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P13941

- CO3A1_RAT

UniProt

P13941 - CO3A1_RAT

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Protein
Collagen alpha-1(III) chain
Gene
Col3a1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of Gpr56 in the developing brain and binding to Gpr56 inhibits neuronal migration and activates the RhoA pathway by coupling Gpr56 to Gna13 and possibly Gna12 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1277 – 12771Calcium By similarity
Metal bindingi1279 – 12791Calcium By similarity
Metal bindingi1280 – 12801Calcium; via carbonyl oxygen By similarity
Metal bindingi1282 – 12821Calcium; via carbonyl oxygen By similarity
Metal bindingi1285 – 12851Calcium By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. aging Source: RGD
  2. blood vessel development Source: Ensembl
  3. cell-matrix adhesion Source: Ensembl
  4. cellular response to amino acid stimulus Source: Ensembl
  5. cerebral cortex development Source: UniProtKB
  6. collagen biosynthetic process Source: Ensembl
  7. collagen fibril organization Source: Ensembl
  8. digestive tract development Source: Ensembl
  9. extracellular fibril organization Source: Ensembl
  10. heart development Source: Ensembl
  11. integrin-mediated signaling pathway Source: Ensembl
  12. negative regulation of immune response Source: Ensembl
  13. negative regulation of neuron migration Source: UniProtKB
  14. peptide cross-linking Source: Ensembl
  15. positive regulation of Rho protein signal transduction Source: UniProtKB
  16. response to cytokine Source: Ensembl
  17. response to mechanical stimulus Source: RGD
  18. response to radiation Source: Ensembl
  19. skeletal system development Source: RGD
  20. skin development Source: Ensembl
  21. transforming growth factor beta receptor signaling pathway Source: Ensembl
  22. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_195275. Extracellular matrix organization.
REACT_198300. Syndecan interactions.
REACT_198584. Collagen biosynthesis and modifying enzymes.
REACT_198733. Scavenging by Class A Receptors.
REACT_198756. Non-integrin membrane-ECM interactions.
REACT_198757. ECM proteoglycans.
REACT_199129. Assembly of collagen fibrils and other multimeric structures.
REACT_199177. Collagen degradation.
REACT_212371. Signaling by PDGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(III) chain
Gene namesi
Name:Col3a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi71029. Col3a1.

Subcellular locationi

GO - Cellular componenti

  1. collagen type III trimer Source: Ensembl
  2. extracellular matrix Source: RGD
  3. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 By similarity
Add
BLAST
Propeptidei24 – 154131N-terminal propeptide By similarity
PRO_0000005746Add
BLAST
Chaini155 – 12181064Collagen alpha-1(III) chain
PRO_0000005747Add
BLAST
Propeptidei1219 – 1463245C-terminal propeptide By similarity
PRO_0000043408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 26215-hydroxylysine; alternate By similarity
Glycosylationi262 – 2621O-linked (Gal...); alternate By similarity
Modified residuei283 – 28315-hydroxylysine By similarity
Modified residuei859 – 85915-hydroxylysine By similarity
Modified residuei976 – 97615-hydroxylysine By similarity
Modified residuei1093 – 109315-hydroxylysine By similarity
Modified residuei1105 – 110515-hydroxylysine By similarity
Disulfide bondi1195 – 1195Interchain By similarity
Disulfide bondi1196 – 1196Interchain By similarity
Disulfide bondi1259 ↔ 1291 By similarity
Disulfide bondi1265 – 1265Interchain (with C-1282) By similarity
Disulfide bondi1282 – 1282Interchain (with C-1265) By similarity
Disulfide bondi1299 ↔ 1461 By similarity
Disulfide bondi1369 ↔ 1414 By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP13941.
PRIDEiP13941.

Expressioni

Gene expression databases

GenevestigatoriP13941.

Interactioni

Subunit structurei

Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.

Protein-protein interaction databases

IntActiP13941. 1 interaction.
STRINGi10116.ENSRNOP00000004956.

Structurei

3D structure databases

ProteinModelPortaliP13941.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 9060VWFC
Add
BLAST
Domaini1229 – 1463235Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni155 – 16915Nonhelical region (N-terminal)
Add
BLAST
Regioni170 – 11951026Triple-helical region
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

eggNOGiNOG12793.
GeneTreeiENSGT00740000114967.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP13941.
KOiK06236.
OMAiKYVWFGE.
OrthoDBiEOG7TJ3HH.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 4 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.

