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UniProtKB - P02459 (CO2A1_BOVIN)
Protein
Collagen alpha-1(II) chain
Gene
COL2A1
Organism
Bos taurus (Bovine)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1301 | CalciumBy similarity | 1 | |
Metal bindingi | 1303 | CalciumBy similarity | 1 | |
Metal bindingi | 1304 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1306 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1309 | CalciumBy similarity | 1 |
GO - Molecular functioni
- extracellular matrix structural constituent Source: GO_Central
- identical protein binding Source: Ensembl
- metal ion binding Source: UniProtKB-KW
- MHC class II protein binding Source: Ensembl
- platelet-derived growth factor binding Source: Ensembl
- proteoglycan binding Source: Ensembl
GO - Biological processi
- anterior head development Source: Ensembl
- cartilage condensation Source: Ensembl
- cartilage development involved in endochondral bone morphogenesis Source: Ensembl
- cellular response to BMP stimulus Source: Ensembl
- central nervous system development Source: Ensembl
- chondrocyte differentiation Source: Ensembl
- collagen fibril organization Source: GO_Central
- embryonic skeletal joint morphogenesis Source: Ensembl
- endochondral ossification Source: Ensembl
- extracellular matrix organization Source: GO_Central
- heart morphogenesis Source: Ensembl
- inner ear morphogenesis Source: Ensembl
- limb bud formation Source: Ensembl
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
- notochord development Source: GO_Central
- otic vesicle development Source: Ensembl
- proteoglycan metabolic process Source: Ensembl
- regulation of gene expression Source: Ensembl
- roof of mouth development Source: Ensembl
- sensory perception of sound Source: Ensembl
- skeletal system development Source: GO_Central
- tissue homeostasis Source: Ensembl
- visual perception Source: Ensembl
Keywordsi
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-BTA-1442490, Collagen degradation R-BTA-1650814, Collagen biosynthesis and modifying enzymes R-BTA-2022090, Assembly of collagen fibrils and other multimeric structures R-BTA-3000171, Non-integrin membrane-ECM interactions R-BTA-3000178, ECM proteoglycans R-BTA-8948216, Collagen chain trimerization |
Names & Taxonomyi
Protein namesi | Recommended name: Collagen alpha-1(II) chainBy similarityAlternative name(s): Alpha-1 type II collagenBy similarity |
Gene namesi | Name:COL2A1By similarity |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | HostDB:ENSBTAG00000013155 |
VGNCi | VGNC:27564, COL2A1 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix PROSITE-ProRule annotation
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: GO_Central
Other locations
- basement membrane Source: Ensembl
- collagen trimer Source: GO_Central
- collagen type II trimer Source: GO_Central
- collagen type XI trimer Source: ComplexPortal
- collagen-containing extracellular matrix Source: ComplexPortal
- cytoplasm Source: Ensembl
- extracellular matrix Source: GO_Central
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Sequence analysisAdd BLAST | 25 | |
PropeptideiPRO_0000401210 | 26 – 181 | N-terminal propeptideBy similarityAdd BLAST | 156 | |
ChainiPRO_0000005725 | 182 – 1487 | Collagen alpha-1(II) chainAdd BLAST | 1306 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 190 | 5-hydroxylysineBy similarity | 1 | |
Glycosylationi | 190 | O-linked (Gal...) hydroxylysineBy similarity | 1 | |
Modified residuei | 212 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 218 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 230 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 233 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 245 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 248 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 251 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 260 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 269 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 278 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 281 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 284 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 287 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 287 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 293 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 299 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 299 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 305 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 308 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 308 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 314 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 320 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 329 | Hydroxyproline2 Publications | 1 | |
Modified residuei | 350 | Hydroxyproline3 Publications | 1 | |
Modified residuei | 356 | Hydroxyproline3 Publications | 1 | |
Modified residuei | 365 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 368 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 371 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 374 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 374 | O-linked (Gal...) hydroxylysineBy similarity | 1 | |
Modified residuei | 395 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 398 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 401 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 410 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 416 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 419 | 5-hydroxylysine1 Publication | 1 | |
