A2AX52 (CO6A4_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 39.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Collagen alpha-4(VI) chain | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 2309 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Collagen VI acts as a cell-binding protein By similarity. |
| Subunit structure | Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). Ref.2 |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Tissue specificity | In newborn, it is expressed in lung, kidney, brain, intestine, skin, sternum and, at weak level, calvaria. In adult, it is almost absent with some weak expression in ovary and very weak expression in spleen, lung, uterus and brain. Ref.2 |
| Post-translational modification | Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains By similarity. |
| Sequence similarities | Belongs to the type VI collagen family. Contains 8 VWFA domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Extracellular matrix Secreted |
| Domain | Collagen Repeat Signal |
| PTM | Glycoprotein Hydroxylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW protein heterotrimerizationInferred from direct assay. Source: MGI |
| Cellular component | collagen Inferred from electronic annotation. Source: UniProtKB-KW protein complexInferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||
| Chain | 23 – 2309 | 2287 | Collagen alpha-4(VI) chain | PRO_5000214197 | |||||
Regions | |||||||||
| Domain | 34 – 206 | 173 | VWFA 1 | ||||||
| Domain | 235 – 413 | 179 | VWFA 2 | ||||||
| Domain | 430 – 653 | 224 | VWFA 3 | ||||||
| Domain | 634 – 811 | 178 | VWFA 4 | ||||||
| Domain | 849 – 1018 | 170 | VWFA 5 | ||||||
| Domain | 1030 – 1199 | 170 | VWFA 6 | ||||||
| Domain | 1776 – 1957 | 182 | VWFA 7 | ||||||
| Domain | 1982 – 2187 | 206 | VWFA 8 | ||||||
| Region | 21 – 1410 | 1390 | Nonhelical region | ||||||
| Region | 1411 – 1744 | 334 | Triple-helical region | ||||||
| Region | 1745 – 2309 | 565 | Nonhelical region | ||||||
| Motif | 1527 – 1529 | 3 | Cell attachment site Potential | ||||||
| Motif | 2208 – 2210 | 3 | Cell attachment site Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 188 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 754 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1114 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 77 | 1 | S → G in BAF95091. Ref.1 | ||||||
| Sequence conflict | 147 | 1 | T → A in BAF95091. Ref.1 | ||||||
| Sequence conflict | 215 | 1 | G → A in BAF95091. Ref.1 | ||||||
| Sequence conflict | 223 | 1 | R → Q in BAF95091. Ref.1 | ||||||
| Sequence conflict | 263 | 1 | S → L in BAF95091. Ref.1 | ||||||
| Sequence conflict | 386 | 1 | N → S in BAF95091. Ref.1 | ||||||
| Sequence conflict | 425 | 1 | T → N in BAF95091. Ref.1 | ||||||
| Sequence conflict | 443 | 1 | Q → P in BAF95091. Ref.1 | ||||||
| Sequence conflict | 468 | 1 | Q → R in BAF95091. Ref.1 | ||||||
| Sequence conflict | 646 | 1 | R → G in BAF95091. Ref.1 | ||||||
| Sequence conflict | 699 | 1 | R → S in BAF95091. Ref.1 | ||||||
| Sequence conflict | 707 | 1 | R → Q in BAF95091. Ref.1 | ||||||
| Sequence conflict | 713 | 1 | A → T in BAF95091. Ref.1 | ||||||
| Sequence conflict | 747 | 1 | I → M in BAF95091. Ref.1 | ||||||
| Sequence conflict | 774 | 1 | T → I in BAF95091. Ref.1 | ||||||
| Sequence conflict | 822 | 1 | G → R in BAF95091. Ref.1 | ||||||
| Sequence conflict | 922 | 1 | V → E in BAF95091. Ref.1 | ||||||
| Sequence conflict | 945 | 1 | I → V in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1079 | 1 | Q → R in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1281 – 1283 | 3 | DET → NEI in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1353 – 1354 | 2 | IG → VS in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1434 | 1 | P → L in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1629 | 1 | L → P in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1703 | 1 | R → H in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1775 | 1 | T → M in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1780 | 1 | T → A in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1788 | 1 | A → S in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1809 | 1 | C → S in BAF95091. Ref.1 | ||||||
| Sequence conflict | 1978 | 1 | K → D in BAF95091. Ref.1 | ||||||
| Sequence conflict | 2222 | 1 | F → L in BAF95091. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of osteoarthritis-associated gene DVWA." Nakajima M., Miyamoto Y., Ikegawa S. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Three novel collagen VI chains with high homology to the alpha 3 chain." Gara S.K., Grumati P., Urciuolo A., Bonaldo P., Kobbe B., Koch M., Paulsson M., Wagener R. J. Biol. Chem. 283:10658-10670(2008) [PubMed: 18276594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY. Strain: C57BL/6J. Tissue: Brain and Uterus. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB370265 mRNA. Translation: BAF95091.1. AM231151 mRNA. Translation: CAJ77150.1. AM231152 mRNA. Translation: CAJ77151.1. AM231153 mRNA. Translation: CAJ77152.1. AC120386 Genomic DNA. No translation available. |
| IPI | IPI00828867. |
| RefSeq | NP_081039.2. NM_026763.2. |
| UniGene | Mm.28854. |
3D structure databases | |
| ProteinModelPortal | A2AX52. |
| SMR | A2AX52. Positions 32-212, 225-583, 631-819, 837-1205, 1420-1454, 1681-1714. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A2AX52. |
PTM databases | |
| PhosphoSite | A2AX52. |
Proteomic databases | |
| PRIDE | A2AX52. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000121963; ENSMUSP00000112472; ENSMUSG00000032572. |
| GeneID | 68553. |
| KEGG | mmu:68553. |
| UCSC | uc012gzq.1. mouse. |
Organism-specific databases | |
| CTD | 68553. |
| MGI | MGI:1915803. Col6a4. |
Phylogenomic databases | |
| HOGENOM | HBG444500. |
| HOVERGEN | HBG107742. |
| InParanoid | A2AX52. |
| OrthoDB | EOG476JZ9. |
Gene expression databases | |
| Bgee | A2AX52. |
| Genevestigator | A2AX52. |
Family and domain databases | |
| InterPro | IPR008160. Collagen. IPR002035. VWF_A. [Graphical view] |
| KO | K06238. |
| Pfam | PF01391. Collagen. 2 hits. PF00092. VWA. 7 hits. [Graphical view] |
| SMART | SM00327. VWA. 9 hits. [Graphical view] |
| PROSITE | PS50234. VWFA. 8 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 327440. |
| SOURCE | Search... |
Entry information
| Entry name | CO6A4_MOUSE | ||||||||
| Accession | Primary (citable) accession number: A2AX52 Secondary accession number(s): A2AX53, A2AX54, A9CR35 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with