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P05539

- CO2A1_RAT

UniProt

P05539 - CO2A1_RAT

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Protein
Collagen alpha-1(II) chain
Gene
Col2a1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei113 – 1142Cleavage; by procollagen N-endopeptidase By similarity
Sitei1173 – 11742Cleavage; by procollagen C-endopeptidase By similarity
Metal bindingi1233 – 12331Calcium By similarity
Metal bindingi1235 – 12351Calcium By similarity
Metal bindingi1236 – 12361Calcium; via carbonyl oxygen By similarity
Metal bindingi1238 – 12381Calcium; via carbonyl oxygen By similarity
Metal bindingi1241 – 12411Calcium By similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: RGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cartilage development Source: RGD
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
Cleaved into the following 2 chains:
Gene namesi
Name:Col2a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2375. Col2a1.

Subcellular locationi

GO - Cellular componenti

  1. collagen type II trimer Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Propeptidei26 – 11388N-terminal propeptide By similarity
PRO_0000005735Add
BLAST
Chaini114 – 11731060Collagen alpha-1(II) chain
PRO_0000005736Add
BLAST
Chaini1174 – 1419246Chondrocalcin By similarity
PRO_0000043407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 12215-hydroxylysine By similarity
Glycosylationi122 – 1221O-linked (Gal...) By similarity
Modified residuei219 – 21915-hydroxylysine By similarity
Glycosylationi219 – 2191O-linked (Gal...) By similarity
Modified residuei231 – 23115-hydroxylysine By similarity
Glycosylationi231 – 2311O-linked (Gal...) By similarity
Modified residuei240 – 24015-hydroxylysine By similarity
Glycosylationi240 – 2401O-linked (Gal...) By similarity
Modified residuei306 – 30615-hydroxylysine By similarity
Glycosylationi306 – 3061O-linked (Gal...) By similarity
Modified residuei540 – 54015-hydroxylysine By similarity
Glycosylationi540 – 5401O-linked (Gal...) By similarity
Modified residuei552 – 55215-hydroxylysine By similarity
Glycosylationi552 – 5521O-linked (Gal...) By similarity
Modified residuei602 – 60213-hydroxyproline; partial1 Publication
Modified residuei839 – 83913-hydroxyproline; partial1 Publication
Modified residuei1076 – 107613-hydroxyproline; partial1 Publication
Modified residuei1118 – 111813-hydroxyproline1 Publication
Modified residuei1133 – 113313-hydroxyproline; partial1 Publication
Modified residuei1139 – 113913-hydroxyproline; partial1 Publication
Modified residuei1145 – 114513-hydroxyproline; partial1 Publication
Disulfide bondi1215 ↔ 1247 By similarity
Disulfide bondi1221 – 1221Interchain (with C-1238) By similarity
Disulfide bondi1238 – 1238Interchain (with C-1221) By similarity
Disulfide bondi1255 ↔ 1417 By similarity
Glycosylationi1320 – 13201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1325 ↔ 1370 By similarity

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-602, Pro-839, Pro-1076, Pro-1133, Pro-1139 and Pro-1145 by LEPREL1.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP05539.
PRIDEiP05539.

Expressioni

Tissue specificityi

Expressed in chondrocytes.1 Publication

Gene expression databases

GenevestigatoriP05539.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

Protein-protein interaction databases

IntActiP05539. 1 interaction.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1185 – 1419235Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 11461014Triple-helical region
Add
BLAST
Regioni1147 – 117327Nonhelical 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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
KOiK06236.
PhylomeDBiP05539.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 4 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05539-1 [UniParc]FASTAAdd to Basket

