ID   CO3A1_CHICK             Reviewed;        1262 AA.
AC   P12105; P79758; P79759; Q90790; Q90791; Q90794; Q92029;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   02-SEP-2026, entry version 143.
DE   RecName: Full=Collagen alpha-1(III) chain;
DE   Flags: Precursor; Fragments;
GN   Name=COL3A1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-886.
RC   TISSUE=Kidney;
RX   PubMed=8206952; DOI=10.1016/s0021-9258(17)34026-7;
RA   Nah H.-D., Niu Z., Adams S.L.;
RT   "An alternative transcript of the chick type III collagen gene that does
RT   not encode type III collagen.";
RL   J. Biol. Chem. 269:16443-16448(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-96; 332-397; 431-484; 503-535 AND
RP   869-976.
RX   PubMed=6547770; DOI=10.1038/310333a0;
RA   Yamada Y., Liau G., Mudryj M., Obici S., de Crombrugghe B.;
RT   "Conservation of the sizes for one but not another class of exons in two
RT   chick collagen genes.";
RL   Nature 310:333-337(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 869-886 AND 977-994.
RX   PubMed=6298201; DOI=10.1016/s0021-9258(18)32779-0;
RA   Yamada Y., Mudryj M., Sullivan M., de Crombrugghe B.;
RT   "Isolation and characterization of a genomic clone encoding chick alpha-1
RT   type III collagen.";
RL   J. Biol. Chem. 258:2758-2761(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 977-1262.
RX   PubMed=6856474; DOI=10.1093/nar/11.9.2733;
RA   Yamada Y., Kuhn K., de Crombrugghe B.;
RT   "A conserved nucleotide sequence, coding for a segment of the C-propeptide,
RT   is found at the same location in different collagen genes.";
RL   Nucleic Acids Res. 11:2733-2744(1983).
CC   -!- FUNCTION: Collagen type III occurs in most soft connective tissues
CC       along with type I collagen.
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.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC   -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC       crucial roles in tissue growth and repair by controlling both the
CC       intracellular assembly of procollagen molecules and the extracellular
CC       assembly of collagen fibrils. It binds a calcium ion which is essential
CC       for its function (By similarity). {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   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR   EMBL; U07973; AAA83407.1; -; mRNA.
DR   EMBL; X00822; CAB52686.1; -; Genomic_DNA.
DR   EMBL; X00823; CAB52686.1; JOINED; Genomic_DNA.
DR   EMBL; X00826; CAA25397.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X00825; CAA25397.1; JOINED; Genomic_DNA.
DR   EMBL; X00827; CAA25398.1; -; Genomic_DNA.
DR   EMBL; X00828; CAA25399.1; -; Genomic_DNA.
DR   EMBL; X00830; CAA25401.1; -; Genomic_DNA.
DR   EMBL; X00831; CAA25402.1; -; Genomic_DNA.
DR   EMBL; K02302; AAD15299.1; -; Genomic_DNA.
DR   EMBL; K02301; AAD15298.1; -; Genomic_DNA.
DR   EMBL; V00391; CAA23689.1; -; Genomic_DNA.
DR   EMBL; V00392; CAA23690.1; -; Genomic_DNA.
DR   EMBL; M36662; AAA18519.1; ALT_SEQ; Unassigned_DNA.
DR   PIR; A05269; A05269.
DR   PIR; I50694; I50694.
DR   AlphaFoldDB; P12105; -.
DR   SMR; P12105; -.
DR   STRING; 9031.ENSGALP00000051057; -.
DR   GlyCosmos; P12105; 1 site, No reported glycans.
DR   GlyGen; P12105; 5 sites.
DR   PaxDb; 9031-ENSGALP00000051057; -.
DR   VEuPathDB; HostDB:geneid_396243; -.
DR   VEuPathDB; HostDB:geneid_396340; -.
DR   VEuPathDB; HostDB:geneid_424526; -.
DR   InParanoid; P12105; -.
DR   OrthoDB; 8939548at2759; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005586; C:collagen type III trimer; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IBA:GO_Central.
DR   GO; GO:0043588; P:skin development; IBA:GO_Central.
DR   FunFam; 2.60.120.1000:FF:000001; Collagen alpha-1 type I chain; 1.
