SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q91717

- CO2A1_XENLA

UniProt

Q91717 - CO2A1_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei183 – 1842Cleavage; by procollagen N-endopeptidase By similarity
Sitei1243 – 12442Cleavage; by procollagen C-endopeptidase By similarity
Metal bindingi1300 – 13001Calcium By similarity
Metal bindingi1302 – 13021Calcium By similarity
Metal bindingi1303 – 13031Calcium; via carbonyl oxygen By similarity
Metal bindingi1305 – 13051Calcium; via carbonyl oxygen By similarity
Metal bindingi1308 – 13081Calcium By 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

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed prediction
Add
BLAST
Propeptidei27 – 183157N-terminal propeptide By similarity
PRO_0000286178Add
BLAST
Chaini184 – 12431060Collagen alpha-1(II) chain
PRO_0000286179Add
BLAST
Propeptidei1244 – 1486243C-terminal propeptide By similarity
PRO_0000286180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1282 ↔ 1314 By similarity
Disulfide bondi1288 – 1288Interchain (with C-1305) By similarity
Disulfide bondi1305 – 1305Interchain (with C-1288) By similarity
Disulfide bondi1322 ↔ 1484 By similarity
Glycosylationi1387 – 13871N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1392 ↔ 1437 By similarity

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 9459VWFC
Add
BLAST
Domaini1252 – 1486235Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni203 – 12161014Triple-helical region
Add
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.

Sequence similaritiesi

Contains 1 VWFC domain.

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

MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLDTGSCVQ HGQRYSDKDV     50
WKPEPCQICV CDTGTVLCDD IICEESKDCP NAEIPFGECC PICPTEQSST 100
SSGQGVLKGQ KGEPGDIKDV LGPRGPPGPQ GPSGEQGSRG ERGDKGEKGA 150
PGPRGRDGEP GTPGNPGPVG PPGPPGLGGN FAAQMTGGFD EKAGGAQMGV 200
MQGPMGPMGP RGPPGPTGAP GPQGFQGNPG EPGEPGAGGP MGPRGPPGPS 250
GKPGDDGEAG KPGKSGERGP PGPQGARGFP GTPGLPGVKG HRGYPGLDGA 300
KGEAGAAGAK GEGGATGEAG SPGPMGPRGL PGERGRPGSS GAAGARGNDG 350
LPGPAGPPGP VGPAGAPGFP GAPGSKGEAG PTGARGPEGA QGPRGESGTP 400
GSPGPAGASG NPGTDGIPGA KGSSGGPGIA GAPGFPGPRG PPGPQGATGP 450
LGPKGQTGDP GVAGFKGEQG PKGEIGSAGP QGAPGPAGEE GKRGARGEPG 500
AAGPNGPPGE RGAPGNRGFP GQDGLAGPKG APGERGVPGL GGPKGGNGDP 550
GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GASGEDGRPG PPGPQGARGQ 600
PGVMGFPGPK GANGEPGKAG EKGLVGAPGL RGLPGKDGET GSQGPNGPAG 650
PAGERGEQGP PGPSGFQGLP GPPGSPGEGG KPGDQGVPGE AGAPGLVGPR 700
GERGFPGERG SSGPQGLQGP RGLPGTPGTD GPKGASGPSG PNGAQGPPGL 750
QGMPGERGAA GISGPKGDRG DTGEKGPEGA SGKDGSRGLT GPIGPPGPAG 800
PNGEKGESGP SGPPGIVGAR GAPGDRGENG PPGPAGFAGP PGADGQSGLK 850
GDQGESGQKG DAGAPGPQGP SGAPGPQGPT GVFGPKGARG AQGPAGATGF 900
PGAAGRVGTP GPNGNPGPPG PPGSAGKEGP KGVRGDAGPP GRAGDPGLQG 950
AAGAPGEKGE PGEDGPSGPD GPPGPQGLSG QRGIVGLPGQ RGERGFPGLP 1000
GPSGEPGKQG GPGSSGDRGP PGPVGPPGLT GPSGEPGREG NPGSDGPPGR 1050
DGATGIKGDR GETGPLGAPG APGAPGAPGS VGPTGKQGDR GESGPQGPLG 1100
PSGPAGARGL AGPQGPRGDK GEAGEAGERG QKGHRGFTGL QGLPGPPGSA 1150
GDQGATGPAG PAGPRGPPGP VGPSGKDGSN GISGPIGPPG PRGRSGETGP 1200
SGPPGQPGPP GPPGPPGPGI DMSAFAGLSQ PEKGPDPMRY MRADQASNSL 1250
PVDVEATLKS LNNQIENIRS PDGTKKNPAR TCRDLKLCHP EWKSGDYWID 1300
PNQGCTVDAI KVFCDMETGE TCVYPNPSKI PKKNWWSAKG KEKKHIWFGE 1350
TINGGFQFSY GDDSSAPNTA NIQMTFLRLL STDASQNITY HCKNSIAFMD 1400
EASGNLKKAV LLQGSNDVEI RAEGNSRFTY NALEDGCKKH TGKWSKTVIE 1450
YRTQKTSRLP IVDIAPMDIG GADQEFGVDI GPVCFL 1486
Length:1,486
Mass (Da):142,263
Last modified:May 1, 2007 - v2
Checksum:i02C18E5F5807100E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561Q → E in AAA49678. 1 Publication
Sequence conflicti1287 – 12871L → I in AAA49678. 1 Publication
Sequence conflicti1315 – 13151D → N in AAA49678. 1 Publication

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: July 9, 2014
This is version 71 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

Similar proteinsi