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P04258 (CO3A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Collagen alpha-1(III) chain
Gene names
Name:COL3A1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1049 AA.
Sequence statusComplete.
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 By similarity.

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.

Post-translational modification

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

Sequence similarities

Belongs to the fibrillar collagen family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10491049Collagen alpha-1(III) chain
PRO_0000059398

Regions

Region1 – 1414Nonhelical region (N-terminal)
Region15 – 10401026Triple-helical region
Region1041 – 10499Nonhelical region (C-terminal)

Amino acid modifications

Modified residue9515-hydroxylysine Ref.1 Ref.6
Modified residue10715-hydroxylysine Ref.1 Ref.6
Modified residue11915-hydroxylysine Ref.1 Ref.6
Modified residue93815-hydroxylysine Ref.1 Ref.6
Modified residue95015-hydroxylysine Ref.1 Ref.6
Glycosylation1071O-linked (Gal...) Ref.1
Glycosylation9501O-linked (Gal...)
Disulfide bond1040Interchain
Disulfide bond1041Interchain

Sequences

Sequence LengthMass (Da)Tools
P04258 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 8EEC33D1C66EC9A3

FASTA1,04993,651
        10         20         30         40         50         60 
EYEAYDVKSG VAGGGIAGYP GPAGPPGPPG PPGTSGHPGA PGAPGYQGPP GEPGQAGPAG 

        70         80         90        100        110        120 
PPGPPGAIGP SGKDGESGRP GRPGPRGFPG PPGMKGPAGM PGFPGMKGHR GFDGRNGEKG 

       130        140        150        160        170        180 
EPGAPGLKGE NGVPGEDGAP GPMGPRGAPG ERGRPGLPGA AGARGNDGAR GSDGQPGPPG 

       190        200        210        220        230        240 
PPGTAGFPGS PGAKGEVGPA GSPGSSGAPG QRGEPGPQGH AGAPGPPGPP GSDGSPGGKG 

       250        260        270        280        290        300 
EMGPAGIPGA PGLIGARGPP GPPGTNGVPG QRGAAGEPGK NGAKGDPGPR GERGEAGSPG 

       310        320        330        340        350        360 
IAGPKGEDGK DGSPGEPGAN GLPGAAGERG VPGFRGPAGA NGLPGEKGPP GDRGGPGPAG 

       370        380        390        400        410        420 
PRGVAGEPGR NGLPGGPGLR GIPGSPGGPG SNGKPGPPGS QGETGRPGPP GSPGPRGQPG 

       430        440        450        460        470        480 
VMGFPGPKGN DGAPGKNGER GGPGGPGPQG PAGKNGETGP QGPPGPTGPS GDKGDTGPPG 

       490        500        510        520        530        540 
PQGLQGLPGT SGPPGENGKP GEPGPKGEAG APGIPGGKGD SGAPGERGPP GAGGPPGPRG 

       550        560        570        580        590        600 
GAGPPGPEGG KGAAGPPGPP GSAGTPGLQG MPGERGGPGG PGPKGDKGEP GSSGVDGAPG 

       610        620        630        640        650        660 
KDGPRGPTGP IGPPGPAGQP GDKGESGAPG VPGIAGPRGG PGERGEQGPP GPAGFPGAPG 

       670        680        690        700        710        720 
QNGEPGAKGE RGAPGEKGEG GPPGAAGPAG GSGPAGPPGP QGVKGERGSP GGPGAAGFPG 

       730        740        750        760        770        780 
GRGPPGPPGS NGNPGPPGSS GAPGKDGPPG PPGSNGAPGS PGISGPKGDS GPPGERGAPG 

       790        800        810        820        830        840 
PQGPPGAPGP LGIAGLTGAR GLAGPPGMPG ARGSPGPQGI KGENGKPGPS GQNGERGPPG 

       850        860        870        880        890        900 
PQGLPGLAGT AGEPGRDGNP GSDGLPGRDG APGAKGDRGE NGSPGAPGAP GHPGPPGPVG 

       910        920        930        940        950        960 
PAGKSGDRGE TGPAGPSGAP GPAGSRGPPG PQGPRGDKGE TGERGAMGIK GHRGFPGNPG 

       970        980        990       1000       1010       1020 
APGSPGPAGH QGAVGSPGPA GPRGPVGPSG PPGKDGASGH PGPIGPPGPR GNRGERGSEG 

      1030       1040 
SPGHPGQPGP PGPPGAPGPC CGAGGVAAI 

« Hide

References

[1]"The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (positions 1-222)."
Fietzek P.P., Allmann H., Rauterberg J., Henkel W., Wachter E., Kuhn K.
Hoppe-Seyler's Z. Physiol. Chem. 360:809-820(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-242.
[2]"The covalent structure of calf skin type III collagen. II. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB1,8,10,2 (positions 223-402)."
Dewes H., Fietzek P.P., Kuhn K.
Hoppe-Seyler's Z. Physiol. Chem. 360:821-832(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 243-422.
[3]"The covalent structure of calf skin type III collagen. III. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB4 (positions 403-551)."
Bentz H., Fietzek P.P., Kuhn K.
Hoppe-Seyler's Z. Physiol. Chem. 360:833-840(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 423-571.
[4]"The covalent structure of calf skin type III collagen. IV. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB5 (positions 552-788)."
Lang H., Glanville R.W., Fietzek P.P., Kuhn K.
Hoppe-Seyler's Z. Physiol. Chem. 360:841-850(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 572-808.
[5]"The covalent structure of calf skin type III collagen. V. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB9A (position 789-927)."
Dewes H., Fietzek P.P., Kuhn K.
Hoppe-Seyler's Z. Physiol. Chem. 360:851-860(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 809-947.
[6]"The covalent structure of calf skin type III collagen. VI. The amino acid sequence of the carboxyterminal cyanogen bromide peptide alpha 1(III)CB9B (positions 928-1028)."
Allmann H., Fietzek P.P., Glanville R.W., Kuhn K.
Hoppe-Seyler's Z. Physiol. Chem. 360:861-868(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 948-1049.

Cross-references

Sequence databases

PIRCGBO7S. A02862.
UniGeneBt.64714.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000028617.

Proteomic databases

PaxDbP04258.
PRIDEP04258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085654.
HOVERGENHBG004933.

Family and domain databases

InterProIPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 7 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCO3A1_BOVIN
AccessionPrimary (citable) accession number: P04258
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: March 19, 2014
This is version 85 of the entry and version 1 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