BGH3_BOVIN
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 03-AUG-2022, entry version 79.
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 STRING; 9913.ENSBTAP00000012519; -.
DR PaxDb; P55906; -.
DR PRIDE; P55906; -.
DR Ensembl; ENSBTAT00000076090; ENSBTAP00000072728; ENSBTAG00000009513.
DR GeneID; 539596; -.
DR KEGG; bta:539596; -.
DR CTD; 7045; -.
DR VEuPathDB; HostDB:ENSBTAG00000009513; -.
DR VGNC; VGNC:52886; TGFBI.
DR eggNOG; KOG1437; Eukaryota.
DR GeneTree; ENSGT00530000063860; -.
DR OMA; LHQVDRP; -.
DR OrthoDB; 926852at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000009513; Expressed in monocyte and 108 other tissues.
DR ExpressionAtlas; P55906; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR Gene3D; 2.30.180.10; -; 4.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR032954; TGFBI.
DR InterPro; IPR016666; TGFBI/POSTN.
DR PANTHER; PTHR10900:SF82; PTHR10900:SF82; 1.
DR Pfam; PF02469; Fasciclin; 4.
DR PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 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