P13941-1 [UniParc]FASTAAdd to Basket

« Hide

MMSFVQCGTW FLLTLLHPSL ILAQQSNVDE LGCNYLGQSY ESRDVWKPEP     50
CQICVCDSGS VLCDDIMCDD EPLDCPNPEI PFGECCAICP QPSTPAPVIP 100
DGNRPQGPKG DPGPPGIPGR NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ 150
NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP PGPPGSSGHP GSPGSPGYQG 200
PPGEPGQAGP AGPPGPPGAI GPSGPAGKDG ESGRPGRPGE RGLPGPPGIK 250
GPAGIPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP 300
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG 350
EVGPAGSPGS NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA 400
GIPGAPGLLG ARGPPGPAGA NGAPGQRGPS GEPGKNGAKG EPGARGERGE 450
AGSPGIPGPK GEDGKDGSPG EPGANGVPGN PGERGAPGFR GPAGPNGAPG 500
EKGPAGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS PGGPGNDGKP 550
GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG 600
PGLPGPAGKN GETGPQGPPG PTGAPGDKGD AGPPGPQGLQ GIPGTSGPPG 650
ENGKPGEPGP KGEAGAPGVP GGKGDSGAPG ERGPPGTAGT PGLRGGAGPP 700
GPEGGKGPAG PPGPPGTSGP PGLQGMPGER GGPGSPGPKG EKGEPGGAGA 750
DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE GGAPGLPGIA GPRGGPGERG 800
EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGA AGPPGGSGPA 850
GPPGPQGVKG ERGSPGGPGA AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK 900
DGPPGPAGNS GSPGNPGVAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG 950
LTGARGLAGP PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP 1000
GQPGTAGEPG RDGNPGSDGQ PGRDGSPGGK GDRGENGSPG APGAPGHPGP 1050
PGPVGPSGKN GDRGETGPAG PSGAPGPAGA RGAPGPQGPR GDKGETGERG 1100
SNGIKGHRGF PGNPGPPGSP GAAGHQGAVG SPGPAGPRGP VGPHGPPGKD 1150
GSSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA 1200
AIAGVGGEKS GGFSPYYGDD PMDFKINTEE IMSSLKSVNG QIESLISPDG 1250
SRKNPARNCR DLKFCHPELK SGEYWVDPNQ GCKMDAIKVF CNMETGETCI 1300
NASPMTVPRK HWWTDAGAEK KHVWFGESMN GGFQFSYGNP DLPEDVLDVQ 1350
LAFLRLLSSR ASQNITYHCK NSIAYMDQAN GNVKKSLKLM GSNEGEFKAE 1400
GNSKFTYTVL EDGCTKHTGE WSKTVFEYQT RKAMRLPIID IAPYDIGGPD 1450
QEFGVDIGPV CFL 1463
Length:1,463
Mass (Da):138,936
Last modified:December 6, 2005 - v3
Checksum:i63C218CD2BCA47B6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1167 – 11671N → D in CAA06510. 1 Publication
Sequence conflicti1256 – 12561A → G in CAA06510. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC087039 mRNA. Translation: AAH87039.1.
X70369 mRNA. Translation: CAA49832.1.
AJ005395 mRNA. Translation: CAA06510.1.
M21354 mRNA. Translation: AAA40942.1.
PIRiS41067.
RefSeqiNP_114474.1. NM_032085.1.
UniGeneiRn.3247.

Genome annotation databases

EnsembliENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357.
GeneIDi84032.
KEGGirno:84032.
UCSCiRGD:71029. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC087039 mRNA. Translation: AAH87039.1 .
X70369 mRNA. Translation: CAA49832.1 .
AJ005395 mRNA. Translation: CAA06510.1 .
M21354 mRNA. Translation: AAA40942.1 .
PIRi S41067.
RefSeqi NP_114474.1. NM_032085.1.
UniGenei Rn.3247.

3D structure databases

ProteinModelPortali P13941.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13941. 1 interaction.
STRINGi 10116.ENSRNOP00000004956.

Proteomic databases

PaxDbi P13941.
PRIDEi P13941.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000004956 ; ENSRNOP00000004956 ; ENSRNOG00000003357 .
GeneIDi 84032.
KEGGi rno:84032.
UCSCi RGD:71029. rat.

Organism-specific databases

CTDi 1281.
RGDi 71029. Col3a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00740000114967.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi P13941.
KOi K06236.
OMAi KYVWFGE.
OrthoDBi EOG7TJ3HH.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_195275. Extracellular matrix organization.
REACT_198300. Syndecan interactions.
REACT_198584. Collagen biosynthesis and modifying enzymes.
REACT_198733. Scavenging by Class A Receptors.
REACT_198756. Non-integrin membrane-ECM interactions.
REACT_198757. ECM proteoglycans.
REACT_199129. Assembly of collagen fibrils and other multimeric structures.
REACT_199177. Collagen degradation.
REACT_212371. Signaling by PDGF.

Miscellaneous databases

NextBioi 616623.
PROi P13941.

Gene expression databases

Genevestigatori P13941.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 4 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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  2. "Cloning of cDNA for rat pro alpha 1(III) collagen mRNA. Different expression patterns of type I and type III collagen and fibronectin genes in experimental granulation tissue."
    Glumoff V., Maekelae J.K., Vuorio E.
    Biochim. Biophys. Acta 1217:41-48(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 828-1463.
  3. Wurtz T., Ellerstroem C., Lundmark C., Christersson C.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 900-1463.
    Strain: Sprague-Dawley.
    Tissue: Fibroblast.
  4. "Regulation of alpha 2(I), alpha 1(III), and alpha 2(V) collagen mRNAs by estradiol in the immature rat uterus."
    Frankel F.R., Hsu C.-Y.J., Meyers J.C., Lin E., Lyttle C.R., Komm B., Mohn K.
    DNA 7:347-354(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1135-1309.

Entry informationi

Entry nameiCO3A1_RAT
AccessioniPrimary (citable) accession number: P13941
Secondary accession number(s): O70604, Q5PQT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 6, 2005
Last modified: September 3, 2014
This is version 121 of the entry and version 3 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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