UniProtKB - Q6P4Z2 (CO2A1_XENTR)
Protein
Collagen alpha-1(II) chain
Gene
col2a1
Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
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 (By similarity).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1306 | CalciumBy similarity | 1 | |
Metal bindingi | 1308 | CalciumBy similarity | 1 | |
Metal bindingi | 1309 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1311 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1314 | CalciumBy similarity | 1 |
GO - Molecular functioni
- extracellular matrix structural constituent Source: GO_Central
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- collagen fibril organization Source: GO_Central
- extracellular matrix organization Source: GO_Central
- notochord development Source: GO_Central
- skeletal system development Source: GO_Central
Keywordsi
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-XTR-1442490 Collagen degradation R-XTR-1474244 Extracellular matrix organization R-XTR-1650814 Collagen biosynthesis and modifying enzymes R-XTR-186797 Signaling by PDGF R-XTR-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell R-XTR-2022090 Assembly of collagen fibrils and other multimeric structures R-XTR-216083 Integrin cell surface interactions R-XTR-3000171 Non-integrin membrane-ECM interactions R-XTR-3000178 ECM proteoglycans R-XTR-419037 NCAM1 interactions R-XTR-8874081 MET activates PTK2 signaling R-XTR-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 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
Taxonomic identifieri | 8364 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Silurana |
Proteomesi |
|
Organism-specific databases
Xenbasei | XB-GENE-6258353 col2a1 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix PROSITE-ProRule annotation
Extracellular region or secreted
- extracellular matrix Source: GO_Central
- extracellular space Source: GO_Central
Other locations
- collagen trimer Source: GO_Central
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 26 | Sequence analysisAdd BLAST | 26 | |
PropeptideiPRO_0000286181 | 27 – 186 | N-terminal propeptideBy similarityAdd BLAST | 160 | |
ChainiPRO_0000286182 | 187 – 1246 | Collagen alpha-1(II) chainAdd BLAST | 1060 | |
PropeptideiPRO_0000286183 | 1247 – 1492 | C-terminal propeptideBy similarityAdd BLAST | 246 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 664 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 673 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 675 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 676 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 679 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 912 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 913 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 919 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 925 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1149 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1186 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1191 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1192 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1206 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1207 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1210 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1212 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1213 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1216 | 4-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1218 | 3-hydroxyprolineBy similarity | 1 | |
Modified residuei | 1219 | 4-hydroxyprolineBy similarity | 1 | |
Disulfide bondi | 1288 ↔ 1320 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1294 | Interchain (with C-1311)PROSITE-ProRule annotation | ||
Disulfide bondi | 1311 | Interchain (with C-1294)PROSITE-ProRule annotation | ||
Disulfide bondi | 1328 ↔ 1490 | PROSITE-ProRule annotation | ||
Glycosylationi | 1393 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1398 ↔ 1443 | PROSITE-ProRule annotation |
Post-translational modificationi
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.By similarity
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.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 186 – 187 | Cleavage; by procollagen N-endopeptidaseBy similarity | 2 | |
Sitei | 1246 – 1247 | Cleavage; by procollagen C-endopeptidaseBy similarity | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, HydroxylationProteomic databases
PaxDbi | Q6P4Z2 |
PRIDEi | Q6P4Z2 |
Interactioni
Subunit structurei
Homotrimers of alpha 1(II) chains.
By similarityProtein-protein interaction databases
STRINGi | 8364.ENSXETP00000043834 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 36 – 94 | VWFCPROSITE-ProRule annotationAdd BLAST | 59 | |