Modified residuei | 425 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 431 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 434 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 440 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 452 | 5-hydroxylysine1 Publication | 1 | |
Modified residuei | 458 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 464 | 5-hydroxylysine1 Publication | 1 | |
Modified residuei | 470 | 5-hydroxylysine1 Publication | 1 | |
Modified residuei | 473 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 482 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 497 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 506 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 512 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 518 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 527 | 5-hydroxylysine1 Publication | 1 | |
Modified residuei | 530 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 542 | 5-hydroxylysine1 Publication | 1 | |
Modified residuei | 551 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 557 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 566 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 581 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 587 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 590 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 599 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 605 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 608 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 608 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 614 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 620 | 5-hydroxylysine1 Publication | 1 | |
Glycosylationi | 620 | O-linked (Gal...) hydroxylysine1 Publication | 1 | |
Modified residuei | 623 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 626 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 632 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 644 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 659 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 668 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 670 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 671 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 674 | Hydroxyproline1 Publication | 1 | |
Modified residuei | 907 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 908 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 914 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 920 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1130 | 5-hydroxylysineBy similarity | 1 | |
Glycosylationi | 1130 | O-linked (Gal...) hydroxylysineBy similarity | 1 | |
Modified residuei | 1144 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1181 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1186 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1187 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1201 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1202 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1205 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1207 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1208 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1211 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1213 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1214 | 4-hydroxyprolineBy similarity | 1 | |
Disulfide bondi | 1283 ↔ 1315 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1289 | Interchain (with C-1306)PROSITE-ProRule annotation | ||
Disulfide bondi | 1306 | Interchain (with C-1289)PROSITE-ProRule annotation | ||
Disulfide bondi | 1323 ↔ 1485 | PROSITE-ProRule annotation | ||
Glycosylationi | 1388 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1393 ↔ 1438 | PROSITE-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
Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains.4 Publications
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.By similarity
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.By similarity
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.3 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 181 – 182 | Cleavage; by procollagen N-endopeptidaseBy similarity | 2 | |
Sitei | 1241 – 1242 | Cleavage; by procollagen C-endopeptidaseBy similarity | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, HydroxylationProteomic databases
PaxDbi | P02459 |
PRIDEi | P02459 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000013155, Expressed in laryngeal cartilage and 55 other tissues |
Interactioni
Subunit structurei
Homotrimers of alpha 1(II) chains.
Binary interactionsi
P02459
With | #Exp. | IntAct |
---|---|---|
MATN1 [P21941] from Homo sapiens. | 3 | EBI-5281315,EBI-20828128 |
GO - Molecular functioni
- identical protein binding Source: Ensembl
- MHC class II protein binding Source: Ensembl
- platelet-derived growth factor binding Source: Ensembl
- proteoglycan binding Source: Ensembl
Protein-protein interaction databases
ComplexPortali | CPX-3105, Collagen type II trimer CPX-3108, Collagen type XI trimer variant 1 |
IntActi | P02459, 3 interactors |
STRINGi | 9913.ENSBTAP00000017505 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 32 – 90 | VWFCPROSITE-ProRule annotationAdd BLAST | 59 | |
Domaini | 1253 – 1487 | Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST | 235 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 96 – 1234 | DisorderedSequence analysisAdd BLAST | 1139 | |
