Q64739 · COBA2_MOUSE
- ProteinCollagen alpha-2(XI) chain
- GeneCol11a2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1736 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | collagen trimer | |
Cellular Component | collagen type XI trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular region | |
Molecular Function | extracellular matrix structural constituent | |
Molecular Function | metal ion binding | |
Biological Process | chondrocyte differentiation | |
Biological Process | collagen fibril organization | |
Biological Process | osteoblast differentiation | |
Biological Process | sensory perception of sound | |
Biological Process | skeletal system morphogenesis | |
Biological Process | tissue homeostasis |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-2(XI) chain
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64739
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, propeptide, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MERCSRCHRLLLFLPLVLGLSAAPGWA | ||||||
Chain | PRO_0000005842 | 28-1736 | Collagen alpha-2(XI) chain | |||
Sequence: GAPSVDVLRALRFPSLPDGVRRSKGVCPGDVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHILDDEVFEGDVQELLVVPGVQAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQSQEPQKQPTESLYYDYEPPYYDVMTTGTAPDYQYPTPGEEEGVLESSPLPFLEEEQTDLQVSPTADSFQAEEYGEGGTDSPAGFYDYTYGYGDDYREETELGPALSAETAHSGAVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGEPGMKGDRGFDGLPGLPGEKGQRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGAQGLPGPQGAIGPHGEKGARGKPGLPGMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPTGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGTAGESGPMGERGHSGPPGPPGEQGLPGTSGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDGGPMGPPGPPGPRGPAGPNGADGPQGSPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGESGQAGEAGPPGPKGPTGDNGPKGNPGPVGFPGDPGPPGEAGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGLAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETGIPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSKLIQDEEAVPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPAGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFADLGAPTRRGGVLLGPVCFMG | ||||||
Propeptide | PRO_0000005843 | 1501-1736 | C-terminal propeptide | |||
Sequence: IQPLPIQMPKKTRRSVDGSKLIQDEEAVPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPAGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFADLGAPTRRGGVLLGPVCFMG | ||||||
Disulfide bond | 1571↔1603 | |||||
Sequence: CQDLKLCHPELPDGEYWVDPNQGCARDAFRVFC | ||||||
Disulfide bond | 1577 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1594 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 1604 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1612↔1733 | |||||
Sequence: CVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFADLGAPTRRGGVLLGPVC | ||||||
Disulfide bond | 1655↔1689 | |||||
Sequence: CSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGC |
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II) (By similarity).
Complex viewer
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 57-228 | Laminin G-like | ||||
Sequence: DVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHILDDEVFEGDVQELLVVPGVQAAYQSCGQKDLEC | ||||||
Region | 215-486 | Nonhelical region | ||||
Sequence: QAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQSQEPQKQPTESLYYDYEPPYYDVMTTGTAPDYQYPTPGEEEGVLESSPLPFLEEEQTDLQVSPTADSFQAEEYGEGGTDSPAGFYDYTYGYGDDYREETELGPALSAETAHSGAVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALR | ||||||
Compositional bias | 228-258 | Basic and acidic residues | ||||
Sequence: CEREQRDGPQTQKPHRAQRSPKKEPARLHKP | ||||||
Region | 228-270 | Disordered | ||||
Sequence: CEREQRDGPQTQKPHRAQRSPKKEPARLHKPQSQEPQKQPTES | ||||||
Region | 364-465 | Disordered | ||||
Sequence: LSAETAHSGAVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGP | ||||||
Domain | 399-447 | Collagen-like 1 | ||||
Sequence: GPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPG | ||||||
Region | 485-1538 | Disordered | ||||
Sequence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| ||||||
Domain | 487-545 | Collagen-like 2 | ||||
Sequence: GPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGA | ||||||
Region | 487-1500 | Triple-helical region | ||||
Sequence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| ||||||
Domain | 546-583 | Collagen-like 3 | ||||
Sequence: RGMPGEPGMKGDRGFDGLPGLPGEKGQRGDTGAQGLPG | ||||||
Domain | 682-737 | Collagen-like 4 | ||||
Sequence: GMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGE | ||||||
Compositional bias | 727-744 | Basic and acidic residues | ||||
Sequence: GIRGLKGHKGEKGEDGFP | ||||||
Domain | 868-924 | Collagen-like 5 | ||||
Sequence: GPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPP | ||||||
Compositional bias | 874-900 | Pro residues | ||||
Sequence: GERGLPGPQGPNGFPGPKGPPGPAGKD | ||||||
Domain | 967-1025 | Collagen-like 6 | ||||
Sequence: GDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGS | ||||||
Domain | 1026-1055 | Collagen-like 7 | ||||
Sequence: GGPIGPPGRPGPQGPPGAAGEKGVPGEKGP | ||||||
Domain | 1056-1086 | Collagen-like 8 | ||||
Sequence: IGPTGRDGVQGPVGLPGPAGPPGVAGEDGDK | ||||||
Domain | 1114-1172 | Collagen-like 9 | ||||
Sequence: GPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGD | ||||||
Compositional bias | 1175-1189 | Pro residues | ||||
Sequence: PMGPPGPPGPRGPAG | ||||||
Domain | 1393-1447 | Collagen-like 10 | ||||
Sequence: GPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETG | ||||||
Domain | 1448-1499 | Collagen-like 11 | ||||
Sequence: IPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGE | ||||||
Domain | 1541-1735 | Fibrillar collagen NC1 | ||||
Sequence: EEIFGSLDSLREEIEQMRRPAGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFADLGAPTRRGGVLLGPVCFM |
Domain
The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).
