVLHRHALYL 137
Cdd:smart00462   1 GSGVSFRVKYLGSVE---VPEARGLQVVQEAIRKLRAAQ----GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002585882  138 IVRMVCYDDGLgagkSLLALKTTDSNSEEYSLWIYQCNSL--EQAQAICKVLSTAFDSVLTSEKS 200
Cdd:smart00462  74 ISFCAVGPDDL----DVFGYIARDPGSSRFACHVFRCEKAaeDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 61-191 2.80e-13

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 63.68  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  61 AEFRVKYVGAIEKLNLDESKTLEGPLDLINYIdVAQQDGKLPfvpgeeEFIMGVSKYGIKVTSLDQYDVLHRHALYLIVR 140
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAA-LKSSKRKPG------PVLLEVSSKGVKLLDLDTKELLLRHPLHRISY 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002585882 141 mVCYDDGlgaGKSLLALKTTDSNSEEYSLWIYQCNSLEQAQAICKVLSTAF 191
Cdd:cd00934    74 -CGRDPD---NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB_CCM2 cd13166
Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22 ...
 62-196 4.22e-04

Cerebral cavernous malformation 2 FERM domain C-lobe; CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM) along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signalling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours. CCM2 possesses an N-terminal PTB domain and a C-terminal Karet domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269987  Cd Length: 193  Bit Score: 39.79  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882  62 EFRVKYVGAIEKL--NLDESKTLEgpldLINYIDVAQQDGKLPFV-PGEEEFIMGVSKYGIKVTSLDQYDVLHR---H-- 133
Cdd:cd13166    22 EKEVKYLGQLTSVpgSLDPSSRTE----LLQLLDTARRLGQLPLQlTPEQDAILSLSAYNVKLLWRDGEDLILRvptHdi 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002585882 134 ---------ALYLIVRMVCYDDGLGAGKSLLALKTTDSNSEEYS---------LWIYQCNSLEQAQAICKVLSTAFDSVL 195
Cdd:cd13166    98 aavsyvrddSLHLVVLKTASEPGISPSQSLSAESSPTSGSLSESgpvpveycnLVVLACENKAAAEELCSLLCQVFQIVY 177


                  .
gi 1002585882 196 T 196
Cdd:cd13166   178 T 178
 
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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