Skip Header

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

P13941

- CO3A1_RAT

UniProt

P13941 - CO3A1_RAT

(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(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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1277 – 12771CalciumBy similarity
Metal bindingi1279 – 12791CalciumBy similarity
Metal bindingi1280 – 12801Calcium; via carbonyl oxygenBy similarity
Metal bindingi1282 – 12821Calcium; via carbonyl oxygenBy similarity
Metal bindingi1285 – 12851CalciumBy 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 fibril organization Source: Ensembl
  7. digestive tract development Source: Ensembl
  8. extracellular fibril organization Source: Ensembl
  9. heart development Source: Ensembl
  10. integrin-mediated signaling pathway Source: Ensembl
  11. negative regulation of immune response Source: Ensembl
  12. negative regulation of neuron migration Source: UniProtKB
  13. peptide cross-linking Source: Ensembl
  14. positive regulation of Rho protein signal transduction Source: UniProtKB
  15. response to cytokine Source: Ensembl
  16. response to mechanical stimulus Source: RGD
  17. response to radiation Source: Ensembl
  18. skeletal system development Source: RGD
  19. skin development Source: Ensembl
  20. transforming growth factor beta receptor signaling pathway Source: Ensembl
  21. 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.
REACT_231038. NCAM1 interactions.
REACT_252097. Integrin cell surface interactions.

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

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

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 – 2323By similarityAdd
BLAST
Propeptidei24 – 154131N-terminal propeptideBy similarityPRO_0000005746Add
BLAST
Chaini155 – 12181064Collagen alpha-1(III) chainPRO_0000005747Add
BLAST
Propeptidei1219 – 1463245C-terminal propeptideBy similarityPRO_0000043408Add
BLAST

Amino acid modifications

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

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 9060VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1229 – 1463235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

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

eggNOGiNOG12793.
GeneTreeiENSGT00770000120467.
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

        10         20         30         40         50
MMSFVQCGTW FLLTLLHPSL ILAQQSNVDE LGCNYLGQSY ESRDVWKPEP
60 70 80 90 100
CQICVCDSGS VLCDDIMCDD EPLDCPNPEI PFGECCAICP QPSTPAPVIP
110 120 130 140 150
DGNRPQGPKG DPGPPGIPGR NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ
160 170 180 190 200
NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP PGPPGSSGHP GSPGSPGYQG
210 220 230 240 250
PPGEPGQAGP AGPPGPPGAI GPSGPAGKDG ESGRPGRPGE RGLPGPPGIK
260 270 280 290 300
GPAGIPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP
310 320 330 340 350
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG
360 370 380 390 400
EVGPAGSPGS NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA
410 420 430 440 450
GIPGAPGLLG ARGPPGPAGA NGAPGQRGPS GEPGKNGAKG EPGARGERGE
460 470 480 490 500
AGSPGIPGPK GEDGKDGSPG EPGANGVPGN PGERGAPGFR GPAGPNGAPG
510 520 530 540 550
EKGPAGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS PGGPGNDGKP
560 570 580 590 600
GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG
610 620 630 640 650
PGLPGPAGKN GETGPQGPPG PTGAPGDKGD AGPPGPQGLQ GIPGTSGPPG
660 670 680 690 700
ENGKPGEPGP KGEAGAPGVP GGKGDSGAPG ERGPPGTAGT PGLRGGAGPP
710 720 730 740 750
GPEGGKGPAG PPGPPGTSGP PGLQGMPGER GGPGSPGPKG EKGEPGGAGA
760 770 780 790 800
DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE GGAPGLPGIA GPRGGPGERG
810 820 830 840 850
EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGA AGPPGGSGPA
860 870 880 890 900
GPPGPQGVKG ERGSPGGPGA AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK
910 920 930 940 950
DGPPGPAGNS GSPGNPGVAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG
960 970 980 990 1000
LTGARGLAGP PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP
1010 1020 1030 1040 1050
GQPGTAGEPG RDGNPGSDGQ PGRDGSPGGK GDRGENGSPG APGAPGHPGP
1060 1070 1080 1090 1100
PGPVGPSGKN GDRGETGPAG PSGAPGPAGA RGAPGPQGPR GDKGETGERG
1110 1120 1130 1140 1150
SNGIKGHRGF PGNPGPPGSP GAAGHQGAVG SPGPAGPRGP VGPHGPPGKD
1160 1170 1180 1190 1200
GSSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA
1210 1220 1230 1240 1250
AIAGVGGEKS GGFSPYYGDD PMDFKINTEE IMSSLKSVNG QIESLISPDG
1260 1270 1280 1290 1300
SRKNPARNCR DLKFCHPELK SGEYWVDPNQ GCKMDAIKVF CNMETGETCI
1310 1320 1330 1340 1350
NASPMTVPRK HWWTDAGAEK KHVWFGESMN GGFQFSYGNP DLPEDVLDVQ
1360 1370 1380 1390 1400
LAFLRLLSSR ASQNITYHCK NSIAYMDQAN GNVKKSLKLM GSNEGEFKAE
1410 1420 1430 1440 1450
GNSKFTYTVL EDGCTKHTGE WSKTVFEYQT RKAMRLPIID IAPYDIGGPD
1460
QEFGVDIGPV CFL
Length:1,463
Mass (Da):138,936
Last modified:December 6, 2005 - v3
Checksum:i63C218CD2BCA47B6
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00770000120467.
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.
REACT_231038. NCAM1 interactions.
REACT_252097. Integrin cell surface interactions.

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: November 26, 2014
This is version 124 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