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Q91717 (CO2A1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Gene names
Name:col2a1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length1486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

Homotrimers of alpha 1(II) chains By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix By similarity.

Developmental stage

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. Ref.1

Domain

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.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains By similarity.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 183157N-terminal propeptide By similarity
PRO_0000286178
Chain184 – 12431060Collagen alpha-1(II) chain
PRO_0000286179
Propeptide1244 – 1486243C-terminal propeptide By similarity
PRO_0000286180

Regions

Domain36 – 9459VWFC
Domain1252 – 1486235Fibrillar collagen NC1
Region203 – 12161014Triple-helical region
Region1217 – 124327Nonhelical region (C-terminal)

Sites

Metal binding13001Calcium By similarity
Metal binding13021Calcium By similarity
Metal binding13031Calcium; via carbonyl oxygen By similarity
Metal binding13051Calcium; via carbonyl oxygen By similarity
Metal binding13081Calcium By similarity
Site183 – 1842Cleavage; by procollagen N-endopeptidase By similarity
Site1243 – 12442Cleavage; by procollagen C-endopeptidase By similarity

Amino acid modifications

Glycosylation13871N-linked (GlcNAc...) Potential
Disulfide bond1282 ↔ 1314 By similarity
Disulfide bond1288Interchain (with C-1305) By similarity
Disulfide bond1305Interchain (with C-1288) By similarity
Disulfide bond1322 ↔ 1484 By similarity
Disulfide bond1392 ↔ 1437 By similarity

Experimental info

Sequence conflict4561Q → E in AAA49678. Ref.1
Sequence conflict12871L → I in AAA49678. Ref.1
Sequence conflict13151D → N in AAA49678. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91717 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 02C18E5F5807100E

FASTA1,486142,263
        10         20         30         40         50         60 
MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLDTGSCVQ HGQRYSDKDV WKPEPCQICV 

        70         80         90        100        110        120 
CDTGTVLCDD IICEESKDCP NAEIPFGECC PICPTEQSST SSGQGVLKGQ KGEPGDIKDV 

       130        140        150        160        170        180 
LGPRGPPGPQ GPSGEQGSRG ERGDKGEKGA PGPRGRDGEP GTPGNPGPVG PPGPPGLGGN 

       190        200        210        220        230        240 
FAAQMTGGFD EKAGGAQMGV MQGPMGPMGP RGPPGPTGAP GPQGFQGNPG EPGEPGAGGP 

       250        260        270        280        290        300 
MGPRGPPGPS GKPGDDGEAG KPGKSGERGP PGPQGARGFP GTPGLPGVKG HRGYPGLDGA 

       310        320        330        340        350        360 
KGEAGAAGAK GEGGATGEAG SPGPMGPRGL PGERGRPGSS GAAGARGNDG LPGPAGPPGP 

       370        380        390        400        410        420 
VGPAGAPGFP GAPGSKGEAG PTGARGPEGA QGPRGESGTP GSPGPAGASG NPGTDGIPGA 

       430        440        450        460        470        480 
KGSSGGPGIA GAPGFPGPRG PPGPQGATGP LGPKGQTGDP GVAGFKGEQG PKGEIGSAGP 

       490        500        510        520        530        540 
QGAPGPAGEE GKRGARGEPG AAGPNGPPGE RGAPGNRGFP GQDGLAGPKG APGERGVPGL 

       550        560        570        580        590        600 
GGPKGGNGDP GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GASGEDGRPG PPGPQGARGQ 

       610        620        630        640        650        660 
PGVMGFPGPK GANGEPGKAG EKGLVGAPGL RGLPGKDGET GSQGPNGPAG PAGERGEQGP 

       670        680        690        700        710        720 
PGPSGFQGLP GPPGSPGEGG KPGDQGVPGE AGAPGLVGPR GERGFPGERG SSGPQGLQGP 

       730        740        750        760        770        780 
RGLPGTPGTD GPKGASGPSG PNGAQGPPGL QGMPGERGAA GISGPKGDRG DTGEKGPEGA 

       790        800        810        820        830        840 
SGKDGSRGLT GPIGPPGPAG PNGEKGESGP SGPPGIVGAR GAPGDRGENG PPGPAGFAGP 

       850        860        870        880        890        900 
PGADGQSGLK GDQGESGQKG DAGAPGPQGP SGAPGPQGPT GVFGPKGARG AQGPAGATGF 

       910        920        930        940        950        960 
PGAAGRVGTP GPNGNPGPPG PPGSAGKEGP KGVRGDAGPP GRAGDPGLQG AAGAPGEKGE 

       970        980        990       1000       1010       1020 
PGEDGPSGPD GPPGPQGLSG QRGIVGLPGQ RGERGFPGLP GPSGEPGKQG GPGSSGDRGP 

      1030       1040       1050       1060       1070       1080 
PGPVGPPGLT GPSGEPGREG NPGSDGPPGR DGATGIKGDR GETGPLGAPG APGAPGAPGS 

      1090       1100       1110       1120       1130       1140 
VGPTGKQGDR GESGPQGPLG PSGPAGARGL AGPQGPRGDK GEAGEAGERG QKGHRGFTGL 

      1150       1160       1170       1180       1190       1200 
QGLPGPPGSA GDQGATGPAG PAGPRGPPGP VGPSGKDGSN GISGPIGPPG PRGRSGETGP 

      1210       1220       1230       1240       1250       1260 
SGPPGQPGPP GPPGPPGPGI DMSAFAGLSQ PEKGPDPMRY MRADQASNSL PVDVEATLKS 

      1270       1280       1290       1300       1310       1320 
LNNQIENIRS PDGTKKNPAR TCRDLKLCHP EWKSGDYWID PNQGCTVDAI KVFCDMETGE 

      1330       1340       1350       1360       1370       1380 
TCVYPNPSKI PKKNWWSAKG KEKKHIWFGE TINGGFQFSY GDDSSAPNTA NIQMTFLRLL 

      1390       1400       1410       1420       1430       1440 
STDASQNITY HCKNSIAFMD EASGNLKKAV LLQGSNDVEI RAEGNSRFTY NALEDGCKKH 

      1450       1460       1470       1480 
TGKWSKTVIE YRTQKTSRLP IVDIAPMDIG GADQEFGVDI GPVCFL

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M63595 mRNA. Translation: AAA49678.1.
BC048221 mRNA. Translation: AAH48221.1.
BC111515 mRNA. Translation: AAI11516.1.
PIRA40333.
B40333.
RefSeqNP_001081258.1. NM_001087789.1.
UniGeneXl.606.

3D structure databases

HSSPHSSP built from PDB template 1Q7D based on UniProtKB Q15201.
ProteinModelPortalQ91717.
SMRQ91717. Positions 34-101.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397738.
KEGGxla:397738.

Organism-specific databases

CTD1280.
XenbaseXB-GENE-6252613. col2a1.

Phylogenomic databases

HOVERGENHBG004933.
KOK06236.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCO2A1_XENLA
AccessionPrimary (citable) accession number: Q91717
Secondary accession number(s): Q7ZTI6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: April 3, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents