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Conserved domains on  [gi|1846398813|ref|NP_001371034|]
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von Willebrand factor A domain-containing protein 5B2 isoform 4 [Mus musculus]

Protein Classification

VWA domain-containing protein( domain architecture ID 10618621)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 7.04e-32

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


:

Pssm-ID: 404621  Cd Length: 78  Bit Score: 119.11  E-value: 7.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1846398813    2 PGLYCPTSWTPLPLTDSCVRAYAKGPCLSLRARLTYHNPQPQPVEGVFVYPLAEAEVVSGFEAEAAGRRVSFQLHSRR 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 354-501 1.42e-29

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 pfam13768:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 155  Bit Score: 115.57  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  354 ELLFLLDGSGAGH------KDAIVLAVKSLPAQTLVNLAIFGTLVQPLFPESRPCSDDTVQLICESIETLQTVNGPPDML 427
Cdd:pfam13768    2 DVVIVVDVSSSMSgepklqKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1846398813  428 AVLDWALGQPQHRAYPRQMFLItAASPTAATTHQALEFMRWHRGAARCFSFALAP-ACRQLLHDLSVLSRGQAYF 501
Cdd:pfam13768   82 GALKEAVRAPASPGYIRHVLLL-TDGSPMQGETRVSDLISRAPGKIRFFAYGLGAsISAPMLQLLAEASNGTYEF 155
 
Name Accession Description Interval E-value
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 7.04e-32

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 404621  Cd Length: 78  Bit Score: 119.11  E-value: 7.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1846398813    2 PGLYCPTSWTPLPLTDSCVRAYAKGPCLSLRARLTYHNPQPQPVEGVFVYPLAEAEVVSGFEAEAAGRRVSFQLHSRR 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
354-501 1.42e-29

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 115.57  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  354 ELLFLLDGSGAGH------KDAIVLAVKSLPAQTLVNLAIFGTLVQPLFPESRPCSDDTVQLICESIETLQTVNGPPDML 427
Cdd:pfam13768    2 DVVIVVDVSSSMSgepklqKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1846398813  428 AVLDWALGQPQHRAYPRQMFLItAASPTAATTHQALEFMRWHRGAARCFSFALAP-ACRQLLHDLSVLSRGQAYF 501
Cdd:pfam13768   82 GALKEAVRAPASPGYIRHVLLL-TDGSPMQGETRVSDLISRAPGKIRFFAYGLGAsISAPMLQLLAEASNGTYEF 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 353-514 4.06e-14

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 71.48  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  353 RELLFLLDGSG--AGH-----KDAIVLAVKSLPAQTLVNLAIFGTLVQPLFPESRPCSDDTVQLICESIETLQtVNGPPD 425
Cdd:cd01461      3 KEVVFVIDTSGsmSGTkieqtKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQ-ALGGTN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  426 MLAVLDWALGQPQHRA-YPRQMFLItaASPTAATTHQALEFMRWH-RGAARCFSFALAPAC-RQLLHDLSVLSRGQAYFL 502
Cdd:cd01461     82 MNDALEAALELLNSSPgSVPQIILL--TDGEVTNESQILKNVREAlSGRIRLFTFGIGSDVnTYLLERLAREGRGIARRI 159

                          170
                   ....*....|..
gi 1846398813  503 RPGERLQPKLVQ 514
Cdd:cd01461    160 YETDDIESQLLR 171
 
Name Accession Description Interval E-value
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 7.04e-32

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 404621  Cd Length: 78  Bit Score: 119.11  E-value: 7.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1846398813    2 PGLYCPTSWTPLPLTDSCVRAYAKGPCLSLRARLTYHNPQPQPVEGVFVYPLAEAEVVSGFEAEAAGRRVSFQLHSRR 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
354-501 1.42e-29

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 115.57  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  354 ELLFLLDGSGAGH------KDAIVLAVKSLPAQTLVNLAIFGTLVQPLFPESRPCSDDTVQLICESIETLQTVNGPPDML 427
Cdd:pfam13768    2 DVVIVVDVSSSMSgepklqKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1846398813  428 AVLDWALGQPQHRAYPRQMFLItAASPTAATTHQALEFMRWHRGAARCFSFALAP-ACRQLLHDLSVLSRGQAYF 501
Cdd:pfam13768   82 GALKEAVRAPASPGYIRHVLLL-TDGSPMQGETRVSDLISRAPGKIRFFAYGLGAsISAPMLQLLAEASNGTYEF 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 353-514 4.06e-14

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 71.48  E-value: 4.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  353 RELLFLLDGSG--AGH-----KDAIVLAVKSLPAQTLVNLAIFGTLVQPLFPESRPCSDDTVQLICESIETLQtVNGPPD 425
Cdd:cd01461      3 KEVVFVIDTSGsmSGTkieqtKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQ-ALGGTN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846398813  426 MLAVLDWALGQPQHRA-YPRQMFLItaASPTAATTHQALEFMRWH-RGAARCFSFALAPAC-RQLLHDLSVLSRGQAYFL 502
Cdd:cd01461     82 MNDALEAALELLNSSPgSVPQIILL--TDGEVTNESQILKNVREAlSGRIRLFTFGIGSDVnTYLLERLAREGRGIARRI 159

                          170
                   ....*....|..
gi 1846398813  503 RPGERLQPKLVQ 514
Cdd:cd01461    160 YETDDIESQLLR 171
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 36-71 7.20e-05

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 43.24  E-value: 7.20e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1846398813   36 TYHNPQPQPVEGVFVYPLAEAEVVSGFEAEAAGRRV 71
Cdd:pfam08487   22 TFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVI 57
 
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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