CO3A1_RAT
ID CO3A1_RAT Reviewed; 1463 AA.
AC P13941; O70604; Q5PQT6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Collagen alpha-1(III) chain;
DE Flags: Precursor;
GN Name=Col3a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 828-1463.
RX PubMed=8286415;
RA Glumoff V., Maekelae J.K., Vuorio E.;
RT "Cloning of cDNA for rat pro alpha 1(III) collagen mRNA. Different
RT expression patterns of type I and type III collagen and fibronectin genes
RT in experimental granulation tissue.";
RL Biochim. Biophys. Acta 1217:41-48(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 900-1463.
RC STRAIN=Sprague-Dawley; TISSUE=Fibroblast;
RA Wurtz T., Ellerstroem C., Lundmark C., Christersson C.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1135-1309.
RX PubMed=2456904; DOI=10.1089/dna.1.1988.7.347;
RA Frankel F.R., Hsu C.-Y.J., Meyers J.C., Lin E., Lyttle C.R., Komm B.,
RA Mohn K.;
RT "Regulation of alpha 2(I), alpha 1(III), and alpha 2(V) collagen mRNAs by
RT estradiol in the immature rat uterus.";
RL DNA 7:347-354(1988).
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: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: O-glycosylated. {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; BC087039; AAH87039.1; -; mRNA.
DR EMBL; X70369; CAA49832.1; -; mRNA.
DR EMBL; AJ005395; CAA06510.1; -; mRNA.
DR EMBL; M21354; AAA40942.1; -; mRNA.
DR PIR; S41067; S41067.
DR RefSeq; NP_114474.1; NM_032085.1.
DR AlphaFoldDB; P13941; -.
DR SMR; P13941; -.
DR BioGRID; 249898; 1.
DR IntAct; P13941; 2.
DR MINT; P13941; -.
DR STRING; 10116.ENSRNOP00000004956; -.
DR GlyGen; P13941; 1 site.
DR iPTMnet; P13941; -.
DR PhosphoSitePlus; P13941; -.
DR PaxDb; P13941; -.
DR PRIDE; P13941; -.
DR Ensembl; ENSRNOT00000004956; ENSRNOP00000004956; ENSRNOG00000003357.
DR GeneID; 84032; -.
DR KEGG; rno:84032; -.
DR UCSC; RGD:71029; rat.
DR CTD; 1281; -.
DR RGD; 71029; Col3a1.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161229; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P13941; -.
DR OMA; PQFESYD; -.
DR OrthoDB; 1406711at2759; -.
DR TreeFam; TF344135; -.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474244; Extracellular matrix organization.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-419037; NCAM1 interactions.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR PRO; PR:P13941; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000003357; Expressed in esophagus and 18 other tissues.
DR Genevisible; P13941; RN.
DR GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR GO; GO:0005586; C:collagen type III trimer; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0071711; P:basement membrane organization; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR GO; GO:0048251; P:elastic fiber assembly; ISO:RGD.
DR GO; GO:0060350; P:endochondral bone morphogenesis; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0048144; P:fibroblast proliferation; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISO:RGD.
DR GO; GO:0036022; P:limb joint morphogenesis; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0050777; P:negative regulation of immune response; ISO:RGD.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:1990776; P:response to angiotensin; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; IEP:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0032905; P:transforming growth factor beta1 production; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 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:0000250"
FT PROPEP 24..154
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005746"
FT CHAIN 155..1218
FT /note="Collagen alpha-1(III) chain"
FT /id="PRO_0000005747"
FT PROPEP 1219..1463
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043408"
FT DOMAIN 31..90
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1229..1463
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 97..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..169
FT /note="Nonhelical region (N-terminal)"
FT REGION 170..1195
FT /note="Triple-helical region"
FT COMPBIAS 97..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="5-hydroxylysine; alternate"
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 MOD_RES 976
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1093
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1105
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 262
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 1195
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1196
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1259..1291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1265
FT /note="Interchain (with C-1282)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1282
FT /note="Interchain (with C-1265)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1299..1461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1369..1414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 1167
FT /note="N -> D (in Ref. 3; CAA06510)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="A -> G (in Ref. 3; CAA06510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1463 AA; 138936 MW; 63C218CD2BCA47B6 CRC64;
MMSFVQCGTW FLLTLLHPSL ILAQQSNVDE LGCNYLGQSY ESRDVWKPEP CQICVCDSGS
VLCDDIMCDD EPLDCPNPEI PFGECCAICP QPSTPAPVIP DGNRPQGPKG DPGPPGIPGR
NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP
PGPPGSSGHP GSPGSPGYQG PPGEPGQAGP AGPPGPPGAI GPSGPAGKDG ESGRPGRPGE
RGLPGPPGIK GPAGIPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG EVGPAGSPGS
NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA GIPGAPGLLG ARGPPGPAGA
NGAPGQRGPS GEPGKNGAKG EPGARGERGE AGSPGIPGPK GEDGKDGSPG EPGANGVPGN
PGERGAPGFR GPAGPNGAPG EKGPAGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS
PGGPGNDGKP GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG
PGLPGPAGKN GETGPQGPPG PTGAPGDKGD AGPPGPQGLQ GIPGTSGPPG ENGKPGEPGP
KGEAGAPGVP GGKGDSGAPG ERGPPGTAGT PGLRGGAGPP GPEGGKGPAG PPGPPGTSGP
PGLQGMPGER GGPGSPGPKG EKGEPGGAGA DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE
GGAPGLPGIA GPRGGPGERG EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGA
AGPPGGSGPA GPPGPQGVKG ERGSPGGPGA AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK
DGPPGPAGNS GSPGNPGVAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG LTGARGLAGP
PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP GQPGTAGEPG RDGNPGSDGQ
PGRDGSPGGK GDRGENGSPG APGAPGHPGP PGPVGPSGKN GDRGETGPAG PSGAPGPAGA
RGAPGPQGPR GDKGETGERG SNGIKGHRGF PGNPGPPGSP GAAGHQGAVG SPGPAGPRGP
VGPHGPPGKD GSSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA
AIAGVGGEKS GGFSPYYGDD PMDFKINTEE IMSSLKSVNG QIESLISPDG SRKNPARNCR
DLKFCHPELK SGEYWVDPNQ GCKMDAIKVF CNMETGETCI NASPMTVPRK HWWTDAGAEK
KHVWFGESMN GGFQFSYGNP DLPEDVLDVQ LAFLRLLSSR ASQNITYHCK NSIAYMDQAN
GNVKKSLKLM GSNEGEFKAE GNSKFTYTVL EDGCTKHTGE WSKTVFEYQT RKAMRLPIID
IAPYDIGGPD QEFGVDIGPV CFL
