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Protein

Collagen alpha-1(II) chain

Gene

COL2A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Metal bindingi1301CalciumBy similarity1
Metal bindingi1303CalciumBy similarity1
Metal bindingi1304Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1306Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1309CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-1442490. Collagen degradation.
R-BTA-1474244. Extracellular matrix organization.
R-BTA-1650814. Collagen biosynthesis and modifying enzymes.
R-BTA-186797. Signaling by PDGF.
R-BTA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-BTA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-BTA-216083. Integrin cell surface interactions.
R-BTA-3000171. Non-integrin membrane-ECM interactions.
R-BTA-3000178. ECM proteoglycans.
R-BTA-419037. NCAM1 interactions.
R-BTA-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Gene namesi
Name:COL2A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
PropeptideiPRO_000040121026 – 181N-terminal propeptideBy similarityAdd BLAST156
ChainiPRO_0000005725182 – 1487Collagen alpha-1(II) chainAdd BLAST1306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1905-hydroxylysineBy similarity1
Glycosylationi190O-linked (Gal...)By similarity1
Modified residuei212Hydroxyproline1 Publication1
Modified residuei218Hydroxyproline1 Publication1
Modified residuei230Hydroxyproline1 Publication1
Modified residuei233Hydroxyproline1 Publication1
Modified residuei245Hydroxyproline1 Publication1
Modified residuei248Hydroxyproline1 Publication1
Modified residuei251Hydroxyproline1 Publication1
Modified residuei260Hydroxyproline1 Publication1
Modified residuei269Hydroxyproline1 Publication1
Modified residuei278Hydroxyproline1 Publication1
Modified residuei281Hydroxyproline1 Publication1
Modified residuei284Hydroxyproline1 Publication1
Modified residuei2875-hydroxylysine1 Publication1
Glycosylationi287O-linked (Gal...)1 Publication1
Modified residuei293Hydroxyproline1 Publication1
Modified residuei2995-hydroxylysine1 Publication1
Glycosylationi299O-linked (Gal...)1 Publication1
Modified residuei305Hydroxyproline1 Publication1
Modified residuei3085-hydroxylysine1 Publication1
Glycosylationi308O-linked (Gal...)1 Publication1
Modified residuei314Hydroxyproline1 Publication1
Modified residuei320Hydroxyproline1 Publication1
Modified residuei329Hydroxyproline2 Publications1
Modified residuei350Hydroxyproline3 Publications1
Modified residuei356Hydroxyproline3 Publications1
Modified residuei365Hydroxyproline1 Publication1
Modified residuei368Hydroxyproline1 Publication1
Modified residuei371Hydroxyproline1 Publication1
Modified residuei3745-hydroxylysine1 Publication1
Glycosylationi374O-linked (Gal...)By similarity1
Modified residuei395Hydroxyproline1 Publication1
Modified residuei398Hydroxyproline1 Publication1
Modified residuei401Hydroxyproline1 Publication1
Modified residuei410Hydroxyproline1 Publication1
Modified residuei416Hydroxyproline1 Publication1
Modified residuei4195-hydroxylysine1 Publication1
Modified residuei425Hydroxyproline1 Publication1
Modified residuei431Hydroxyproline1 Publication1
Modified residuei434Hydroxyproline1 Publication1
Modified residuei440Hydroxyproline1 Publication1
Modified residuei4525-hydroxylysine1 Publication1
Modified residuei458Hydroxyproline1 Publication1
Modified residuei4645-hydroxylysine1 Publication1
Modified residuei4705-hydroxylysine1 Publication1
Modified residuei473Hydroxyproline1 Publication1
Modified residuei482Hydroxyproline1 Publication1
Modified residuei497Hydroxyproline1 Publication1
Modified residuei506Hydroxyproline1 Publication1
Modified residuei512Hydroxyproline1 Publication1
Modified residuei518Hydroxyproline1 Publication1
Modified residuei5275-hydroxylysine1 Publication1
Modified residuei530Hydroxyproline1 Publication1
Modified residuei5425-hydroxylysine1 Publication1
Modified residuei551Hydroxyproline1 Publication1
Modified residuei557Hydroxyproline1 Publication1
Modified residuei566Hydroxyproline1 Publication1
Modified residuei581Hydroxyproline1 Publication1
Modified residuei587Hydroxyproline1 Publication1
Modified residuei590Hydroxyproline1 Publication1
Modified residuei599Hydroxyproline1 Publication1
Modified residuei605Hydroxyproline1 Publication1
Modified residuei6085-hydroxylysine1 Publication1
Glycosylationi608O-linked (Gal...)1 Publication1
Modified residuei614Hydroxyproline1 Publication1
Modified residuei6205-hydroxylysine1 Publication1
Glycosylationi620O-linked (Gal...)1 Publication1
Modified residuei623Hydroxyproline1 Publication1
Modified residuei626Hydroxyproline1 Publication1
Modified residuei632Hydroxyproline1 Publication1
Modified residuei644Hydroxyproline1 Publication1
Modified residuei659Hydroxyproline1 Publication1
Modified residuei668Hydroxyproline1 Publication1
Modified residuei6703-hydroxyprolineBy similarity1
Modified residuei671Hydroxyproline1 Publication1
Modified residuei674Hydroxyproline1 Publication1
Modified residuei9073-hydroxyprolineBy similarity1
Modified residuei11305-hydroxylysineBy similarity1
Glycosylationi1130O-linked (Gal...)By similarity1
Modified residuei11443-hydroxyprolineBy similarity1
Modified residuei11863-hydroxyprolineBy similarity1
Modified residuei12013-hydroxyprolineBy similarity1
Modified residuei12073-hydroxyprolineBy similarity1
Modified residuei12133-hydroxyprolineBy similarity1
Disulfide bondi1283 ↔ 1315PROSITE-ProRule annotation
Disulfide bondi1289Interchain (with C-1306)PROSITE-ProRule annotation
Disulfide bondi1306Interchain (with C-1289)PROSITE-ProRule annotation
Disulfide bondi1323 ↔ 1485PROSITE-ProRule annotation
Glycosylationi1388N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1393 ↔ 1438PROSITE-ProRule annotation

