BGH3_RABIT
ID BGH3_RABIT Reviewed; 683 AA.
AC Q95215;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 25-MAY-2022, entry version 105.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Cornea;
RX PubMed=9112985;
RA Rawe I.M., Zhan Q., Burrows R., Bennett K., Cintron C.;
RT "Beta-ig. Molecular cloning and in situ hybridization in corneal tissues.";
RL Invest. Ophthalmol. Vis. Sci. 38:893-900(1997).
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 -!- TISSUE SPECIFICITY: Located primarily in the epithelium of normal adult
CC cornea, in fetal stromal cells, and both endothelium- and stroma-
CC derived cells in healing corneal wounds (PubMed:9112985). Not expressed
CC in normal adult endothelium and stroma (PubMed:9112985).
CC {ECO:0000269|PubMed:9112985}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB07015.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U66205; AAB07015.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q95215; -.
DR SMR; Q95215; -.
DR STRING; 9986.ENSOCUP00000017414; -.
DR eggNOG; KOG1437; Eukaryota.
DR InParanoid; Q95215; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Extracellular matrix;
KW Gamma-carboxyglutamic acid; Phosphoprotein; Reference proteome; Repeat;
KW 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_0000008771"
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; 74685 MW; 4548520497548CD6 CRC64;
MALFVRLLAL ALALALGPAA TLAGPAKSPY QLVLQHSRLR RQQHGPNVCA VQKVIGTNRK
YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGERSCPAA LPLANLYETL GVVGSTTTQL
YTDRTEKLRP EMEGPGRFTI FAPSNEAWAS LPAEVLDSLV SNVNIELLNA LRYHMVDRRV
LTDELKHGMA LTSMYQNSKF QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTVT
NNIQQIIEIE DTFETLRAAV AASGLNTLLE SDGQFTLLAP TNEAKEKIPT ETLNRILGDP
EALRDLLNNH ILKSAMCAEA IVAGLSMETL EATTLEVGCS GDMLTINGKA IISNKDVLAT
NGVIHFIDEL LIPDSAKTLS ELAAGSDVST AIDLFGQAGL GTHLSGNERL TLLAPLNSVF
EEGAPPIDAH TRNLLRNHII KDQLASKYLY HGQTLDTLGG KKLRVFVYRN SLCIENSCIA
AHDKRGRYGT LFTMDRMLTP PSGTVMDVLK GDNRFSMLVA AIQFRRLTET LNREGAYTVF
APTNEAFQAL PPGELNKLLG NAKELADILK YHVGEEILVS GGIGTLVRLK SLQGDKLEVS
SKNNAVSVNK EPVAESDIMA TNGVVYAITS VLQPPANRPQ ERGDELADSA LEIFKQASAF
SRASQRSVRL APVYQRLLER MKH
