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Q6P4Z2

- CO2A1_XENTR

UniProt

Q6P4Z2 - CO2A1_XENTR

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Protein

Collagen alpha-1(II) chain

Gene

col2a1

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed - Annotation score: 4 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei186 – 1872Cleavage; by procollagen N-endopeptidaseBy similarity
Sitei1246 – 12472Cleavage; by procollagen C-endopeptidaseBy similarity
Metal bindingi1306 – 13061CalciumBy similarity
Metal bindingi1308 – 13081CalciumBy similarity
Metal bindingi1309 – 13091Calcium; via carbonyl oxygenBy similarity
Metal bindingi1311 – 13111Calcium; via carbonyl oxygenBy similarity
Metal bindingi1314 – 13141CalciumBy similarity

GO - Molecular functioni

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

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Gene namesi
Name:col2a1
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
ProteomesiUP000008143: Unplaced

Organism-specific databases

XenbaseiXB-GENE-6258353. col2a1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Propeptidei27 – 186160N-terminal propeptideBy similarityPRO_0000286181Add
BLAST
Chaini187 – 12461060Collagen alpha-1(II) chainPRO_0000286182Add
BLAST
Propeptidei1247 – 1492246C-terminal propeptideBy similarityPRO_0000286183Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1288 ↔ 1320PROSITE-ProRule annotation
Disulfide bondi1294 – 1294Interchain (with C-1311)PROSITE-ProRule annotation
Disulfide bondi1311 – 1311Interchain (with C-1294)PROSITE-ProRule annotation
Disulfide bondi1328 ↔ 1490PROSITE-ProRule annotation
Glycosylationi1393 – 13931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1398 ↔ 1443PROSITE-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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ6P4Z2.
PRIDEiQ6P4Z2.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.By similarity

Protein-protein interaction databases

STRINGi8364.ENSXETP00000023334.

Structurei

3D structure databases

ProteinModelPortaliQ6P4Z2.
SMRiQ6P4Z2. Positions 36-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 9459VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1258 – 1492235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 12191014Triple-helical regionAdd
BLAST
Regioni1220 – 124627Nonhelical 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
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG004933.
InParanoidiQ6P4Z2.
KOiK06236.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[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.

Q6P4Z2-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:1,492
Mass (Da):142,696
Last modified:July 5, 2004 - v1
Checksum:iDB7AF42B94210EB7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC063191 mRNA. Translation: AAH63191.1.
RefSeqiNP_989220.1. NM_203889.1.
UniGeneiStr.54515.

Genome annotation databases

GeneIDi394828.
KEGGixtr:394828.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC063191 mRNA. Translation: AAH63191.1 .
RefSeqi NP_989220.1. NM_203889.1.
UniGenei Str.54515.

3D structure databases

ProteinModelPortali Q6P4Z2.
SMRi Q6P4Z2. Positions 36-101.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 8364.ENSXETP00000023334.

Proteomic databases

PaxDbi Q6P4Z2.
PRIDEi Q6P4Z2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 394828.
KEGGi xtr:394828.

Organism-specific databases

CTDi 1280.
Xenbasei XB-GENE-6258353. col2a1.

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG004933.
InParanoidi Q6P4Z2.
KOi K06236.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiCO2A1_XENTR
AccessioniPrimary (citable) accession number: Q6P4Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 61 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