« Hide

MIRLGAPQSL VLLTLLIATV LQCQGQDARK LGPKGQKGEP GDIKDIIGPK     50
GPPGPQGPAG EQGPRGDRGD KGERGAPGPR GRDGEPGTPG NPGPPGPPGP 100
PGPPGLGGGN FAAQMAGGFD EKAGGAQMGV MQGPMGPMGP RGPPGPAGAP 150
GPQGFQGNPG EPGEPGVSGP IGPRGPPGPA GKPGDDGEAG KPGKAGERGL 200
PGPQGARGFP GTPGLPGVKG HRGYPGLDGA KGEAGAPGVK GESGSPGENG 250
SPGPMGPRGL PGERGRTGPA GAAGARGNDG QPGPAGPPGP VGPAGGPGFL 300
GAPGAKGEAG PTGARGPEGA QGSRGEPGNP GSPGPAGASG NPGTDGIPGA 350
KGSAGAPGIA GAPGFPGPRG PPGPQGATGP LGPKGQTGEP GIAGFKGEQG 400
PKGETGPAGP QGAPGPAGEE GKRGARGEPG GAGPIGPPGE RGAPGNRGFP 450
GQDGLAGPKG APGERGPSGL AGPKGANGDP GRPGEPGLPG ARGLTGRPGD 500
AGPQGKVGPS GAPGEDGRPG PPGPQGARGQ PGVMGFPGPK GANGEPGKAG 550
EKGLAGAPGL RGLPGKDGET GAAGPPGPSG PAGERGEQGA PGPSGFQGLP 600
GPPGPPGEGG KQGDQGIPGE AGAPGLVGPR GERGFPGERG SPGAQGLQGP 650
RGLPGTPGTD GPKGAAGPDG PPGAQGPPGL QGMPGERGAA GIAGPKGDRG 700
DVGEKGPEGA PGKDGGRGLT GPIGPPGPAG ANGEKGEVGP PGPSGSTGAR 750
GAPGERGETG PPGPAGFAGP PGADGQPGAK GDQGEAGQKG DAGAPGPQGP 800
SGAPGPQGPT GVTGPKGARG AQGPPGATGF PGAAGRVGPP GSNGNPGPAG 850
PPGPAGKDGP KGARGDTGAP GRAGDPGLQG PAGAPGEKGE PGDDGPSGSD 900
GPPGPQGLAG QRGIVGLPGQ RGERGFPGLP GPSGEPGKQG APGASGDRGP 950
PGPVGPPGLT GPAGEPGREG SPGADGPPGR DGAAGVKGDR GETGALGAPG 1000
APGPPGSPGP AGPTGKQGDR GEAGAQGPMG PSGPAGARGI AGPQGPRGDK 1050
GEAGEPGERG LKGHRGFTGL QGLPGPPGPS GDQGTSGPAG PSGPRGPPGP 1100
VGPSGKDGSN GIPGPIGPPG PRGRSGETGP AGPPGNPGPP GPPGPPGPGI 1150
DMSAFAGLGQ REKGPDPLQY MRADEADSTL RQHDVEVDAT LKSLNNQIES 1200
IRSPDGSRKN PARTCQDLKL CHPEWKSGDY WIDPNQGCTL DAMKVFCNME 1250
TGESCVYPNP ATVPRKNWWS SKSKEKKHIW FGETMNGGFH FSYGDGNLAP 1300
NTANVQMTFL RLLSTEGSQN ITYHCKNSIA YLDEAAGNLK KALLIQGSND 1350
VEMRAEGNSR FTYTALKDGC TKHTGKWGKT IIEYRSQKTS RLPIVDIAPM 1400
DIGGPDQEFG VDIGPVCFL 1419
Length:1,419
Mass (Da):134,570
Last modified:December 6, 2005 - v2
Checksum:iB7C63B77819CE50B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211E → Q in AAA40919. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L48440 mRNA. Translation: AAA79780.1.
K02804 mRNA. Translation: AAA40919.1.
M10613 Genomic DNA. Translation: AAA40920.1.
X79816 mRNA. Translation: CAA56213.1.
PIRiA05152.
I60384.
RefSeqiNP_037061.1. NM_012929.1.
UniGeneiRn.10124.

Genome annotation databases

GeneIDi25412.
KEGGirno:25412.
UCSCiRGD:2375. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L48440 mRNA. Translation: AAA79780.1 .
K02804 mRNA. Translation: AAA40919.1 .
M10613 Genomic DNA. Translation: AAA40920.1 .
X79816 mRNA. Translation: CAA56213.1 .
PIRi A05152.
I60384.
RefSeqi NP_037061.1. NM_012929.1.
UniGenei Rn.10124.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P05539. 1 interaction.

Proteomic databases

PaxDbi P05539.
PRIDEi P05539.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25412.
KEGGi rno:25412.
UCSCi RGD:2375. rat.

Organism-specific databases

CTDi 1280.
RGDi 2375. Col2a1.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
KOi K06236.
PhylomeDBi P05539.

Miscellaneous databases

NextBioi 606543.
PROi P05539.

Gene expression databases

Genevestigatori P05539.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 4 hits.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete rat type II collagen cDNA sequence."
    Urabe K., Sarkar G., Bolander M.E.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone.
  2. "Isolation and characterization of a cDNA clone for the amino-terminal portion of the pro-alpha 1(II) chain of cartilage collagen."
    Kohno K., Martin G.R., Yamada Y.
    J. Biol. Chem. 259:13668-13673(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-122.
  3. "Structure of the promoter of the rat type II procollagen gene."
    Kohno K., Sullivan M., Yamada Y.
    J. Biol. Chem. 260:4441-4447(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 370-422.
    Strain: DA.
    Tissue: Cartilage.
  5. "A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens."
    Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.
    J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT PRO-602; PRO-839; PRO-1076; PRO-1118; PRO-1133; PRO-1139 AND PRO-1145, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCO2A1_RAT
AccessioniPrimary (citable) accession number: P05539
Secondary accession number(s): Q63123, Q63565, Q78DY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 110 of the entry and version 2 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

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