Post-translational modificationi

Probably 3-hydroxylated on prolines by LEPREL1 (By similarity). Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.By similarity4 Publications
O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei181 – 182Cleavage; by procollagen N-endopeptidaseBy similarity2
Sitei1241 – 1242Cleavage; by procollagen C-endopeptidaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP02459.
PRIDEiP02459.

Miscellaneous databases

PMAP-CutDBP02459.

Expressioni

Gene expression databases

BgeeiENSBTAG00000013155.
ExpressionAtlasiP02459. differential.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

Protein-protein interaction databases

IntActiP02459. 1 interactor.
STRINGi9913.ENSBTAP00000017505.

Structurei

3D structure databases

ProteinModelPortaliP02459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 90VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1253 – 1487Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 1214Triple-helical regionBy similarityAdd BLAST1014
Regioni1215 – 1241Nonhelical region (C-terminal)By similarityAdd BLAST27

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
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02459.
KOiK19719.
OMAiKDCLNPE.
OrthoDBiEOG091G03LV.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRLGAPQTL VLLTLLVAAV LRCHGQDVQK AGSCVQDGQR YNDKDVWKPE
60 70 80 90 100
PCRICVCDTG TVLCDDIICE DMKDCLSPET PFGECCPICS ADLPTASGQP
110 120 130 140 150
GPKGQKGEPG DIKDIVGPKG PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG
160 170 180 190 200
RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA AQMAGGFDEK AGGAQMGVMQ
210 220 230 240 250
GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPPGK
260 270 280 290 300
PGDDGEAGKP GKSGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
310 320 330 340 350
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP
360 370 380 390 400
GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS
410 420 430 440 450
PGPAGAAGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG
460 470 480 490 500
PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG APGPAGEEGK RGARGEPGGA
510 520 530 540 550
GPAGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG PKGANGDPGR
560 570 580 590 600
PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
610 620 630 640 650
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA
660 670 680 690 700
GERGEQGAPG PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE
710 720 730 740 750
RGFPGERGSP GSQGLQGARG LPGTPGTDGP KGAAGPAGPP GAQGPPGLQG
760 770 780 790 800
MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN
810 820 830 840 850
GEKGEVGPPG PAGTAGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGE
860 870 880 890 900
QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
910 920 930 940 950
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA
960 970 980 990 1000
GPPGEKGEPG DDGPSGPDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP
1010 1020 1030 1040 1050
SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG
1060 1070 1080 1090 1100
AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG PIGKQGDRGE AGAQGPMGPA
1110 1120 1130 1140 1150
GPAGARGMPG PQGPRGDKGE TGEAGERGLK GHRGFTGLQG LPGPPGPSGD
1160 1170 1180 1190 1200
QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
1210 1220 1230 1240 1250
PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADEAAGNLRQ
1260 1270 1280 1290 1300
HDAEVDATLK SLNNQIESLR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI
1310 1320 1330 1340 1350
DPNQGCTLDA MKVFCNMETG ETCVYPNPAS VPKKNWWSSK SKDKKHIWFG
1360 1370 1380 1390 1400
ETINGGFHFS YGDDNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL
1410 1420 1430 1440 1450
DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTVLKDGCTK HTGKWGKTMI
1460 1470 1480
EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
Length:1,487
Mass (Da):141,828
Last modified:November 30, 2010 - v4
Checksum:iF99891F6FD1E47F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti202P → V AA sequence (PubMed:782511).Curated1