Sequence similarities
Belongs to the fibrillar collagen family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 7 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q64739-2
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsE56789
- Length1,736
- Mass (Da)171,535
- Last updated2003-04-30 v3
- Checksum18D792D4A3387C61
Q64739-3
- Name2
- SynonymsE5689
- Differences from canonical
- 293-313: Missing
Q64739-4
- Name3
- SynonymsE5789
- Differences from canonical
- 267-292: Missing
Q64739-5
- Name4
- SynonymsE569
Q64739-6
- Name5
- SynonymsE589
Q64739-7
- Name6
- SynonymsE59
Q64739-1
- Name7
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 228-258 | Basic and acidic residues | ||||
Sequence: CEREQRDGPQTQKPHRAQRSPKKEPARLHKP | ||||||
Alternative sequence | VSP_007345 | 267-292 | in isoform 3, isoform 5, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_007346 | 293-313 | in isoform 2, isoform 4, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_007347 | 314-373 | in isoform 4, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 536 | in Ref. 2; AAA67751 | ||||
Sequence: R → L | ||||||
Sequence conflict | 621 | in Ref. 3; BAA18910 | ||||
Sequence: P → S | ||||||
Sequence conflict | 704-705 | in Ref. 2; AAA67751 | ||||
Sequence: NQ → KP | ||||||
Compositional bias | 727-744 | Basic and acidic residues | ||||
Sequence: GIRGLKGHKGEKGEDGFP | ||||||
Sequence conflict | 797 | in Ref. 2; AAA67751 | ||||
Sequence: V → A | ||||||
Sequence conflict | 843-845 | in Ref. 2; AAA67751 | ||||
Sequence: TGP → HGS | ||||||
Sequence conflict | 854 | in Ref. 2; AAA67751 | ||||
Sequence: A → S | ||||||
Compositional bias | 874-900 | Pro residues | ||||
Sequence: GERGLPGPQGPNGFPGPKGPPGPAGKD | ||||||
Sequence conflict | 876 | in Ref. 2; AAA67751 | ||||
Sequence: R → G | ||||||
Sequence conflict | 889 | in Ref. 2; AAA67751 | ||||
Sequence: G → V | ||||||
Sequence conflict | 922 | in Ref. 2; AAA67751 | ||||
Sequence: G → D | ||||||
Sequence conflict | 1005 | in Ref. 2; AAA67751 | ||||
Sequence: E → V | ||||||
Compositional bias | 1175-1189 | Pro residues | ||||
Sequence: PMGPPGPPGPRGPAG | ||||||
Sequence conflict | 1253 | in Ref. 2; AAA67751 | ||||
Sequence: P → S | ||||||
Sequence conflict | 1386 | in Ref. 2; AAA67751 | ||||
Sequence: A → T | ||||||
Sequence conflict | 1522 | in Ref. 2; AAA67751 | ||||
Sequence: I → M |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF100956 EMBL· GenBank· DDBJ | AAC69905.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U16789 EMBL· GenBank· DDBJ | AAA67751.1 EMBL· GenBank· DDBJ | mRNA | ||
U16790 EMBL· GenBank· DDBJ | AAA67752.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D38412 EMBL· GenBank· DDBJ | BAA18910.1 EMBL· GenBank· DDBJ | mRNA | ||
D84066 EMBL· GenBank· DDBJ | BAA12208.1 EMBL· GenBank· DDBJ | Genomic DNA |