ID   Q08E14_BOVIN            Unreviewed;      1466 AA.
AC   Q08E14; F1MXS8;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Collagen type III alpha 1 chain {ECO:0000313|Ensembl:ENSBTAP00000028617.6};
DE   SubName: Full=Collagen, type III, alpha 1 {ECO:0000313|EMBL:AAI23470.1};
GN   Name=COL3A1 {ECO:0000313|EMBL:AAI23470.1,
GN   ECO:0000313|Ensembl:ENSBTAP00000028617.6,
GN   ECO:0000313|VGNC:VGNC:27565};
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 {ECO:0000313|EMBL:AAI23470.1};
RN   [1] {ECO:0000313|EMBL:AAI23470.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI23470.1};
RC   TISSUE=Fetal skin {ECO:0000313|EMBL:AAI23470.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000028617.6, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028617.6,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSBTAP00000028617.6}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028617.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC       forming collagen). {ECO:0000256|ARBA:ARBA00003647}.
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DR   EMBL; BC123469; AAI23470.1; -; mRNA.
DR   RefSeq; NP_001070299.1; NM_001076831.1.
DR   STRING; 9913.ENSBTAP00000028617; -.
DR   PaxDb; 9913-ENSBTAP00000028617; -.
DR   Ensembl; ENSBTAT00000028617.6; ENSBTAP00000028617.6; ENSBTAG00000021466.6.
DR   GeneID; 510833; -.
DR   KEGG; bta:510833; -.
DR   CTD; 1281; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021466; -.
DR   VGNC; VGNC:27565; COL3A1.
DR   GeneTree; ENSGT00940000161229; -.
DR   OMA; HSGGTHQ; -.
DR   OrthoDB; 2970887at2759; -.
DR   TreeFam; TF344135; -.
DR   Reactome; R-BTA-1442490; Collagen degradation.
DR   Reactome; R-BTA-1474244; Extracellular matrix organization.
DR   Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-BTA-186797; Signaling by PDGF.
DR   Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-BTA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-BTA-216083; Integrin cell surface interactions.
DR   Reactome; R-BTA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-BTA-3000178; ECM proteoglycans.
DR   Reactome; R-BTA-8874081; MET activates PTK2 signaling.
DR   Reactome; R-BTA-8948216; Collagen chain trimerization.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000021466; Expressed in fornix of vagina and 106 other cell types or tissues.
DR   GO; GO:0005586; C:collagen type III trimer; IEA:Ensembl.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR   GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IEA:Ensembl.
DR   GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR   GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl.
DR   GO; GO:0060350; P:endochondral bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
DR   GO; GO:0036022; P:limb joint morphogenesis; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0050777; P:negative regulation of immune response; IEA:Ensembl.
DR   GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR   GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR   GO; GO:0043588; P:skin development; IEA:Ensembl.
DR   GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032905; P:transforming growth factor beta1 production; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001007; VWF_dom.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 6.
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   Collagen {ECO:0000313|EMBL:AAI23470.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1466
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041198809"
FT   DOMAIN          30..89
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          1232..1466
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          95..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..201
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..222
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..572
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..699
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..890
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..912
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1180..1194
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1466 AA;  138439 MW;  01E27D6281E4FE20 CRC64;
     MMSFVQKGTW LLFALLHPTV ILAQQEAVDG GCSHLGQSYA DRDVWKPEPC QICVCDSGSV
     LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN GQGPQGPKGD PGPPGIPGRN
     GDPGPPGSPG SPGSPGPPGI CESCPTGGQN YSPQYEAYDV KSGVAGGGIA GYPGPAGPPG
     PPGPPGTSGH PGAPGAPGYQ GPPGEPGQAG PAGPPGPPGA IGPSGPAGKD GESGRPGRPG
     ERGFPGPPGM KGPAGMPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGVP GENGAPGPMG
     PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK GEVGPAGSPG
     SSGAPGQRGE PGPQGHAGAP GPPGPPGSNG SPGGKGEMGP AGIPGAPGLI GARGPPGPPG
     TNGVPGQRGA AGEPGKNGAK GDPGPRGERG EAGSPGIAGP KGEDGKDGSP GEPGANGLPG
     AAGERGVPGF RGPAGANGLP GEKGPPGDRG GPGPAGPRGV AGEPGRDGLP GGPGLRGIPG
     SPGGPGSDGK PGPPGSQGET GRPGPPGSPG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG
     GPGPQGPAGK NGETGPQGPP GPTGPSGDKG DTGPPGPQGL QGLPGTSGPP GENGKPGEPG
     PKGEAGAPGI PGGKGDSGAP GERGPPGAGG PPGPRGGAGP PGPEGGKGAA GPPGPPGSAG
     TPGLQGMPGE RGGPGGPGPK GDKGEPGSSG VDGAPGKDGP RGPTGPIGPP GPAGQPGDKG
     ESGAPGVPGI AGPRGGPGER GEQGPPGPAG FPGAPGQNGE PGAKGERGAP GEKGEGGPPG
     AAGPAGGSGP AGPPGPQGVK GERGSPGGPG AAGFPGGRGP PGPPGSNGNP GPPGSSGAPG
     KDGPPGPPGS NGAPGSPGIS GPKGDSGPPG ERGAPGPQGP PGAPGPLGIA GLTGARGLAG
     PPGMPGARGS PGPQGIKGEN GKPGPSGQNG ERGPPGPQGL PGLAGTAGEP GRDGNPGSDG
     LPGRDGAPGA KGDRGENGSP GAPGAPGHPG PPGPVGPAGK SGDRGETGPA GPSGAPGPAG
     SRGPPGPQGP RGDKGETGER GAMGIKGHRG FPGNPGAPGS PGPAGHQGAV GSPGPAGPRG
     PVGPSGPPGK DGASGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGAG
     GVAAIAGVGA EKAGGFAPYY GDEPIDFKIN TDEIMTSLKS VNGQIESLIS PDGSRKNPAR
     NCRDLKFCHP ELQSGEYWVD PNQGCKLDAI KVYCNMETGE TCISASPLTI PQKNWWTDSG
     AEKKHVWFGE SMEGGFQFSY GNPELPEDVL DVQLAFLRLL SSRASQNITY HCKNSIAYMD
     HASGNVKKAL KLMGSNEGEF KAEGNSKFTY TVLEDGCTKH TGEWGKTVFQ YQTRKAVRLP
     IVDIAPYDIG GPDQEFGADI GPVCFL
//