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P08121 (CO3A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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(III) chain
Gene names
Name:Col3a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed in embryonic brain, specifically in the meninges, pial basement membrane and blood vessels (at protein level). Ref.7

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

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.

Disruption phenotype

Neuronal ectopias and abnormal cortical lamination. Ref.7

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

blood vessel development

Inferred from mutant phenotype PubMed 9050868. Source: MGI

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

cerebral cortex development

Inferred from mutant phenotype Ref.7. Source: UniProtKB

collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Inferred from mutant phenotype PubMed 9050868. Source: MGI

digestive tract development

Inferred from mutant phenotype PubMed 9050868. Source: MGI

extracellular fibril organization

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron migration

Inferred from mutant phenotype Ref.7. Source: UniProtKB

peptide cross-linking

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho protein signal transduction

Inferred from direct assay Ref.7. Source: UniProtKB

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcollagen

Inferred from direct assay PubMed 17662583PubMed 8686743. Source: MGI

collagen type III

Inferred from direct assay PubMed 7825727. Source: MGI

extracellular matrix

Inferred from direct assay PubMed 10022501PubMed 2209468PubMed 8984825. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSMAD binding

Inferred from physical interaction PubMed 14559231. Source: MGI

extracellular matrix structural constituent

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Propeptide24 – 154131N-terminal propeptide
PRO_0000005743
Chain155 – 12191065Collagen alpha-1(III) chain
PRO_0000005744
Propeptide1220 – 1464245C-terminal propeptide
PRO_0000005745

Regions

Domain31 – 9060VWFC
Domain1230 – 1464235Fibrillar collagen NC1
Region155 – 16915Nonhelical region (N-terminal)
Region170 – 11951026Triple-helical region

Sites

Metal binding12781Calcium By similarity
Metal binding12801Calcium By similarity
Metal binding12811Calcium; via carbonyl oxygen By similarity
Metal binding12831Calcium; via carbonyl oxygen By similarity
Metal binding12861Calcium By similarity

Amino acid modifications

Modified residue26215-hydroxylysine; alternate By similarity
Modified residue28315-hydroxylysine By similarity
Modified residue85915-hydroxylysine By similarity
Modified residue97615-hydroxylysine By similarity
Modified residue109315-hydroxylysine By similarity
Modified residue110515-hydroxylysine By similarity
Glycosylation2621O-linked (Gal...); alternate By similarity
Disulfide bond1195Interchain By similarity
Disulfide bond1196Interchain By similarity
Disulfide bond1260 ↔ 1292 By similarity
Disulfide bond1266Interchain (with C-1283) By similarity
Disulfide bond1283Interchain (with C-1266) By similarity
Disulfide bond1300 ↔ 1462 By similarity
Disulfide bond1370 ↔ 1415 By similarity

Sequences

Sequence LengthMass (Da)Tools
P08121 [UniParc].

Last modified July 15, 1999. Version 4.
Checksum: 2104EC27A886090B

FASTA1,464138,943
        10         20         30         40         50         60 
MMSFVQSGTW FLLTLLHPTL ILAQQSNVDE LGCSHLGQSY ESRDVWKPEP CQICVCDSGS 

        70         80         90        100        110        120 
VLCDDIICDE EPLDCPNPEI PFGECCAICP QPSTPAPVLP DGHGPQGPKG DPGPPGIPGR 

       130        140        150        160        170        180 
NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP 

       190        200        210        220        230        240 
PGPPGSSGHP GSPGSPGYQG PPGEPGQAGP AGPPGPPGAL GPAGPAGKDG ESGRPGRPGE 

       250        260        270        280        290        300 
RGLPGPPGIK GPAGMPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP 

       310        320        330        340        350        360 
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG EVGPAGSPGS 

       370        380        390        400        410        420 
NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA GIPGAPGLIG ARGPPGPAGT 

