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Protein

Collagen alpha-1(II) chain

Gene

COL2A1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_272039. Integrin cell surface interactions.
REACT_291360. Extracellular matrix organization.
REACT_311308. Collagen biosynthesis and modifying enzymes.
REACT_325682. Signaling by PDGF.
REACT_338317. Assembly of collagen fibrils and other multimeric structures.
REACT_343968. ECM proteoglycans.
REACT_346737. Non-integrin membrane-ECM interactions.
REACT_347678. NCAM1 interactions.
REACT_349136. Collagen degradation.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X02663 mRNA. Translation: CAA26499.1.
L00063, L00061, L00062 Genomic DNA. Translation: AAB59967.1.
PIRiA02860. CGCH6C.
S07133.
UniGeneiGga.2839.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02460. 1 interaction.
STRINGi9031.ENSGALP00000035064.

Proteomic databases

PaxDbiP02460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG103137.
InParanoidiP02460.
PhylomeDBiP02460.

Enzyme and pathway databases

ReactomeiREACT_272039. Integrin cell surface interactions.
REACT_291360. Extracellular matrix organization.
REACT_311308. Collagen biosynthesis and modifying enzymes.
REACT_325682. Signaling by PDGF.
REACT_338317. Assembly of collagen fibrils and other multimeric structures.
REACT_343968. ECM proteoglycans.
REACT_346737. Non-integrin membrane-ECM interactions.
REACT_347678. NCAM1 interactions.
REACT_349136. Collagen degradation.

Miscellaneous databases

PMAP-CutDBP02460.
PROiP02460.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.