DR   FunFam; 2.10.70.10:FF:000013; Collagen, type I, alpha 1; 1.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050938; Collagen_Structural_Proteins.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001007; VWF_dom.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..150
FT                   /note="N-terminal propeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005737"
FT   CHAIN           151..1017
FT                   /note="Collagen alpha-1(III) chain"
FT                   /id="PRO_0000005738"
FT   PROPEP          1018..1262
FT                   /note="C-terminal propeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005739"
FT   DOMAIN          29..88
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          1028..1262
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          95..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..164
FT                   /note="Nonhelical region (N-terminal)"
FT   REGION          160..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..994
FT                   /note="Triple-helical region"
FT   REGION          995..1003
FT                   /note="Nonhelical region (C-terminal)"
FT   COMPBIAS        102..118
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..190
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..201
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..264
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..295
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..376
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..414
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..549
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..640
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..650
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..684
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..701
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..738
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..790
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..817
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..838
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..872
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..904
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..940
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..993
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1076
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1078
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1079
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1081
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1084
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         262
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         283
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         859
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        1163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        994
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        995
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1058..1090
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1064
FT                   /note="Interchain (with C-1285)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1081
FT                   /note="Interchain (with C-1268)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1098..1260
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1168..1213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   CONFLICT        96
FT                   /note="E -> K (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        881
FT                   /note="G -> R (in Ref. 3; CAA23689)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        884
FT                   /note="G -> V (in Ref. 3; CAA23689)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        984
FT                   /note="L -> V (in Ref. 3; CAA23690)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1132
FT                   /note="F -> S (in Ref. 4; AAA18519)"
FT                   /evidence="ECO:0000305"
FT   NON_CONS        886..887
FT                   /evidence="ECO:0000305"
FT   NON_CONS        922..923
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1262 AA;  121249 MW;  96ABE7B2E9DEB43D CRC64;
     MMSFVQKVSL FILAVFQPSV ILAQQDALGG CTHLGQEYAD RDVWKPEPCQ ICVCDSGSVL
     CDDIICDDQE LDCPNPEIPL GECCPVCPQT TPQPTELPYT QGPKGDPGSP GSPGRTGAPG
     PPGQPGSPGA PGPPGICQSC PSISGGSFSP QYDSYDVKAG SVGMGYPPQP ISGFPGPPGP
     SGPPGPPGHA GPPGSNGYQG PPGEPGQPGP SGPPGPAGMI GPAGPPGKDG EPGRPGRNGD
     RGIPGLPGHK GHPGMPGMPG MKGARGFDGK DGAKGDSGAP GPKGEAGQPG ANGSPGQPGP
     GGPTGERGRP GNPGGPGAHG KDGAPGTAGP LGPPGPPGTA GFPGSPGFKG EAGPPGPAGA
     SGNPGERGEP GPQGQAGPPG PQGPPGRAGS PGGKGEMGPS GIPGGPGPPG GRGLPGPPGT
     SGNPGAKGTP GEPGKNGAKG DPGPKGERGE NGTPGARGPP GEEGKRGANG EPGQNGVPGT
     PGERGSPGFR GLPGSNGLPG EKGPAGERGS PGPPGPSGPA GDRGQDGGPG LPGMRGLPGI
     PGSPGSDGKP GPPGNQGEPG RSGPPGPAGP RGQPGVMGFP GPKGNEGAPG KNGERGPGGP
     PGTPGPAGKN GDVGLPGPPG PAGPAGDRGE PGPSGSPGLQ GLPGGPGPAG ENGKPGEPGP
     KGDIGGPGFP GPKGENGIPG ERGPQGPPGP TGARGGPGPA GSEGAKGPPG PPGAPGGTGL
     PGLQGMPGER GASGSPGPKG DKGEPGGKGA DGLPGARGER GNVGPIGPPG PAGPPGDKGE
     TGPAGAPGPA GSRGGPGERG EQGLPGPAGF PGAPGQNGEP GGKGERGPPG LRGEAGPPGA
     AGPQGGPGAP GPPGPQGVKG ERGSPGGPGA AGFPGARGPP GPPGNNGDRG ESGPPGVPGP
     PGHPGPAGNN GAPGKAGERG FQGPLGPQGA IGSPGASGAR GPPGPAGPPG KDGRGGYPGP
     IGPPGPRGNR GESGPAGPPG QPGLPGPSGP PGPCCGGGVA SLGAGEKGPV GYGYEYRDEP
     KENEINLGEI MSSMKSINNQ IENILSPDGS RKNPARNCRD LKFCHPELKS GEYWIDPNQG
     CKMDAIKVYC NMETGETCLS ANPATVPRKN WWTTESSGKK HVWFGESMKG GFQFSYGDPD
     LPEDVSEVQL AFLRILSSRA SQNITYHCKN SIAYMNQASG NVKKALKLMS SVETDIKAEG
     NSKYMYAVLE DGCTKHTGEW GKTVFEYRTR KTMRLPVVDI APIDIGGPDQ EFGVDVGPVC
     FL
//