       430        440        450        460        470        480 
NGIPGTRGPS GEPGKNGAKG EPGARGERGE AGSPGIPGPK GEDGKDGSPG EPGANGLPGA 

       490        500        510        520        530        540 
AGERGPSGFR GPAGPNGIPG EKGPPGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS 

       550        560        570        580        590        600 
PGGPGNDGKP GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG 

       610        620        630        640        650        660 
PGLPGPAGKN GETGPQGPPG PTGPAGDKGD SGPPGPQGLQ GIPGTGGPPG ENGKPGEPGP 

       670        680        690        700        710        720 
KGEVGAPGAP GGKGDSGAPG ERGPPGTAGI PGARGGAGPP GPEGGKGPAG PPGPPGASGS 

       730        740        750        760        770        780 
PGLQGMPGER GGPGSPGPKG EKGEPGGAGA DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE 

       790        800        810        820        830        840 
GGSPGLPGIA GPRGGPGERG EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGP 

       850        860        870        880        890        900 
AGPTGSSGPA GPPGPQGVKG ERGSPGGPGT AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK 

       910        920        930        940        950        960 
DGPPGPAGNS GSPGNPGIAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG LTGARGLAGP 

       970        980        990       1000       1010       1020 
PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP GQPGTAGEPG RDGNPGSDGQ 

      1030       1040       1050       1060       1070       1080 
PGRDGSPGGK GDRGENGSPG APGAPGHPGP PGPVGPSGKS GDRGETGPAG PSGAPGPAGA 

      1090       1100       1110       1120       1130       1140 
RGAPGPQGPR GDKGETGERG SNGIKGHRGF PGNPGPPGSP GAAGHQGAIG SPGPAGPRGP 

      1150       1160       1170       1180       1190       1200 
VGPHGPPGKD GTSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA 

      1210       1220       1230       1240       1250       1260 
AAIAGVGGEK SGGFSPYYGD DPMDFKINTE EIMSSLKSVN GQIESLISPD GSRKNPARNC 

      1270       1280       1290       1300       1310       1320 
RDLKFCHPEL KSGEYWVDPN QGCKMDAIKV FCNMETGETC INASPMTVPR KHWWTDSGAE 

      1330       1340       1350       1360       1370       1380 
KKHVWFGESM NGGFQFSYGP PDLPEDVVDV QLAFLRLLSS RASQNITYHC KNSIAYMDQA 

      1390       1400       1410       1420       1430       1440 
SGNVKKSLKL MGSNEGEFKA EGNSKFTYTV LEDGCTKHTG EWSKTVFEYQ TRKAMRLPII 

      1450       1460 
DIAPYDIGGP DQEFGVDIGP VCFL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA27353.
S59856.
RefSeqNP_034060.2. NM_009930.2.
UniGeneMm.249555.

3D structure databases

ProteinModelPortalP08121.
SMRP08121. Positions 28-95, 1247-1464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198815. 5 interactions.
IntActP08121. 2 interactions.

PTM databases

PhosphoSiteP08121.

Proteomic databases

PaxDbP08121.
PRIDEP08121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087883; ENSMUSP00000085192; ENSMUSG00000026043.
GeneID12825.
KEGGmmu:12825.
UCSCuc007awq.2. mouse.

Organism-specific databases

CTD1281.
MGIMGI:88453. Col3a1.

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
InParanoidP08121.
KOK06236.
OMAPGPSGHQ.
OrthoDBEOG7TJ3HH.
TreeFamTF344135.

Gene expression databases

ArrayExpressP08121.
BgeeP08121.
CleanExMM_COL3A1.
GenevestigatorP08121.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 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...

Other

ChiTaRSCOL3A1. mouse.
NextBio282310.
PROP08121.
SOURCESearch...

Entry information

Entry nameCO3A1_MOUSE
AccessionPrimary (citable) accession number: P08121
Secondary accession number(s): Q61429, Q9CRN7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 15, 1999
Last modified: April 16, 2014
This is version 137 of the entry and version 4 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot