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P02460 (CO2A1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Gene names
Name:COL2A1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length369 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.

Subunit structure

Homotrimers of alpha 1(II) chains.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

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.

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.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainCollagen
Repeat
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage condensation

Inferred from electronic annotation. Source: Ensembl

cartilage development involved in endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to BMP stimulus

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from electronic annotation. Source: Ensembl

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal joint morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

limb bud formation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

notochord development

Inferred from electronic annotation. Source: Ensembl

otic vesicle development

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

proteoglycan metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

collagen type II trimer

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 123›123Collagen alpha-1(II) chain
PRO_0000005727
Propeptide124 – 369246C-terminal propeptide
PRO_0000005728

Regions

Domain135 – 369235Fibrillar collagen NC1
Region‹1 – 96›96Triple-helical region
Region97 – 12327Nonhelical region (C-terminal)

Sites

Metal binding1831Calcium By similarity
Metal binding1851Calcium By similarity
Metal binding1861Calcium; via carbonyl oxygen By similarity
Metal binding1881Calcium; via carbonyl oxygen By similarity
Metal binding1911Calcium By similarity
Site123 – 1242Cleavage; by procollagen C-endopeptidase

Amino acid modifications

Glycosylation2701N-linked (GlcNAc...) Potential
Disulfide bond165 ↔ 197 By similarity
Disulfide bond171Interchain (with C-188) By similarity
Disulfide bond188Interchain (with C-171) By similarity
Disulfide bond205 ↔ 367 By similarity
Disulfide bond275 ↔ 320 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P02460 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: EF5306925B0BA3B0

FASTA36938,990
        10         20         30         40         50         60 
GETGEAGERG LKGHRGFTGL QGLPGPPGPS GDQGAAGPAG PSGPRGPPGP VGPSGKDGSN 

        70         80         90        100        110        120 
GMPGPIGPPG PRGRSGEPGP AGPPGNPGPP GPPGPPGTGI DMSAFAGLGQ TEKGPDPIRY 

       130        140        150        160        170        180 
MRADEAAGGL RQHDVEVDAT LKSLNNQIES IRSPEGSKKN PARTCRDIKL CHPEWKSGDY 

       190        200        210        220        230        240 
WIDPNQGCTL DAIKVFCNME TGETCVYPTP SSIPRKNWWT SKTKDKKHVW FAETINGGFH 

       250        260        270        280        290        300 
FSYGDENLSP NTASIQMTFL RLLSTEGSQN VTYHCKNSIA YMDEETGNLK KAILIQGSND 

       310        320        330        340        350        360 
VEIRAEGNSR FTYSVLEDGC TKHTGKWGKT VIEYRSQKTS RLPIVDIAPM DIGGADQEFG 


VDIGPVCFL 

« Hide

References

[1]"Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis."
Deak F., Argraves W.S., Kiss I., Sparks K.J., Goetinck P.F.
Biochem. J. 229:189-196(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-193.
[2]"Structure and sequence of the chicken type II procollagen gene. Characterization of the region encoding the carboxyl-terminal telopeptide and propeptide."
Sandell L.J., Prentice H.L., Kravis D., Upholt W.B.
J. Biol. Chem. 259:7826-7834(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-369.
[3]"Structure of the carboxyl propeptide of chicken type II procollagen determined by DNA and protein sequence analysis."
Ninomiya Y., Showalter A.M., van der Rest M., Seidah N.G., Chretien M., Olsen B.R.
Biochemistry 23:617-624(1984)
Cited for: NUCLEOTIDE SEQUENCE OF 114-369.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02663 mRNA. Translation: CAA26499.1.
L00063, L00061, L00062 Genomic DNA. Translation: AAB59967.1.
PIRCGCH6C. A02860.
S07133.
UniGeneGga.2839.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02460. 1 interaction.
STRING9031.ENSGALP00000035064.

Proteomic databases

PaxDbP02460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085654.
HOVERGENHBG103137.
InParanoidP02460.
PhylomeDBP02460.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 2 hits.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP02460.
PROP02460.

Entry information

Entry nameCO2A1_CHICK
AccessionPrimary (citable) accession number: P02460
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families