Domaini | 1258 – 1492 | Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST | 235 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 206 – 1219 | Triple-helical regionAdd BLAST | 1014 | |
Regioni | 1220 – 1246 | Nonhelical region (C-terminal)Add BLAST | 27 |
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 ENOG410XNMM LUCA |
InParanoidi | Q6P4Z2 |
KOi | K19719 |
OrthoDBi | 337699at2759 |
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, 6 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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
Q6P4Z2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLATGSCVQ HGQRYSDKDV
60 70 80 90 100
WKPEPCQICV CDTGNVLCDE IICEDPKDCP NAEIPFGECC PICPTEQSST
110 120 130 140 150
SSGQGVLKGQ KGEPGDIKDV VGPKGPPGPQ GPSGEQGPRG DRGDKGEKGA
160 170 180 190 200
PGPRGRDGEP GTPGNPGPVG PPGPPGPPGL GGNFAAQMTG GFDEKAGGAQ
210 220 230 240 250
MGVMQGPMGP MGPRGPPGPT GAPGPQGFQG NPGEPGEPGA GGPMGPRGPP
260 270 280 290 300
GPAGKPGDDG EAGKPGKSGE RGPPGPQGAR GFPGTPGLPG VKGHRGYPGL
310 320 330 340 350
DGSKGEAGAA GAKGEGGATG EAGSPGPMGP RGLPGERGRP GASGAAGARG
360 370 380 390 400
NDGLPGPAGP PGPVGPAGAP GFPGAPGSKG EAGPTGARGP EGAQGPRGES
410 420 430 440 450
GTPGSPGPAG ASGNPGTDGI PGAKGSSGAP GIAGAPGFPG PRGPPGPQGA
460 470 480 490 500
TGPLGPKGQT GDPGVAGFKG EHGPKGEIGS AGPQGAPGPA GEEGKRGARG
510 520 530 540 550
EPGAAGPLGP PGERGAPGNR GFPGQDGLAG PKGAPGERGV PGLGGPKGAN
560 570 580 590 600
GDPGRPGEPG LPGARGLTGR PGDAGPQGKV GPSGASGEDG RPGPPGPQGA
610 620 630 640 650
RGQPGVMGFP GPKGANGEPG KAGEKGLLGA PGLRGLPGKD GETGAQGPNG
660 670 680 690 700
PAGPAGERGE QGPPGPSGFQ GLPGPPGSPG EGGKPGDQGV PGEAGAPGLV
710 720 730 740 750
GPRGERGFPG ERGSSGPQGL QGPRGLPGTP GTDGPKGATG PSGPNGAQGP
760 770 780 790 800
PGLQGMPGER GAAGISGPKG DRGDTGEKGP EGAPGKDGSR GLTGPIGPPG
810 820 830 840 850
PSGPNGEKGE SGPSGPAGIV GARGAPGDRG ETGPPGPAGF AGPPGADGQA
860 870 880 890 900
GLKGDQGESG QKGDAGAPGP QGPSGAPGPQ GPTGVNGPKG ARGAQGPPGA
910 920 930 940 950
TGFPGAAGRV GPPGPNGNPG PSGAPGSAGK EGPKGARGDA GPTGRAGDPG
960 970 980 990 1000
LQGPAGVPGE KGESGEDGPS GPDGPPGPQG LSGQRGIVGL PGQRGERGFP
1010 1020 1030 1040 1050
GLPGPSGEPG KQGGPGSAGD RGPPGPVGPP GLTGPAGEPG REGNAGSDGP
1060 1070 1080 1090 1100
PGRDGATGIK GDRGETGPLG APGAPGAPGA PGPVGPTGKQ GDRGESGPQG
1110 1120 1130 1140 1150
PLGPSGPAGA RGLPGPQGPR GDKGEAGEAG ERGQKGHRGF TGLQGLPGPP
1160 1170 1180 1190 1200
GTAGDQGASG PAGPGGPRGP PGPVGPSGKD GSNGLPGPIG PPGPRGRGGE
1210 1220 1230 1240 1250
TGPAGPPGQP GPPGPPGPPG PGIDMSAFAG LSQPEKGPDP MRYMRADQAS
1260 1270 1280 1290 1300
SSVPQRDVDV EATLKSLNNQ IESIRSPDGT KKNPARTCRD LKLCHPEWKS
1310 1320 1330 1340 1350
GDYWIDPNQG CTVDAIKVFC NMETGETCVY PNPSKIPKKN WWSAKGKEKK
1360 1370 1380 1390 1400
HIWFGETING GFQFSYGDDS SAPNTANIQM TFLRLLSTDA TQNITYHCKN
1410 1420 1430 1440 1450
SIAFMDEASG NLKKAVLLQG SNDVEIRAEG NSRFTYNALE DGCKKHTGKW
1460 1470 1480 1490
SKTVIEYRTQ KTSRLPIVDI APMDIGGADQ EFGVDIGPVC FL
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF6WIP1 | F6WIP1_XENTR | Collagen alpha-1(II) chain | col2a1 | 1,494 | Annotation score: | ||
F7B315 | F7B315_XENTR | Collagen alpha-1(II) chain | col2a1 | 1,492 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC063191 mRNA Translation: AAH63191.1 |
RefSeqi | NP_989220.1, NM_203889.1 |
Genome annotation databases
GeneIDi | 394828 |
KEGGi | xtr:394828 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC063191 mRNA Translation: AAH63191.1 |
RefSeqi | NP_989220.1, NM_203889.1 |
3D structure databases
SMRi | Q6P4Z2 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 8364.ENSXETP00000043834 |
Proteomic databases
PaxDbi | Q6P4Z2 |
PRIDEi | Q6P4Z2 |
Genome annotation databases
GeneIDi | 394828 |
KEGGi | xtr:394828 |
Organism-specific databases
CTDi | 1280 |
Xenbasei | XB-GENE-6258353 col2a1 |
Phylogenomic databases
eggNOGi | KOG3544 Eukaryota ENOG410XNMM LUCA |
InParanoidi | Q6P4Z2 |
KOi | K19719 |
OrthoDBi | 337699at2759 |
Enzyme and pathway databases
Reactomei | R-XTR-1442490 Collagen degradation R-XTR-1474244 Extracellular matrix organization R-XTR-1650814 Collagen biosynthesis and modifying enzymes R-XTR-186797 Signaling by PDGF R-XTR-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell R-XTR-2022090 Assembly of collagen fibrils and other multimeric structures R-XTR-216083 Integrin cell surface interactions R-XTR-3000171 Non-integrin membrane-ECM interactions R-XTR-3000178 ECM proteoglycans R-XTR-419037 NCAM1 interactions R-XTR-8874081 MET activates PTK2 signaling R-XTR-8948216 Collagen chain trimerization |
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, 6 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CO2A1_XENTR | |
Accessioni | Q6P4Z2Primary (citable) accession number: Q6P4Z2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 2007 |
Last sequence update: | July 5, 2004 | |
Last modified: | July 3, 2019 | |
This is version 80 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families