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P02460

- CO2A1_CHICK

UniProt

P02460 - CO2A1_CHICK

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Protein

Collagen alpha-1(II) chain

Gene

COL2A1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei123 – 1242Cleavage; by procollagen C-endopeptidase
Metal bindingi183 – 1831CalciumBy similarity
Metal bindingi185 – 1851CalciumBy similarity
Metal bindingi186 – 1861Calcium; via carbonyl oxygenBy similarity
Metal bindingi188 – 1881Calcium; via carbonyl oxygenBy similarity
Metal bindingi191 – 1911CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cartilage condensation Source: Ensembl
  2. cartilage development involved in endochondral bone morphogenesis Source: Ensembl
  3. cellular response to BMP stimulus Source: Ensembl
  4. central nervous system development Source: Ensembl
  5. chondrocyte differentiation Source: Ensembl
  6. collagen fibril organization Source: Ensembl
  7. embryonic skeletal joint morphogenesis Source: Ensembl
  8. endochondral ossification Source: Ensembl
  9. heart morphogenesis Source: Ensembl
  10. inner ear morphogenesis Source: Ensembl
  11. limb bud formation Source: Ensembl
  12. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  13. notochord development Source: Ensembl
  14. otic vesicle development Source: Ensembl
  15. palate development Source: Ensembl
  16. proteoglycan metabolic process Source: Ensembl
  17. regulation of gene expression Source: Ensembl
  18. sensory perception of sound Source: Ensembl
  19. tissue homeostasis Source: Ensembl
  20. visual perception Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196873. Extracellular matrix organization.
REACT_197163. Assembly of collagen fibrils and other multimeric structures.
REACT_197191. Collagen degradation.
REACT_198057. Non-integrin membrane-ECM interactions.
REACT_198079. ECM proteoglycans.
REACT_198187. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Gene namesi
Name:COL2A1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. collagen type II trimer Source: Ensembl
  3. cytoplasm Source: Ensembl
  4. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 123›123Collagen alpha-1(II) chainPRO_0000005727Add
BLAST
Propeptidei124 – 369246C-terminal propeptidePRO_0000005728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi165 ↔ 197PROSITE-ProRule annotation
Disulfide bondi171 – 171Interchain (with C-188)PROSITE-ProRule annotation
Disulfide bondi188 – 188Interchain (with C-171)PROSITE-ProRule annotation
Disulfide bondi205 ↔ 367PROSITE-ProRule annotation
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi275 ↔ 320PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP02460.

Miscellaneous databases

PMAP-CutDBP02460.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

Protein-protein interaction databases

IntActiP02460. 1 interaction.
STRINGi9031.ENSGALP00000035064.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 369235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni‹1 – 96›96Triple-helical regionAdd
BLAST
Regioni97 – 12327Nonhelical region (C-terminal)Add
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG103137.
InParanoidiP02460.
PhylomeDBiP02460.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 2 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
GETGEAGERG LKGHRGFTGL QGLPGPPGPS GDQGAAGPAG PSGPRGPPGP
60 70 80 90 100
VGPSGKDGSN GMPGPIGPPG PRGRSGEPGP AGPPGNPGPP GPPGPPGTGI
110 120 130 140 150
DMSAFAGLGQ TEKGPDPIRY MRADEAAGGL RQHDVEVDAT LKSLNNQIES
160 170 180 190 200
IRSPEGSKKN PARTCRDIKL CHPEWKSGDY WIDPNQGCTL DAIKVFCNME
210 220 230 240 250
TGETCVYPTP SSIPRKNWWT SKTKDKKHVW FAETINGGFH FSYGDENLSP
260 270 280 290 300
NTASIQMTFL RLLSTEGSQN VTYHCKNSIA YMDEETGNLK KAILIQGSND
310 320 330 340 350
VEIRAEGNSR FTYSVLEDGC TKHTGKWGKT VIEYRSQKTS RLPIVDIAPM
360
DIGGADQEFG VDIGPVCFL
Length:369
Mass (Da):38,990
Last modified:November 1, 1988 - v1
Checksum:iEF5306925B0BA3B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02663 mRNA. Translation: CAA26499.1.
L00063, L00061, L00062 Genomic DNA. Translation: AAB59967.1.
PIRiA02860. CGCH6C.
S07133.
UniGeneiGga.2839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02663 mRNA. Translation: CAA26499.1 .
L00063 , L00061 , L00062 Genomic DNA. Translation: AAB59967.1 .
PIRi A02860. CGCH6C.
S07133.
UniGenei Gga.2839.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P02460. 1 interaction.
STRINGi 9031.ENSGALP00000035064.

Proteomic databases

PaxDbi P02460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085654.
HOVERGENi HBG103137.
InParanoidi P02460.
PhylomeDBi P02460.

Enzyme and pathway databases

Reactomei REACT_196873. Extracellular matrix organization.
REACT_197163. Assembly of collagen fibrils and other multimeric structures.
REACT_197191. Collagen degradation.
REACT_198057. Non-integrin membrane-ECM interactions.
REACT_198079. ECM proteoglycans.
REACT_198187. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

PMAP-CutDB P02460.
PROi P02460.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 2 hits.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCO2A1_CHICK
AccessioniPrimary (citable) accession number: P02460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: October 1, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3