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Database: UniProt
Entry: P04258
LinkDB: P04258
Original site: P04258 
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   08-MAY-2019, entry version 114.
DE   RecName: Full=Collagen alpha-1(III) chain;
GN   Name=COL3A1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-242, AND HYDROXYLATION AT LYS-95; LYS-107;
RP   LYS-119; LYS-938 AND LYS-950.
RX   PubMed=488906;
RA   Fietzek P.P., Allmann H., Rauterberg J., Henkel W., Wachter E.,
RA   Kuhn K.;
RT   "The covalent structure of calf skin type III collagen. I. The amino
RT   acid sequence of the amino terminal region of the alpha 1(III) chain
RT   (positions 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
RT   acid sequence of the cyanogen bromide peptide alpha 1(III)CB1,8,10,2
RT   (positions 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
RT   acid sequence of the cyanogen bromide peptide alpha 1(III)CB4
RT   (positions 403-551).";
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
RT   acid sequence of the cyanogen bromide peptide alpha 1(III)CB5
RT   (positions 552-788).";
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;
RP   LYS-119; 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
RT   acid sequence of the cyanogen bromide peptide alpha 1(III)CB9A
RT   (position 789-927).";
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
RT   acid sequence of the carboxyterminal cyanogen bromide peptide alpha
RT   1(III)CB9B (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
CC       and binding to ADGRG1 inhibits neuronal migration and activates
CC       the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12
CC       (By similarity). {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
CC       also cross-linked via hydroxylysines.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (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.
CC       {ECO:0000305}.
DR   PIR; A02862; CGBO7S.
DR   ComplexPortal; CPX-3106; Collagen type III trimer.
DR   STRING; 9913.ENSBTAP00000028617; -.
DR   PeptideAtlas; P04258; -.
DR   PRIDE; P04258; -.
DR   HOGENOM; HOG000085654; -.
DR   InParanoid; P04258; -.
DR   OrthoDB; 1406711at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW   Reference proteome; Repeat; Secreted.
FT   CHAIN         1   1049       Collagen alpha-1(III) chain.
FT                                /FTId=PRO_0000059398.
FT   REGION        1     14       Nonhelical region (N-terminal).
FT   REGION       15   1040       Triple-helical region.
FT   REGION     1041   1049       Nonhelical region (C-terminal).
FT   MOD_RES      95     95       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:488906,
FT                                ECO:0000269|PubMed:488911}.
FT   MOD_RES     107    107       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:488906,
FT                                ECO:0000269|PubMed:488911}.
FT   MOD_RES     119    119       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:488906,
FT                                ECO:0000269|PubMed:488911}.
FT   MOD_RES     938    938       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:488906,
FT                                ECO:0000269|PubMed:488911}.
FT   MOD_RES     950    950       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:488906,
FT                                ECO:0000269|PubMed:488911}.
FT   CARBOHYD    107    107       O-linked (Gal...) hydroxylysine.
FT                                {ECO:0000269|PubMed:488906}.
FT   CARBOHYD    950    950       O-linked (Gal...) hydroxylysine.
FT   DISULFID   1040   1040       Interchain.
FT   DISULFID   1041   1041       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
//
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