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Q91717

- CO2A1_XENLA

UniProt

Q91717 - CO2A1_XENLA

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Protein

Collagen alpha-1(II) chain

Gene

col2a1

Organism
Xenopus laevis (African clawed frog)
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
Sitei183 – 1842Cleavage; by procollagen N-endopeptidaseBy similarity
Sitei1243 – 12442Cleavage; by procollagen C-endopeptidaseBy similarity
Metal bindingi1300 – 13001CalciumBy similarity
Metal bindingi1302 – 13021CalciumBy similarity
Metal bindingi1303 – 13031Calcium; via carbonyl oxygenBy similarity
Metal bindingi1305 – 13051Calcium; via carbonyl oxygenBy similarity
Metal bindingi1308 – 13081CalciumBy 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 laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6252613. 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 – 183157N-terminal propeptideBy similarityPRO_0000286178Add
BLAST
Chaini184 – 12431060Collagen alpha-1(II) chainPRO_0000286179Add
BLAST
Propeptidei1244 – 1486243C-terminal propeptideBy similarityPRO_0000286180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1282 ↔ 1314PROSITE-ProRule annotation
Disulfide bondi1288 – 1288Interchain (with C-1305)PROSITE-ProRule annotation
Disulfide bondi1305 – 1305Interchain (with C-1288)PROSITE-ProRule annotation
Disulfide bondi1322 ↔ 1484PROSITE-ProRule annotation
Glycosylationi1387 – 13871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1392 ↔ 1437PROSITE-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

Expressioni

Developmental stagei

Initially, the transcripts are localized to notochord, somites, and the dorsal region of the lateral plate mesoderm. At later stages of development and parallel to increased mRNA accumulation, collagen expression becomes progressively more confined to chondrogenic regions of the tadpole.1 Publication

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ91717.
SMRiQ91717. Positions 34-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 9459VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1252 – 1486235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni203 – 12161014Triple-helical regionAdd
BLAST
Regioni1217 – 124327Nonhelical 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

HOVERGENiHBG004933.
KOiK06236.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 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.

Q91717-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLDTGSCVQ HGQRYSDKDV
60 70 80 90 100
WKPEPCQICV CDTGTVLCDD IICEESKDCP NAEIPFGECC PICPTEQSST
110 120 130 140 150
SSGQGVLKGQ KGEPGDIKDV LGPRGPPGPQ GPSGEQGSRG ERGDKGEKGA
160 170 180 190 200
PGPRGRDGEP GTPGNPGPVG PPGPPGLGGN FAAQMTGGFD EKAGGAQMGV
210 220 230 240 250
MQGPMGPMGP RGPPGPTGAP GPQGFQGNPG EPGEPGAGGP MGPRGPPGPS
260 270 280 290 300
GKPGDDGEAG KPGKSGERGP PGPQGARGFP GTPGLPGVKG HRGYPGLDGA
310 320 330 340 350
KGEAGAAGAK GEGGATGEAG SPGPMGPRGL PGERGRPGSS GAAGARGNDG
360 370 380 390 400
LPGPAGPPGP VGPAGAPGFP GAPGSKGEAG PTGARGPEGA QGPRGESGTP
410 420 430 440 450
GSPGPAGASG NPGTDGIPGA KGSSGGPGIA GAPGFPGPRG PPGPQGATGP
460 470 480 490 500
LGPKGQTGDP GVAGFKGEQG PKGEIGSAGP QGAPGPAGEE GKRGARGEPG
510 520 530 540 550
AAGPNGPPGE RGAPGNRGFP GQDGLAGPKG APGERGVPGL GGPKGGNGDP
560 570 580 590 600
GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GASGEDGRPG PPGPQGARGQ
610 620 630 640 650
PGVMGFPGPK GANGEPGKAG EKGLVGAPGL RGLPGKDGET GSQGPNGPAG
660 670 680 690 700
PAGERGEQGP PGPSGFQGLP GPPGSPGEGG KPGDQGVPGE AGAPGLVGPR
710 720 730 740 750
GERGFPGERG SSGPQGLQGP RGLPGTPGTD GPKGASGPSG PNGAQGPPGL
760 770 780 790 800
QGMPGERGAA GISGPKGDRG DTGEKGPEGA SGKDGSRGLT GPIGPPGPAG
810 820 830 840 850
PNGEKGESGP SGPPGIVGAR GAPGDRGENG PPGPAGFAGP PGADGQSGLK
860 870 880 890 900
GDQGESGQKG DAGAPGPQGP SGAPGPQGPT GVFGPKGARG AQGPAGATGF
910 920 930 940 950
PGAAGRVGTP GPNGNPGPPG PPGSAGKEGP KGVRGDAGPP GRAGDPGLQG
960 970 980 990 1000
AAGAPGEKGE PGEDGPSGPD GPPGPQGLSG QRGIVGLPGQ RGERGFPGLP
1010 1020 1030 1040 1050
GPSGEPGKQG GPGSSGDRGP PGPVGPPGLT GPSGEPGREG NPGSDGPPGR
1060 1070 1080 1090 1100
DGATGIKGDR GETGPLGAPG APGAPGAPGS VGPTGKQGDR GESGPQGPLG
1110 1120 1130 1140 1150
PSGPAGARGL AGPQGPRGDK GEAGEAGERG QKGHRGFTGL QGLPGPPGSA
1160 1170 1180 1190 1200
GDQGATGPAG PAGPRGPPGP VGPSGKDGSN GISGPIGPPG PRGRSGETGP
1210 1220 1230 1240 1250
SGPPGQPGPP GPPGPPGPGI DMSAFAGLSQ PEKGPDPMRY MRADQASNSL
1260 1270 1280 1290 1300
PVDVEATLKS LNNQIENIRS PDGTKKNPAR TCRDLKLCHP EWKSGDYWID
1310 1320 1330 1340 1350
PNQGCTVDAI KVFCDMETGE TCVYPNPSKI PKKNWWSAKG KEKKHIWFGE
1360 1370 1380 1390 1400
TINGGFQFSY GDDSSAPNTA NIQMTFLRLL STDASQNITY HCKNSIAFMD
1410 1420 1430 1440 1450
EASGNLKKAV LLQGSNDVEI RAEGNSRFTY NALEDGCKKH TGKWSKTVIE
1460 1470 1480
YRTQKTSRLP IVDIAPMDIG GADQEFGVDI GPVCFL
Length:1,486
Mass (Da):142,263
Last modified:May 1, 2007 - v2
Checksum:i02C18E5F5807100E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561Q → E in AAA49678. (PubMed:1918153)Curated
Sequence conflicti1287 – 12871L → I in AAA49678. (PubMed:1918153)Curated
Sequence conflicti1315 – 13151D → N in AAA49678. (PubMed:1918153)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63595 mRNA. Translation: AAA49678.1.
BC048221 mRNA. Translation: AAH48221.1.
BC111515 mRNA. Translation: AAI11516.1.
PIRiA40333.
B40333.
RefSeqiNP_001081258.1. NM_001087789.1.
UniGeneiXl.606.

Genome annotation databases

GeneIDi397738.
KEGGixla:397738.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63595 mRNA. Translation: AAA49678.1 .
BC048221 mRNA. Translation: AAH48221.1 .
BC111515 mRNA. Translation: AAI11516.1 .
PIRi A40333.
B40333.
RefSeqi NP_001081258.1. NM_001087789.1.
UniGenei Xl.606.

3D structure databases

ProteinModelPortali Q91717.
SMRi Q91717. Positions 34-101.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397738.
KEGGi xla:397738.

Organism-specific databases

CTDi 1280.
Xenbasei XB-GENE-6252613. col2a1.

Phylogenomic databases

HOVERGENi HBG004933.
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. 9 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

« Hide 'large scale' publications
  1. "Expression of two nonallelic type II procollagen genes during Xenopus laevis embryogenesis is characterized by stage-specific production of alternatively spliced transcripts."
    Su M.W., Suzuki H.R., Bieker J.J., Solursh M., Ramirez F.
    J. Cell Biol. 115:565-575(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiCO2A1_XENLA
AccessioniPrimary (citable) accession number: Q91717
Secondary accession number(s): Q7ZTI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3