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 04-NOV-2026, entry version 136. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; A02862; CGBO7S. DR AlphaFoldDB; P04258; -. DR ComplexPortal; CPX-3106; Collagen type III trimer. DR FunCoup; P04258; 18. DR GlyCosmos; P04258; 2 sites, No reported glycans. DR GlyGen; P04258; 5 sites. DR PeptideAtlas; P04258; -. DR eggNOG; KOG3544; Eukaryota. DR InParanoid; P04258; -. DR OMA; AAYQMYV; -. DR OrthoDB; 8939548at2759; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; NAS:ComplexPortal. 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 PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1. DR Pfam; PF01391; Collagen; 5. 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 22..32 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..46 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..94 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..106 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..121 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 155..166 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..223 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..243 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 244..257 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 361..371 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..393 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..497 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..522 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 539..555 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 562..572 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 573..583 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 667..679 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 680..694 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 708..721 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 754..779 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 790..799 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 890..899 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 913..926 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 967..977 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1025..1037 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 //