Q64739 · COBA2_MOUSE

  • Protein
    Collagen alpha-2(XI) chain
  • Gene
    Col11a2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

Features

Showing features for binding site.

117362004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Binding site1589Ca2+ (UniProtKB | ChEBI)
Binding site1591Ca2+ (UniProtKB | ChEBI)
Binding site1592Ca2+ (UniProtKB | ChEBI)
Binding site1594Ca2+ (UniProtKB | ChEBI)
Binding site1597Ca2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen trimer
Cellular Componentcollagen type XI trimer
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular region
Molecular Functionextracellular matrix structural constituent
Molecular Functionmetal ion binding
Biological Processchondrocyte differentiation
Biological Processcollagen fibril organization
Biological Processosteoblast differentiation
Biological Processsensory perception of sound
Biological Processskeletal system morphogenesis
Biological Processtissue homeostasis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Collagen alpha-2(XI) chain

Gene names

    • Name
      Col11a2

Organism names

  • Taxonomic identifier
  • Strains
    • 129/SvJ
    • 129/Sv
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q64739
  • Secondary accessions
    • Q61432
    • Q9Z1W0

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for signal, chain, propeptide, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000000584228-1736Collagen alpha-2(XI) chain
PropeptidePRO_00000058431501-1736C-terminal propeptide
Disulfide bond1571↔1603
Disulfide bond1577Interchain
Disulfide bond1594Interchain
Glycosylation1604N-linked (GlcNAc...) asparagine
Disulfide bond1612↔1733
Disulfide bond1655↔1689

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

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

View interactors in UniProtKB
View CPX-2975 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain57-228Laminin G-like
Region215-486Nonhelical region
Compositional bias228-258Basic and acidic residues
Region228-270Disordered
Region364-465Disordered
Domain399-447Collagen-like 1
Region485-1538Disordered
Domain487-545Collagen-like 2
Region487-1500Triple-helical region
Domain546-583Collagen-like 3
Domain682-737Collagen-like 4
Compositional bias727-744Basic and acidic residues
Domain868-924Collagen-like 5
Compositional bias874-900Pro residues
Domain967-1025Collagen-like 6
Domain1026-1055Collagen-like 7
Domain1056-1086Collagen-like 8
Domain1114-1172Collagen-like 9
Compositional bias1175-1189Pro residues
Domain1393-1447Collagen-like 10
Domain1448-1499Collagen-like 11
Domain1541-1735Fibrillar collagen NC1

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

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (7)
  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Name
    1
  • Synonyms
    E56789
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,736
  • Mass (Da)
    171,535
  • Last updated
    2003-04-30 v3
  • Checksum
    18D792D4A3387C61
MERCSRCHRLLLFLPLVLGLSAAPGWAGAPSVDVLRALRFPSLPDGVRRSKGVCPGDVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHILDDEVFEGDVQELLVVPGVQAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQSQEPQKQPTESLYYDYEPPYYDVMTTGTAPDYQYPTPGEEEGVLESSPLPFLEEEQTDLQVSPTADSFQAEEYGEGGTDSPAGFYDYTYGYGDDYREETELGPALSAETAHSGAVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGEPGMKGDRGFDGLPGLPGEKGQRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGAQGLPGPQGAIGPHGEKGARGKPGLPGMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPTGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGTAGESGPMGERGHSGPPGPPGEQGLPGTSGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDGGPMGPPGPPGPRGPAGPNGADGPQGSPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGESGQAGEAGPPGPKGPTGDNGPKGNPGPVGFPGDPGPPGEAGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGLAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETGIPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSKLIQDEEAVPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPAGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFADLGAPTRRGGVLLGPVCFMG

Q64739-3

  • Name
    2
  • Synonyms
    E5689
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q64739-4

  • Name
    3
  • Synonyms
    E5789
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q64739-5

  • Name
    4
  • Synonyms
    E569
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q64739-6

  • Name
    5
  • Synonyms
    E589
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q64739-7

Q64739-1

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias228-258Basic and acidic residues
Alternative sequenceVSP_007345267-292in isoform 3, isoform 5, isoform 6 and isoform 7
Alternative sequenceVSP_007346293-313in isoform 2, isoform 4, isoform 5 and isoform 6
Alternative sequenceVSP_007347314-373in isoform 4, isoform 6 and isoform 7
Sequence conflict536in Ref. 2; AAA67751
Sequence conflict621in Ref. 3; BAA18910
Sequence conflict704-705in Ref. 2; AAA67751
Compositional bias727-744Basic and acidic residues
Sequence conflict797in Ref. 2; AAA67751
Sequence conflict843-845in Ref. 2; AAA67751
Sequence conflict854in Ref. 2; AAA67751
Compositional bias874-900Pro residues
Sequence conflict876in Ref. 2; AAA67751
Sequence conflict889in Ref. 2; AAA67751
Sequence conflict922in Ref. 2; AAA67751
Sequence conflict1005in Ref. 2; AAA67751
Compositional bias1175-1189Pro residues
Sequence conflict1253in Ref. 2; AAA67751
Sequence conflict1386in Ref. 2; AAA67751
Sequence conflict1522in Ref. 2; AAA67751

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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