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Protein

Collagen alpha-1(III) chain

Gene

COL3A1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Biological processi

  1. cerebral cortex development Source: UniProtKB
  2. negative regulation of neuron migration Source: UniProtKB
  3. positive regulation of Rho protein signal transduction Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_328627. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(III) chain
Gene namesi
Name:COL3A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: Reactome
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10491049Collagen alpha-1(III) chainPRO_0000059398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 9515-hydroxylysine2 Publications
Modified residuei107 – 10715-hydroxylysine2 Publications
Glycosylationi107 – 1071O-linked (Gal...)1 Publication
Modified residuei119 – 11915-hydroxylysine2 Publications
Modified residuei938 – 93815-hydroxylysine2 Publications
Modified residuei950 – 95015-hydroxylysine2 Publications
Glycosylationi950 – 9501O-linked (Gal...)
Disulfide bondi1040 – 1040Interchain
Disulfide bondi1041 – 1041Interchain

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP04258.
PRIDEiP04258.

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

STRINGi9913.ENSBTAP00000028617.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1414Nonhelical region (N-terminal)Add
BLAST
Regioni15 – 10401026Triple-helical regionAdd
BLAST
Regioni1041 – 10499Nonhelical region (C-terminal)

Sequence similaritiesi

Belongs to the fibrillar collagen family.Curated

Keywords - Domaini

Collagen, Repeat

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP04258.

Family and domain databases

InterProiIPR008160. Collagen.
[Graphical view]
PfamiPF01391. Collagen. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04258-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EYEAYDVKSG VAGGGIAGYP GPAGPPGPPG PPGTSGHPGA PGAPGYQGPP
60 70 80 90 100
GEPGQAGPAG PPGPPGAIGP SGKDGESGRP GRPGPRGFPG PPGMKGPAGM
110 120 130 140 150
PGFPGMKGHR GFDGRNGEKG EPGAPGLKGE NGVPGEDGAP GPMGPRGAPG
160 170 180 190 200
ERGRPGLPGA AGARGNDGAR GSDGQPGPPG PPGTAGFPGS PGAKGEVGPA
210 220 230 240 250
GSPGSSGAPG QRGEPGPQGH AGAPGPPGPP GSDGSPGGKG EMGPAGIPGA
260 270 280 290 300
PGLIGARGPP GPPGTNGVPG QRGAAGEPGK NGAKGDPGPR GERGEAGSPG
310 320 330 340 350
IAGPKGEDGK DGSPGEPGAN GLPGAAGERG VPGFRGPAGA NGLPGEKGPP
360 370 380 390 400
GDRGGPGPAG PRGVAGEPGR NGLPGGPGLR GIPGSPGGPG SNGKPGPPGS
410 420 430 440 450
QGETGRPGPP GSPGPRGQPG VMGFPGPKGN DGAPGKNGER GGPGGPGPQG
460 470 480 490 500
PAGKNGETGP QGPPGPTGPS GDKGDTGPPG PQGLQGLPGT SGPPGENGKP
510 520 530 540 550
GEPGPKGEAG APGIPGGKGD SGAPGERGPP GAGGPPGPRG GAGPPGPEGG
560 570 580 590 600
KGAAGPPGPP GSAGTPGLQG MPGERGGPGG PGPKGDKGEP GSSGVDGAPG
610 620 630 640 650
KDGPRGPTGP IGPPGPAGQP GDKGESGAPG VPGIAGPRGG PGERGEQGPP
660 670 680 690 700
GPAGFPGAPG QNGEPGAKGE RGAPGEKGEG GPPGAAGPAG GSGPAGPPGP
710 720 730 740 750
QGVKGERGSP GGPGAAGFPG GRGPPGPPGS NGNPGPPGSS GAPGKDGPPG
760 770 780 790 800
PPGSNGAPGS PGISGPKGDS GPPGERGAPG PQGPPGAPGP LGIAGLTGAR
810 820 830 840 850
GLAGPPGMPG ARGSPGPQGI KGENGKPGPS GQNGERGPPG PQGLPGLAGT
860 870 880 890 900
AGEPGRDGNP GSDGLPGRDG APGAKGDRGE NGSPGAPGAP GHPGPPGPVG
910 920 930 940 950
PAGKSGDRGE TGPAGPSGAP GPAGSRGPPG PQGPRGDKGE TGERGAMGIK
960 970 980 990 1000
GHRGFPGNPG APGSPGPAGH QGAVGSPGPA GPRGPVGPSG PPGKDGASGH
1010 1020 1030 1040
PGPIGPPGPR GNRGERGSEG SPGHPGQPGP PGPPGAPGPC CGAGGVAAI
Length:1,049
Mass (Da):93,651
Last modified:March 19, 1987 - v1
Checksum:i8EEC33D1C66EC9A3
GO

Sequence databases

PIRiA02862. CGBO7S.
UniGeneiBt.64714.

Cross-referencesi

Sequence databases

PIRiA02862. CGBO7S.
UniGeneiBt.64714.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028617.

Proteomic databases

PaxDbiP04258.
PRIDEiP04258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP04258.

Enzyme and pathway databases

ReactomeiREACT_328627. ECM proteoglycans.

Family and domain databases

InterProiIPR008160. Collagen.
[Graphical view]
PfamiPF01391. Collagen. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-242, HYDROXYLATION.
  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(1978) [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(1978) [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(1978) [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(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 809-947, HYDROXYLATION.
  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(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 948-1049, HYDROXYLATION.

Entry informationi

Entry nameiCO3A1_BOVIN
AccessioniPrimary (citable) accession number: P04258
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 1987
Last sequence update: March 19, 1987
Last modified: March 31, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.