Regioni | 201 – 1214 | Triple-helical regionBy similarityAdd BLAST | 1014 | |
Regioni | 1215 – 1241 | Nonhelical region (C-terminal)By similarityAdd BLAST | 27 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 133 – 149 | Basic and acidic residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 157 – 174 | Pro residuesSequence analysisAdd BLAST | 18 | |
Compositional biasi | 237 – 251 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 351 – 365 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 432 – 446 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 910 – 924 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1200 – 1217 | Pro residuesSequence analysisAdd BLAST | 18 |
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
Keywords - Domaini
Collagen, Repeat, SignalPhylogenomic databases
eggNOGi | KOG3544, Eukaryota |
GeneTreei | ENSGT00940000155224 |
InParanoidi | P02459 |
OMAi | GWQPGPK |
OrthoDBi | 337699at2759 |
TreeFami | TF344135 |
Family and domain databases
InterProi | View protein in InterPro IPR008160, Collagen IPR000885, Fib_collagen_C IPR001007, VWF_dom |
Pfami | View protein in Pfam PF01410, COLFI, 1 hit PF01391, Collagen, 7 hits PF00093, VWC, 1 hit |
SMARTi | View protein in SMART SM00038, COLFI, 1 hit SM00214, VWC, 1 hit |
PROSITEi | View protein in PROSITE PS51461, NC1_FIB, 1 hit PS01208, VWFC_1, 1 hit PS50184, VWFC_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P02459-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 202 | P → V AA sequence (PubMed:782511).Curated | 1 | |
Sequence conflicti | 380 | T → Q AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 400 | S → A AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 412 | T → A AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 436 | P → A AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 443 | Q → T AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 446 | T → S AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 476 | A → T in AAA30436 (PubMed:7511638).Curated | 1 | |
Sequence conflicti | 478 | P → V AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 514 | N → S AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 518 | P → S in AAA30436 (PubMed:7511638).Curated | 1 | |
Sequence conflicti | 523 | L → I AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 529 | A → P AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 535 – 539 | PSGLA → SPGAV AA sequence (PubMed:2714276).Curated | 5 | |
Sequence conflicti | 544 – 548 | ANGDP → SPGEA AA sequence (PubMed:2714276).Curated | 5 | |
Sequence conflicti | 554 | P → A AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 560 | R → K AA sequence (PubMed:2714276).Curated | 1 | |
Sequence conflicti | 677 | G → P AA sequence (PubMed:4857180).Curated | 1 | |
Sequence conflicti | 712 | S → A in AAD42347 (PubMed:10479530).Curated | 1 | |
Sequence conflicti | 718 | A → P in AAD42347 (PubMed:10479530).Curated | 1 | |
Sequence conflicti | 734 | A → S in AAD42347 (PubMed:10479530).Curated | 1 | |
Sequence conflicti | 1372 | N → D in CAA26269 (PubMed:2582365).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 349 | Q → L1 Publication | 1 |
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 |
PIRi | A90369, CGBO6C I45876 |
RefSeqi | NP_001001135.2, NM_001001135.3 |
Genome annotation databases
Ensembli | ENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155 |
GeneIDi | 407142 |
KEGGi | bta:407142 |
Similar proteinsi
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 |
PIRi | A90369, CGBO6C I45876 |
RefSeqi | NP_001001135.2, NM_001001135.3 |
3D structure databases
AlphaFoldDBi | P02459 |
PCDDBi | P02459 |
SMRi | P02459 |
ModBasei | Search... |
Protein-protein interaction databases
ComplexPortali | CPX-3105, Collagen type II trimer CPX-3108, Collagen type XI trimer variant 1 |
IntActi | P02459, 3 interactors |
STRINGi | 9913.ENSBTAP00000017505 |
Proteomic databases
PaxDbi | P02459 |
PRIDEi | P02459 |
Protocols and materials databases
ABCDi | P02459, 5 sequenced antibodies |
Genome annotation databases
Ensembli | ENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155 |
GeneIDi | 407142 |
KEGGi | bta:407142 |
Organism-specific databases
CTDi | 1280 |
VEuPathDBi | HostDB:ENSBTAG00000013155 |
VGNCi | VGNC:27564, COL2A1 |
Phylogenomic databases
eggNOGi | KOG3544, Eukaryota |
GeneTreei | ENSGT00940000155224 |
InParanoidi | P02459 |
OMAi | GWQPGPK |
OrthoDBi | 337699at2759 |
TreeFami | TF344135 |
Enzyme and pathway databases
Reactomei | R-BTA-1442490, Collagen degradation R-BTA-1650814, Collagen biosynthesis and modifying enzymes R-BTA-2022090, Assembly of collagen fibrils and other multimeric structures R-BTA-3000171, Non-integrin membrane-ECM interactions R-BTA-3000178, ECM proteoglycans R-BTA-8948216, Collagen chain trimerization |
Gene expression databases
Bgeei | ENSBTAG00000013155, Expressed in laryngeal cartilage and 55 other tissues |
Family and domain databases
InterProi | View protein in InterPro IPR008160, Collagen IPR000885, Fib_collagen_C IPR001007, VWF_dom |
Pfami | View protein in Pfam PF01410, COLFI, 1 hit PF01391, Collagen, 7 hits PF00093, VWC, 1 hit |
SMARTi | View protein in SMART SM00038, COLFI, 1 hit SM00214, VWC, 1 hit |
PROSITEi | View protein in PROSITE PS51461, NC1_FIB, 1 hit PS01208, VWFC_1, 1 hit PS50184, VWFC_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CO2A1_BOVIN | |
Accessioni | P02459Primary (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: | May 25, 2022 | |
This is version 171 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families