ID   BGH3_BOVIN              Reviewed;         683 AA.
AC   P55906; A7YWB6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 2.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=Transforming growth factor-beta-induced protein ig-h3;
DE            Short=Beta ig-h3;
DE   AltName: Full=MP70;
DE   AltName: Full=MP78;
DE   Flags: Precursor;
GN   Name=TGFBI; Synonyms=BIGH3;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8557636; DOI=10.1074/jbc.271.2.1096;
RA   Gibson M.A., Hatzinikolas G., Kumaratilake J.S., Sandberg L.B.,
RA   Nicholl J.K., Sutherland G.R., Cleary E.G.;
RT   "Further characterization of proteins associated with elastic fiber
RT   microfibrils including the molecular cloning of MAGP-2 (MP25).";
RL   J. Biol. Chem. 271:1096-1103(1996).
CC   -!- FUNCTION: Plays a role in cell adhesion (By similarity). May play a
CC       role in cell-collagen interactions (By similarity).
CC       {ECO:0000250|UniProtKB:O11780, ECO:0000250|UniProtKB:Q15582}.
CC   -!- SUBUNIT: Binds to type I, II, and IV collagens.
CC       {ECO:0000250|UniProtKB:O11780}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q15582}.
CC       Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:Q15582}. Note=May be associated both with
CC       microfibrils and with the cell surface. {ECO:0000250|UniProtKB:Q15582}.
CC   -!- PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated;
CC       gamma-carboxyglutamate residues are formed by vitamin K dependent
CC       carboxylation; this may be required for calcium binding. According to a
CC       more recent report, does not contain vitamin K-dependent gamma-
CC       carboxyglutamate residues. {ECO:0000250|UniProtKB:Q15582}.
CC   -!- PTM: The EMI domain contains 2 expected intradomain disulfide bridges
CC       (Cys-49-Cys85 and Cys-84-Cys-97) and one unusual interdomain disulfide
CC       bridge to the second FAS1 domain (Cys-74-Cys-339). This arrangement
CC       violates the predicted disulfide bridge pattern of an EMI domain.
CC       {ECO:0000250|UniProtKB:Q15582}.
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DR   EMBL; BC134483; AAI34484.1; -; mRNA.
DR   RefSeq; NP_001192331.1; NM_001205402.1.
DR   AlphaFoldDB; P55906; -.
DR   SMR; P55906; -.
DR   FunCoup; P55906; 300.
DR   STRING; 9913.ENSBTAP00000072728; -.
DR   GlyGen; P55906; 1 site.
DR   PaxDb; 9913-ENSBTAP00000072728; -.
DR   GeneID; 539596; -.
DR   KEGG; bta:539596; -.
DR   CTD; 7045; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009513; -.
DR   VGNC; VGNC:52886; TGFBI.
DR   eggNOG; KOG1437; Eukaryota.
DR   InParanoid; P55906; -.
DR   OMA; MYQNIDI; -.
DR   OrthoDB; 286301at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000009513; Expressed in monocyte and 108 other cell types or tissues.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProtKB-ARBA.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IBA:GO_Central.
DR   FunFam; 2.30.180.10:FF:000001; periostin isoform X1; 1.
DR   FunFam; 2.30.180.10:FF:000002; periostin isoform X1; 1.
DR   FunFam; 2.30.180.10:FF:000003; periostin isoform X1; 1.
DR   FunFam; 2.30.180.10:FF:000007; Transforming growth factor-beta-induced protein ig-h3; 1.
DR   Gene3D; 2.30.180.10; FAS1 domain; 4.
DR   InterPro; IPR050904; Adhesion/Biosynth-related.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR036378; FAS1_dom_sf.
DR   InterPro; IPR000782; FAS1_domain.
DR   InterPro; IPR016666; TGFBI/POSTN.
DR   PANTHER; PTHR10900; PERIOSTIN-RELATED; 1.
DR   PANTHER; PTHR10900:SF82; TRANSFORMING GROWTH FACTOR-BETA-INDUCED PROTEIN IG-H3; 1.
DR   Pfam; PF02469; Fasciclin; 4.
DR   PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR   SMART; SM00554; FAS1; 4.
DR   SUPFAM; SSF82153; FAS1 domain; 4.
DR   PROSITE; PS51041; EMI; 1.
DR   PROSITE; PS50213; FAS1; 4.
PE   1: Evidence at protein level;
KW   Cell adhesion; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Gamma-carboxyglutamic acid; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   CHAIN           24..683
FT                   /note="Transforming growth factor-beta-induced protein ig-
FT                   h3"
FT                   /id="PRO_0000203524"
FT   DOMAIN          45..99
FT                   /note="EMI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DOMAIN          103..236
FT                   /note="FAS1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          240..371
FT                   /note="FAS1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          375..498
FT                   /note="FAS1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          502..632
FT                   /note="FAS1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   MOTIF           642..644
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   MOD_RES         65
FT                   /note="S-cysteinyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   DISULFID        49..85
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   DISULFID        74..339
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   DISULFID        84..97
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   DISULFID        214..317
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
FT   DISULFID        473..478
FT                   /evidence="ECO:0000250|UniProtKB:Q15582"
SQ   SEQUENCE   683 AA;  74408 MW;  24764994C9FA66E2 CRC64;
     MALLGRLLPL ALALALGPAA TPAGPARSPY QLVLQHSRLR GRQHGPNVCA VQKLIGTNKK
     YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGEKGCPAA LPLSNLYETL GVVGATTTQL
     YTDRTEKLRP EMEGPGSFTI FAPSNEAWSS LPAEVLDSLV SNVNIELLNA LRYHMVDRRV
     LTDELKHGMA LTSMYQNSNI QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTVT
     NNIQQIIEIE DTFETLRAAV AASGLNTLLE GDGQYTLLAP TNEAFEKIPA ETLNRILGDP
     EALRDLLNNH ILKSAMCAEA IVAGLSLETL EGTTLEVGCS GDMLTINGKP IISNKDVLAT
     NGVIHFIDEL LIPDSAKTLF ELAADSDVST AIDLFRQAGL SSHLSGNERL TLLAPMNSVF
     KDGTPPINAR TKNLLLNHMI KDQLASKYLY HGQTLDTLGG RKLRVFVYRN SLCIENSCIA
     AHDKRGRYGT LFTMDRMLTP PMGTVMDVLK GDNRFSMLVA AIQSAGLTET LNREGVYTVF
     APTNEAFQAL PRGELNKLMG NAKELANILK YHVGDEILVS GGIGALVRLK SLQGDKLEVS
     SKNNVVSVNK EPVAEVDIMA TNGVVHAISS VLQPPANRPQ ERGDELADSA LEIFKQASAF
     SRATQSSVKL APVYQRLLER MKH
//