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P08121

- CO3A1_MOUSE

UniProt

P08121 - CO3A1_MOUSE

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Protein

Collagen alpha-1(III) chain

Gene
Col3a1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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 Gna12.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1278 – 12781Calcium By similarity
Metal bindingi1280 – 12801Calcium By similarity
Metal bindingi1281 – 12811Calcium; via carbonyl oxygen By similarity
Metal bindingi1283 – 12831Calcium; via carbonyl oxygen By similarity
Metal bindingi1286 – 12861Calcium By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. aging Source: Ensembl
  2. blood vessel development Source: MGI
  3. cell-matrix adhesion Source: Ensembl
  4. cellular response to amino acid stimulus Source: MGI
  5. cerebral cortex development Source: UniProtKB
  6. collagen biosynthetic process Source: Ensembl
  7. collagen fibril organization Source: MGI
  8. digestive tract development Source: MGI
  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: Ensembl
  18. response to radiation Source: Ensembl
  19. skeletal system development Source: Ensembl
  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_196581. Scavenging by Class A Receptors.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(III) chain
Gene namesi
Name:Col3a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:88453. Col3a1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Neuronal ectopias and abnormal cortical lamination.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 By similarityAdd
BLAST
Propeptidei24 – 154131N-terminal propeptidePRO_0000005743Add
BLAST
Chaini155 – 12191065Collagen alpha-1(III) chainPRO_0000005744Add
BLAST
Propeptidei1220 – 1464245C-terminal propeptidePRO_0000005745Add
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 bondi1260 ↔ 1292 By similarity
Disulfide bondi1266 – 1266Interchain (with C-1283) By similarity
Disulfide bondi1283 – 1283Interchain (with C-1266) By similarity
Disulfide bondi1300 ↔ 1462 By similarity
Disulfide bondi1370 ↔ 1415 By similarity

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP08121.
PaxDbiP08121.
PRIDEiP08121.

PTM databases

PhosphoSiteiP08121.

Expressioni

Tissue specificityi

Expressed in embryonic brain, specifically in the meninges, pial basement membrane and blood vessels (at protein level).1 Publication

Gene expression databases

ArrayExpressiP08121.
BgeeiP08121.
CleanExiMM_COL3A1.
GenevestigatoriP08121.

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

BioGridi198815. 5 interactions.
IntActiP08121. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP08121.
SMRiP08121. Positions 1247-1464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 9060VWFCAdd
BLAST
Domaini1230 – 1464235Fibrillar collagen NC1Add
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.

Sequence similaritiesi

Contains 1 VWFC domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG004933.
InParanoidiP08121.
KOiK06236.
OMAiPGPSGHQ.
OrthoDBiEOG7TJ3HH.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 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.

P08121-1 [UniParc]FASTAAdd to Basket

« Hide

MMSFVQSGTW FLLTLLHPTL ILAQQSNVDE LGCSHLGQSY ESRDVWKPEP     50
CQICVCDSGS VLCDDIICDE EPLDCPNPEI PFGECCAICP QPSTPAPVLP 100
DGHGPQGPKG DPGPPGIPGR NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ 150
NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP PGPPGSSGHP GSPGSPGYQG 200
PPGEPGQAGP AGPPGPPGAL GPAGPAGKDG ESGRPGRPGE RGLPGPPGIK 250
GPAGMPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP 300
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG 350
EVGPAGSPGS NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA 400
GIPGAPGLIG ARGPPGPAGT NGIPGTRGPS GEPGKNGAKG EPGARGERGE 450
AGSPGIPGPK GEDGKDGSPG EPGANGLPGA AGERGPSGFR GPAGPNGIPG 500
EKGPPGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS PGGPGNDGKP 550
GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG 600
PGLPGPAGKN GETGPQGPPG PTGPAGDKGD SGPPGPQGLQ GIPGTGGPPG 650
ENGKPGEPGP KGEVGAPGAP GGKGDSGAPG ERGPPGTAGI PGARGGAGPP 700
GPEGGKGPAG PPGPPGASGS PGLQGMPGER GGPGSPGPKG EKGEPGGAGA 750
DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE GGSPGLPGIA GPRGGPGERG 800
EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGP AGPTGSSGPA 850
GPPGPQGVKG ERGSPGGPGT AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK 900
DGPPGPAGNS GSPGNPGIAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG 950
LTGARGLAGP PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP 1000
GQPGTAGEPG RDGNPGSDGQ PGRDGSPGGK GDRGENGSPG APGAPGHPGP 1050
PGPVGPSGKS GDRGETGPAG PSGAPGPAGA RGAPGPQGPR GDKGETGERG 1100
SNGIKGHRGF PGNPGPPGSP GAAGHQGAIG SPGPAGPRGP VGPHGPPGKD 1150
GTSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA 1200
AAIAGVGGEK SGGFSPYYGD DPMDFKINTE EIMSSLKSVN GQIESLISPD 1250
GSRKNPARNC RDLKFCHPEL KSGEYWVDPN QGCKMDAIKV FCNMETGETC 1300
INASPMTVPR KHWWTDSGAE KKHVWFGESM NGGFQFSYGP PDLPEDVVDV 1350
QLAFLRLLSS RASQNITYHC KNSIAYMDQA SGNVKKSLKL MGSNEGEFKA 1400
EGNSKFTYTV LEDGCTKHTG EWSKTVFEYQ TRKAMRLPII DIAPYDIGGP 1450
DQEFGVDIGP VCFL 1464
Length:1,464
Mass (Da):138,943
Last modified:July 15, 1999 - v4
Checksum:i2104EC27A886090B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52046 Genomic DNA. Translation: CAA36279.1.
BC043089 mRNA. Translation: AAH43089.1.
BC058724 mRNA. Translation: AAH58724.1.
M18933 mRNA. Translation: AAA37338.1.
K03037 Genomic DNA. No translation available.
AK019448 mRNA. Translation: BAB31724.1.
X57983 Genomic DNA. Translation: CAA41048.1.
CCDSiCCDS35554.1.
PIRiA27353.
S59856.
RefSeqiNP_034060.2. NM_009930.2.
UniGeneiMm.249555.