Sequence conflicti380T → Q AA sequence (PubMed:2714276).Curated1
Sequence conflicti400S → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti412T → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti436P → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti443Q → T AA sequence (PubMed:2714276).Curated1
Sequence conflicti446T → S AA sequence (PubMed:2714276).Curated1
Sequence conflicti476A → T in AAA30436 (PubMed:7511638).Curated1
Sequence conflicti478P → V AA sequence (PubMed:2714276).Curated1
Sequence conflicti514N → S AA sequence (PubMed:2714276).Curated1
Sequence conflicti518P → S in AAA30436 (PubMed:7511638).Curated1
Sequence conflicti523L → I AA sequence (PubMed:2714276).Curated1
Sequence conflicti529A → P AA sequence (PubMed:2714276).Curated1
Sequence conflicti535 – 539PSGLA → SPGAV AA sequence (PubMed:2714276).Curated5
Sequence conflicti544 – 548ANGDP → SPGEA AA sequence (PubMed:2714276).Curated5
Sequence conflicti554P → A AA sequence (PubMed:2714276).Curated1
Sequence conflicti560R → K AA sequence (PubMed:2714276).Curated1
Sequence conflicti677G → P AA sequence (PubMed:4857180).Curated1
Sequence conflicti712S → A in AAD42347 (PubMed:10479530).Curated1
Sequence conflicti718A → P in AAD42347 (PubMed:10479530).Curated1
Sequence conflicti734A → S in AAD42347 (PubMed:10479530).Curated1
Sequence conflicti1372N → D in CAA26269 (PubMed:2582365).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti349Q → L.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFC03017082 Genomic DNA. No translation available.
AAFC03017085 Genomic DNA. No translation available.
AAFC03056593 Genomic DNA. No translation available.
L28918 mRNA. Translation: AAA30436.2.
AF138883 mRNA. Translation: AAD42346.1.
AF138957 mRNA. Translation: AAD42347.1.
X02420 mRNA. Translation: CAA26269.1.
PIRiA90369. CGBO6C.
I45876.
RefSeqiNP_001001135.2. NM_001001135.3.
UniGeneiBt.21390.

Genome annotation databases

EnsembliENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155.
GeneIDi407142.
KEGGibta:407142.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFC03017082 Genomic DNA. No translation available.
AAFC03017085 Genomic DNA. No translation available.
AAFC03056593 Genomic DNA. No translation available.
L28918 mRNA. Translation: AAA30436.2.
AF138883 mRNA. Translation: AAD42346.1.
AF138957 mRNA. Translation: AAD42347.1.
X02420 mRNA. Translation: CAA26269.1.
PIRiA90369. CGBO6C.
I45876.
RefSeqiNP_001001135.2. NM_001001135.3.
UniGeneiBt.21390.

3D structure databases

ProteinModelPortaliP02459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02459. 1 interactor.
STRINGi9913.ENSBTAP00000017505.

Proteomic databases

PaxDbiP02459.
PRIDEiP02459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155.
GeneIDi407142.
KEGGibta:407142.

Organism-specific databases

CTDi1280.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02459.
KOiK19719.
OMAiKDCLNPE.
OrthoDBiEOG091G03LV.
TreeFamiTF344135.

Enzyme and pathway databases

ReactomeiR-BTA-1442490. Collagen degradation.
R-BTA-1474244. Extracellular matrix organization.
R-BTA-1650814. Collagen biosynthesis and modifying enzymes.
R-BTA-186797. Signaling by PDGF.
R-BTA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-BTA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-BTA-216083. Integrin cell surface interactions.
R-BTA-3000171. Non-integrin membrane-ECM interactions.
R-BTA-3000178. ECM proteoglycans.
R-BTA-419037. NCAM1 interactions.
R-BTA-8874081. MET activates PTK2 signaling.

Miscellaneous databases

PMAP-CutDBP02459.

Gene expression databases

BgeeiENSBTAG00000013155.
ExpressionAtlasiP02459. differential.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO2A1_BOVIN
AccessioniPrimary (citable) accession number: P02459
Secondary accession number(s): Q28070, Q9XT24, Q9XT25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 30, 2010
Last modified: November 30, 2016
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.