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Conserved domains on  [gi|1958654395|ref|XP_038957159|]
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integrin alpha-X isoform X2 [Rattus norvegicus]

Protein Classification

integrin alpha( domain architecture ID 11619903)

integrin alpha forms a heterodimer with integrin beta to mediate cell-extracellular matrix and cell-cell interactions; integrin alpha is a component of integrin, a cell adhesion molecule that mediates cell-extracellular matrix and cell-cell interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
342-766 4.77e-33

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


The actual alignment was detected with superfamily member pfam08441:

Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 133.60  E-value: 4.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 342 RPILRMSSTIQFTPTEISRSVFECQGQVTREQTLgTATVCLrtyeSSKTQRGDLQSIV-TFDLALDPGR---LSPRAIFK 417
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCF-TVRACF----SYTGKPIPNPSLVlNYELELDRQKkkgLPPRVLFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 418 ETKTQALTKVRTL--GLSSHCEPVTLLLPACVEDSVTPITLRLNFSLVGVPIP--SLQNLQPMLAVDEQTYFTASLPFEK 493
Cdd:pfam08441  76 DSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRApsDLPGLKPILDQNQPSTVQEQANFLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 494 NCGADHICQDDLGI--IFGFPDL-KTLVVGSNLELSVAVTVTNDGEDSYGTTITLFYPVGLSFRRVaeaqvfLRTEDTQQ 570
Cdd:pfam08441 156 DCGEDNVCVPDLQLsaKFDSRESdEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGV------RREGSEKQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 571 wqqqgrhslhLMCDSTpdrsqgiwsTSCSSRHVI------FRGGSQMTFLVTFDVSPKAELGDRLLLRARVSSENG-VPE 643
Cdd:pfam08441 230 ----------LSCTAK---------KENSTRQVVcdlgnpMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEqNSN 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 644 TRKTTfqLELPVKYAVYTVIS--SH-DQ-FTKYLNFSASEKSRV-----SVVEHRFQVNNLGQRDLP-VSINFRVPTELK 713
Cdd:pfam08441 291 SNPVS--LKVPVVAEAQLSLSgvSKpDQvVGGSVKGESAMKPRSeedigPLVEHTYEVINNGPSTVSgASLEISWPYELS 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 714 GET----VWTVMVSHPQNPSTQCYQNRLKPTQ-------------------FDLLTHMQKSP----VLDC-SIADCLHFR 765
Cdd:pfam08441 369 NGKwllyLLDVQGQGKGECSPQNEINPLNLTQslesskplrtsrvhhvvkrRDVLKSEKATQtasvLLSCdSGARCVVIR 448

                  .
gi 1958654395 766 C 766
Cdd:pfam08441 449 C 449
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1-51 4.15e-17

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member cd01469:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 177  Bit Score: 80.09  E-value: 4.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958654395   1 MAEAAGIIRYAIGVGQAFYQAQSRQELKDIASSPSREYVFSVENFDALKDI 51
Cdd:cd01469   127 QAEREGIIRYAIGVGGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
243-298 3.01e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 56.61  E-value: 3.01e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395  243 PWGRFGAALTVLGDVNGDDLADVAIGAPGEEESR--GAVYIFHGaSRLEISPSPSQRI 298
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
180-236 3.28e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 56.23  E-value: 3.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395  180 IGSYFGASLCSV-DMDRDDSTDLvLIGAPHYYEQTRGGQVSVCPVPGVGSRWQCEATL 236
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
308-332 2.07e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.35  E-value: 2.07e-03
                           10        20
                   ....*....|....*....|....*
gi 1958654395  308 QYFGQSLSGGQDLTGDGLVDLAVGS 332
Cdd:smart00191   3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
863-877 8.95e-03

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 34.40  E-value: 8.95e-03
                          10
                  ....*....|....*
gi 1958654395 863 KAGFFKRQYKEMLAE 877
Cdd:pfam00357   1 KCGFFKRNYPPQEEE 15
 
Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
342-766 4.77e-33

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 133.60  E-value: 4.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 342 RPILRMSSTIQFTPTEISRSVFECQGQVTREQTLgTATVCLrtyeSSKTQRGDLQSIV-TFDLALDPGR---LSPRAIFK 417
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCF-TVRACF----SYTGKPIPNPSLVlNYELELDRQKkkgLPPRVLFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 418 ETKTQALTKVRTL--GLSSHCEPVTLLLPACVEDSVTPITLRLNFSLVGVPIP--SLQNLQPMLAVDEQTYFTASLPFEK 493
Cdd:pfam08441  76 DSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRApsDLPGLKPILDQNQPSTVQEQANFLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 494 NCGADHICQDDLGI--IFGFPDL-KTLVVGSNLELSVAVTVTNDGEDSYGTTITLFYPVGLSFRRVaeaqvfLRTEDTQQ 570
Cdd:pfam08441 156 DCGEDNVCVPDLQLsaKFDSRESdEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGV------RREGSEKQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 571 wqqqgrhslhLMCDSTpdrsqgiwsTSCSSRHVI------FRGGSQMTFLVTFDVSPKAELGDRLLLRARVSSENG-VPE 643
Cdd:pfam08441 230 ----------LSCTAK---------KENSTRQVVcdlgnpMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEqNSN 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 644 TRKTTfqLELPVKYAVYTVIS--SH-DQ-FTKYLNFSASEKSRV-----SVVEHRFQVNNLGQRDLP-VSINFRVPTELK 713
Cdd:pfam08441 291 SNPVS--LKVPVVAEAQLSLSgvSKpDQvVGGSVKGESAMKPRSeedigPLVEHTYEVINNGPSTVSgASLEISWPYELS 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 714 GET----VWTVMVSHPQNPSTQCYQNRLKPTQ-------------------FDLLTHMQKSP----VLDC-SIADCLHFR 765
Cdd:pfam08441 369 NGKwllyLLDVQGQGKGECSPQNEINPLNLTQslesskplrtsrvhhvvkrRDVLKSEKATQtasvLLSCdSGARCVVIR 448

                  .
gi 1958654395 766 C 766
Cdd:pfam08441 449 C 449
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
1-51 4.15e-17

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 80.09  E-value: 4.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958654395   1 MAEAAGIIRYAIGVGQAFYQAQSRQELKDIASSPSREYVFSVENFDALKDI 51
Cdd:cd01469   127 QAEREGIIRYAIGVGGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
243-298 3.01e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 56.61  E-value: 3.01e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395  243 PWGRFGAALTVLGDVNGDDLADVAIGAPGEEESR--GAVYIFHGaSRLEISPSPSQRI 298
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
180-236 3.28e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 56.23  E-value: 3.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395  180 IGSYFGASLCSV-DMDRDDSTDLvLIGAPHYYEQTRGGQVSVCPVPGVGSRWQCEATL 236
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
VWA pfam00092
von Willebrand factor type A domain;
2-54 1.94e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.59  E-value: 1.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958654395   2 AEAAGIIRYAIGVGQAFYQaqsrqELKDIASSPSREYVFSVENFDALKDIQNQ 54
Cdd:pfam00092 127 LKSAGVTVFAVGVGNADDE-----ELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
247-282 7.32e-08

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 49.05  E-value: 7.32e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958654395 247 FGAALTVlGDVNGDDLADVAIGAPGE-EESRGAVYIF 282
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
2-52 1.24e-03

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 40.90  E-value: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958654395    2 AEAAGIIRYAIGVGQAFYQAqsrqELKDIASSPSREYVFSVENFDALKDIQ 52
Cdd:smart00327 129 LKRSGVKVFVVGVGNDVDEE----ELKKLASAPGGVYVFLPELLDLLIDLL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
308-332 2.07e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.35  E-value: 2.07e-03
                           10        20
                   ....*....|....*....|....*
gi 1958654395  308 QYFGQSLSGGQDLTGDGLVDLAVGS 332
Cdd:smart00191   3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
863-877 8.95e-03

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


Pssm-ID: 459778  Cd Length: 15  Bit Score: 34.40  E-value: 8.95e-03
                          10
                  ....*....|....*
gi 1958654395 863 KAGFFKRQYKEMLAE 877
Cdd:pfam00357   1 KCGFFKRNYPPQEEE 15
 
Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
342-766 4.77e-33

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 133.60  E-value: 4.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 342 RPILRMSSTIQFTPTEISRSVFECQGQVTREQTLgTATVCLrtyeSSKTQRGDLQSIV-TFDLALDPGR---LSPRAIFK 417
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCF-TVRACF----SYTGKPIPNPSLVlNYELELDRQKkkgLPPRVLFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 418 ETKTQALTKVRTL--GLSSHCEPVTLLLPACVEDSVTPITLRLNFSLVGVPIP--SLQNLQPMLAVDEQTYFTASLPFEK 493
Cdd:pfam08441  76 DSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRApsDLPGLKPILDQNQPSTVQEQANFLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 494 NCGADHICQDDLGI--IFGFPDL-KTLVVGSNLELSVAVTVTNDGEDSYGTTITLFYPVGLSFRRVaeaqvfLRTEDTQQ 570
Cdd:pfam08441 156 DCGEDNVCVPDLQLsaKFDSRESdEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGV------RREGSEKQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 571 wqqqgrhslhLMCDSTpdrsqgiwsTSCSSRHVI------FRGGSQMTFLVTFDVSPKAELGDRLLLRARVSSENG-VPE 643
Cdd:pfam08441 230 ----------LSCTAK---------KENSTRQVVcdlgnpMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEqNSN 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 644 TRKTTfqLELPVKYAVYTVIS--SH-DQ-FTKYLNFSASEKSRV-----SVVEHRFQVNNLGQRDLP-VSINFRVPTELK 713
Cdd:pfam08441 291 SNPVS--LKVPVVAEAQLSLSgvSKpDQvVGGSVKGESAMKPRSeedigPLVEHTYEVINNGPSTVSgASLEISWPYELS 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958654395 714 GET----VWTVMVSHPQNPSTQCYQNRLKPTQ-------------------FDLLTHMQKSP----VLDC-SIADCLHFR 765
Cdd:pfam08441 369 NGKwllyLLDVQGQGKGECSPQNEINPLNLTQslesskplrtsrvhhvvkrRDVLKSEKATQtasvLLSCdSGARCVVIR 448

                  .
gi 1958654395 766 C 766
Cdd:pfam08441 449 C 449
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
1-51 4.15e-17

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 80.09  E-value: 4.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958654395   1 MAEAAGIIRYAIGVGQAFYQAQSRQELKDIASSPSREYVFSVENFDALKDI 51
Cdd:cd01469   127 QAEREGIIRYAIGVGGHFQRENSREELKTIASKPPEEHFFNVTDFAALKDI 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
243-298 3.01e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 56.61  E-value: 3.01e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395  243 PWGRFGAALTVLGDVNGDDLADVAIGAPGEEESR--GAVYIFHGaSRLEISPSPSQRI 298
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
180-236 3.28e-10

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 56.23  E-value: 3.28e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395  180 IGSYFGASLCSV-DMDRDDSTDLvLIGAPHYYEQTRGGQVSVCPVPGVGSRWQCEATL 236
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
VWA pfam00092
von Willebrand factor type A domain;
2-54 1.94e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.59  E-value: 1.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958654395   2 AEAAGIIRYAIGVGQAFYQaqsrqELKDIASSPSREYVFSVENFDALKDIQNQ 54
Cdd:pfam00092 127 LKSAGVTVFAVGVGNADDE-----ELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
2-59 2.96e-08

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 55.08  E-value: 2.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958654395   2 AEAAGIIRYAIGVGQAfyqaqSRQELKDIASSPSREYVFSVENFDALKDIQNQLKEKI 59
Cdd:cd01475   131 ARALGIEMFAVGVGRA-----DEEELREIASEPLADHVFYVEDFSTIEELTKKFQGKI 183
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
247-282 7.32e-08

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 49.05  E-value: 7.32e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958654395 247 FGAALTVlGDVNGDDLADVAIGAPGE-EESRGAVYIF 282
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
2-52 1.24e-03

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 40.90  E-value: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958654395    2 AEAAGIIRYAIGVGQAFYQAqsrqELKDIASSPSREYVFSVENFDALKDIQ 52
Cdd:smart00327 129 LKRSGVKVFVVGVGNDVDEE----ELKKLASAPGGVYVFLPELLDLLIDLL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
308-332 2.07e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.35  E-value: 2.07e-03
                           10        20
                   ....*....|....*....|....*
gi 1958654395  308 QYFGQSLSGGQDLTGDGLVDLAVGS 332
Cdd:smart00191   3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
5-45 2.27e-03

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 39.90  E-value: 2.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958654395   5 AGIIRYAIGVGQAfyqaqSRQELKDIASSPSREYVFSVENF 45
Cdd:cd01472   129 AGIEVFAVGVKNA-----DEEELKQIASDPKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
5-45 7.74e-03

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 38.04  E-value: 7.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958654395   5 AGIIRYAIGVGQAFYQaqsrqELKDIASSPSREYVFSVENF 45
Cdd:cd01482   129 LGVNVFAVGVKDADES-----ELKMIASKPSETHVFNVADF 164
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
863-877 8.95e-03

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


Pssm-ID: 459778  Cd Length: 15  Bit Score: 34.40  E-value: 8.95e-03
                          10
                  ....*....|....*
gi 1958654395 863 KAGFFKRQYKEMLAE 877
Cdd:pfam00357   1 KCGFFKRNYPPQEEE 15
 
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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