Genome annotation databases

EnsembliENSMUST00000087883; ENSMUSP00000085192; ENSMUSG00000026043.
GeneIDi12825.
KEGGimmu:12825.
UCSCiuc007awq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52046 Genomic DNA. Translation: CAA36279.1 .
BC043089 mRNA. Translation: AAH43089.1 .
BC058724 mRNA. Translation: AAH58724.1 .
M18933 mRNA. Translation: AAA37338.1 .
K03037 Genomic DNA. No translation available.
AK019448 mRNA. Translation: BAB31724.1 .
X57983 Genomic DNA. Translation: CAA41048.1 .
CCDSi CCDS35554.1.
PIRi A27353.
S59856.
RefSeqi NP_034060.2. NM_009930.2.
UniGenei Mm.249555.

3D structure databases

ProteinModelPortali P08121.
SMRi P08121. Positions 1247-1464.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198815. 5 interactions.
IntActi P08121. 2 interactions.

PTM databases

PhosphoSitei P08121.

Proteomic databases

MaxQBi P08121.
PaxDbi P08121.
PRIDEi P08121.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000087883 ; ENSMUSP00000085192 ; ENSMUSG00000026043 .
GeneIDi 12825.
KEGGi mmu:12825.
UCSCi uc007awq.2. mouse.

Organism-specific databases

CTDi 1281.
MGIi MGI:88453. Col3a1.

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG004933.
InParanoidi P08121.
KOi K06236.
OMAi PGPSGHQ.
OrthoDBi EOG7TJ3HH.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_196581. Scavenging by Class A Receptors.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi COL3A1. mouse.
NextBioi 282310.
PROi P08121.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08121.
Bgeei P08121.
CleanExi MM_COL3A1.
Genevestigatori P08121.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 7 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 mouse type-III procollagen-encoding gene: genomic cloning and complete DNA sequence."
    Toman D., de Crombrugghe B.
    Gene 147:161-168(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6 X DBA.
    Tissue: Embryo.
  2. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Complete nucleotide sequence of the N-terminal domains of the murine alpha-1 type-III collagen chain."
    Wood L., Theriault N., Vogeli G.
    Gene 61:225-230(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-488.
  4. "Identification of the promoter and first exon of the mouse alpha 1 (III) collagen gene."
    Liau G., Mudryj M., de Crombrugghe B.
    J. Biol. Chem. 260:3773-3777(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 810-1464.
    Strain: C57BL/6J.
    Tissue: Embryonic head.
  6. "Specific hybridization probes for mouse type I, II, III and IX collagen mRNAs."
    Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.
    Biochim. Biophys. Acta 1089:241-243(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1442-1464.
    Strain: C57BL/6.
  7. "G protein-coupled receptor 56 and collagen III, a receptor-ligand pair, regulates cortical development and lamination."
    Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.
    Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RECEPTOR-BINDING, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCO3A1_MOUSE
AccessioniPrimary (citable) accession number: P08121
Secondary accession number(s): Q61429, Q9CRN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 15, 1999
Last modified: September 3, 2014
This is version 141 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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