BGH3_PIG
ID BGH3_PIG Reviewed; 683 AA.
AC O11780;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Transforming growth factor-beta-induced protein ig-h3;
DE Short=Beta ig-h3;
DE AltName: Full=Kerato-epithelin;
DE AltName: Full=RGD-containing collagen-associated protein;
DE Short=RGD-CAP;
DE Flags: Precursor;
GN Name=TGFBI;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-41, INTERACTION WITH
RP COLLAGEN, INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Chondrocyte;
RX PubMed=9061001; DOI=10.1016/s0167-4889(96)00147-4;
RA Hashimoto K., Noshiro M., Ohno S., Kawamoto T., Satakeda H., Akagawa Y.,
RA Nakashima K., Okimura A., Ishida H., Okamoto T., Pan H., Shen M., Yan W.,
RA Kato Y.;
RT "Characterization of a cartilage-derived 66-kDa protein (RGD-CAP/beta ig-
RT h3) that binds to collagen.";
RL Biochim. Biophys. Acta 1355:303-314(1997).
CC -!- FUNCTION: Plays a role in cell adhesion (By similarity). May play a
CC role in cell-collagen interactions (PubMed:9061001).
CC {ECO:0000250|UniProtKB:Q15582, ECO:0000269|PubMed:9061001}.
CC -!- SUBUNIT: Binds to type I, II, and IV collagens (PubMed:9061001).
CC {ECO:0000269|PubMed:9061001}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q15582}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:9061001}. Note=May be associated both with
CC microfibrils and with the cell surface. {ECO:0000250|UniProtKB:Q15582}.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues except for
CC the brain. High levels in corneal epithelium (PubMed:9061001).
CC {ECO:0000269|PubMed:9061001}.
CC -!- DEVELOPMENTAL STAGE: Expressed in chondrocytes during all stages
CC (PubMed:9061001). Highest levels during the prehypertrophic stage
CC (PubMed:9061001). {ECO:0000269|PubMed:9061001}.
CC -!- INDUCTION: By TGF-beta (PubMed:9061001). {ECO:0000269|PubMed:9061001}.
CC -!- PTM: Gamma-carboxyglutamated; gamma-carboxyglutamate residues are
CC formed by vitamin K dependent carboxylation; these residues may be
CC required for binding to calcium. According to a report, does not
CC contain any vitamin K-dependent gamma-carboxyglutamate residues.
CC {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; D55717; BAA20089.1; -; mRNA.
DR AlphaFoldDB; O11780; -.
DR SMR; O11780; -.
DR STRING; 9823.ENSSSCP00000015228; -.
DR PeptideAtlas; O11780; -.
DR PRIDE; O11780; -.
DR eggNOG; KOG1437; Eukaryota.
DR InParanoid; O11780; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
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:0000269|PubMed:9061001"
FT CHAIN 24..683
FT /note="Transforming growth factor-beta-induced protein ig-
FT h3"
FT /evidence="ECO:0000269|PubMed:9061001"
FT /id="PRO_0000008770"
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; 74462 MW; B4033E75D1C82A77 CRC64;
MALLGRLLPL ALALALGPAA THAGPAKSPY QLVLQHSRLR GRQHGPNVCA VQKLIGTNKK
YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGEKGCPAV LPLSNLYETL GVVGSTTTQL
YTDRTEKLRP EMEGPGSFTI FAPSNEAWAS LPAEVLDSLV SNVNIELLNA LRYHMVDRRV
LTDELKHGMA LTSMYQNSNI QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTVT
NNIQQIIEIE DTFETLRAAV AASGLNTLLE GDGQYTLLAP SNEAFEKIPA ETLNRILGDP
EALRDLLNNH ILKSAMCAEA IVAGLSLETL EGTTLEVGCS GDMLTINGKP IISNKDVLAT
NGVIHFIDEL LIPDSAKTLF ELAAESDVST AVDLFRQAGL GSHLSGNERL TLLAPMNSVF
KDGTPRIDAR TKNLLLNHMI KDQLASKYLY HGQTLDTLGG KKLRVFVYRN SLCIENSCIA
AHDKRGRYGT LFTMDRMLTP PMGTVMDVLK GDNRFSMLVA AIQSAGLTET LNREGVYTVF
APTNEAFQAL PLGERNKLLG NAKELANILK YHVGDEILVS GGIGALVRLK SLQGDKLEVS
SKNSLVTVNK EPVAEADIMA TNGVVHTINT VLRPPANKPQ ERGDELADSA LEIFKQASAF
SRATQSSVKL APVYQRLLER MKH
