CO3A1_BOVIN
ID CO3A1_BOVIN Reviewed; 1049 AA.
AC P04258;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Collagen alpha-1(III) chain;
GN Name=COL3A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE OF 1-242, AND HYDROXYLATION AT LYS-95; LYS-107; LYS-119;
RP LYS-938 AND LYS-950.
RX PubMed=488906; DOI=10.1515/bchm2.1979.360.2.809;
RA Fietzek P.P., Allmann H., Rauterberg J., Henkel W., Wachter E., Kuhn K.;
RT "The covalent structure of calf skin type III collagen. I. The amino acid
RT sequence of the amino terminal region of the alpha 1(III) chain (positions
RT 1-222).";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:809-820(1979).
RN [2]
RP PROTEIN SEQUENCE OF 243-422.
RX PubMed=488907;
RA Dewes H., Fietzek P.P., Kuhn K.;
RT "The covalent structure of calf skin type III collagen. II. The amino acid
RT sequence of the cyanogen bromide peptide alpha 1(III)CB1,8,10,2 (positions
RT 223-402).";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:821-832(1979).
RN [3]
RP PROTEIN SEQUENCE OF 423-571.
RX PubMed=488908;
RA Bentz H., Fietzek P.P., Kuhn K.;
RT "The covalent structure of calf skin type III collagen. III. The amino acid
RT sequence of the cyanogen bromide peptide alpha 1(III)CB4 (positions 403-
RT 551).";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:833-840(1979).
RN [4]
RP PROTEIN SEQUENCE OF 572-808.
RX PubMed=488909;
RA Lang H., Glanville R.W., Fietzek P.P., Kuhn K.;
RT "The covalent structure of calf skin type III collagen. IV. The amino acid
RT sequence of the cyanogen bromide peptide alpha 1(III)CB5 (positions 552-
RT 788).";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:841-850(1979).
RN [5]
RP PROTEIN SEQUENCE OF 809-947, AND HYDROXYLATION AT LYS-95; LYS-107; LYS-119;
RP LYS-938 AND LYS-950.
RX PubMed=488910;
RA Dewes H., Fietzek P.P., Kuhn K.;
RT "The covalent structure of calf skin type III collagen. V. The amino acid
RT sequence of the cyanogen bromide peptide alpha 1(III)CB9A (position 789-
RT 927).";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:851-860(1979).
RN [6]
RP PROTEIN SEQUENCE OF 948-1049, AND HYDROXYLATION.
RX PubMed=488911;
RA Allmann H., Fietzek P.P., Glanville R.W., Kuhn K.;
RT "The covalent structure of calf skin type III collagen. VI. The amino acid
RT sequence of the carboxyterminal cyanogen bromide peptide alpha 1(III)CB9B
RT (positions 928-1028).";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:861-868(1979).
CC -!- FUNCTION: Collagen type III occurs in most soft connective tissues
CC along with type I collagen. Involved in regulation of cortical
CC development. Is the major ligand of ADGRG1 in the developing brain and
CC binding to ADGRG1 inhibits neuronal migration and activates the RhoA
CC pathway by coupling ADGRG1 to GNA13 and possibly GNA12 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Trimers of identical alpha 1(III) chains. The chains are
CC linked to each other by interchain disulfide bonds. Trimers are also
CC cross-linked via hydroxylysines. Interacts with ADGRG1 (By similarity).
CC {ECO:0000250|UniProtKB:P02461}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC {ECO:0000269|PubMed:488906, ECO:0000269|PubMed:488910,
CC ECO:0000269|PubMed:488911}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family. {ECO:0000305}.
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DR PIR; A02862; CGBO7S.
DR AlphaFoldDB; P04258; -.
DR ComplexPortal; CPX-3106; Collagen type III trimer.
DR PeptideAtlas; P04258; -.
DR PRIDE; P04258; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P04258; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 4.
PE 1: Evidence at protein level;
KW Collagen; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted.
FT CHAIN 1..1049
FT /note="Collagen alpha-1(III) chain"
FT /id="PRO_0000059398"
FT REGION 1..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..14
FT /note="Nonhelical region (N-terminal)"
FT REGION 15..1040
FT /note="Triple-helical region"
FT REGION 1041..1049
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 21..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:488906,
FT ECO:0000269|PubMed:488911"
FT MOD_RES 107
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:488906,
FT ECO:0000269|PubMed:488911"
FT MOD_RES 119
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:488906,
FT ECO:0000269|PubMed:488911"
FT MOD_RES 938
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:488906,
FT ECO:0000269|PubMed:488911"
FT MOD_RES 950
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:488906,
FT ECO:0000269|PubMed:488911"
FT CARBOHYD 107
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:488906"
FT CARBOHYD 950
FT /note="O-linked (Gal...) hydroxylysine"
FT DISULFID 1040
FT /note="Interchain"
FT DISULFID 1041
FT /note="Interchain"
SQ SEQUENCE 1049 AA; 93651 MW; 8EEC33D1C66EC9A3 CRC64;
EYEAYDVKSG VAGGGIAGYP GPAGPPGPPG PPGTSGHPGA PGAPGYQGPP GEPGQAGPAG
PPGPPGAIGP SGKDGESGRP GRPGPRGFPG PPGMKGPAGM PGFPGMKGHR GFDGRNGEKG
EPGAPGLKGE NGVPGEDGAP GPMGPRGAPG ERGRPGLPGA AGARGNDGAR GSDGQPGPPG
PPGTAGFPGS PGAKGEVGPA GSPGSSGAPG QRGEPGPQGH AGAPGPPGPP GSDGSPGGKG
EMGPAGIPGA PGLIGARGPP GPPGTNGVPG QRGAAGEPGK NGAKGDPGPR GERGEAGSPG
IAGPKGEDGK DGSPGEPGAN GLPGAAGERG VPGFRGPAGA NGLPGEKGPP GDRGGPGPAG
PRGVAGEPGR NGLPGGPGLR GIPGSPGGPG SNGKPGPPGS QGETGRPGPP GSPGPRGQPG
VMGFPGPKGN DGAPGKNGER GGPGGPGPQG PAGKNGETGP QGPPGPTGPS GDKGDTGPPG
PQGLQGLPGT SGPPGENGKP GEPGPKGEAG APGIPGGKGD SGAPGERGPP GAGGPPGPRG
GAGPPGPEGG KGAAGPPGPP GSAGTPGLQG MPGERGGPGG PGPKGDKGEP GSSGVDGAPG
KDGPRGPTGP IGPPGPAGQP GDKGESGAPG VPGIAGPRGG PGERGEQGPP GPAGFPGAPG
QNGEPGAKGE RGAPGEKGEG GPPGAAGPAG GSGPAGPPGP QGVKGERGSP GGPGAAGFPG
GRGPPGPPGS NGNPGPPGSS GAPGKDGPPG PPGSNGAPGS PGISGPKGDS GPPGERGAPG
PQGPPGAPGP LGIAGLTGAR GLAGPPGMPG ARGSPGPQGI KGENGKPGPS GQNGERGPPG
PQGLPGLAGT AGEPGRDGNP GSDGLPGRDG APGAKGDRGE NGSPGAPGAP GHPGPPGPVG
PAGKSGDRGE TGPAGPSGAP GPAGSRGPPG PQGPRGDKGE TGERGAMGIK GHRGFPGNPG
APGSPGPAGH QGAVGSPGPA GPRGPVGPSG PPGKDGASGH PGPIGPPGPR GNRGERGSEG
SPGHPGQPGP PGPPGAPGPC CGAGGVAAI
