ID   BGH3_MOUSE              Reviewed;         683 AA.
AC   P82198; Q3U9R1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Transforming growth factor-beta-induced protein ig-h3;
DE            Short=Beta ig-h3;
DE   Flags: Precursor;
GN   Name=Tgfbi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=G8;
RX   PubMed=8024701; DOI=10.1089/dna.1994.13.571;
RA   Skonier J., Bennett K., Rothwell V., Kosowski S., Plowman G., Wallace P.,
RA   Edelhoff S., Disteche C.M., Neubauer M., Marquardt H., Rodgers J.,
RA   Purchio A.F.;
RT   "Beta ig-h3: a transforming growth factor-beta-responsive gene encoding a
RT   secreted protein that inhibits cell attachment in vitro and suppresses the
RT   growth of CHO cells in nude mice.";
RL   DNA Cell Biol. 13:571-584(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Eye, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Plays a role in cell adhesion (PubMed:8024701). May play a
CC       role in cell-collagen interactions (By similarity).
CC       {ECO:0000250|UniProtKB:O11780, ECO:0000269|PubMed:8024701}.
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: Expressed in heart, kidney, liver, skeletal muscle,
CC       testis, thyroid and uterus (PubMed:8024701).
CC       {ECO:0000269|PubMed:8024701}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryo at 12 dpc
CC       (PubMed:8024701). {ECO:0000269|PubMed:8024701}.
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; L19932; AAC37658.1; -; mRNA.
DR   EMBL; AK084431; BAC39181.1; -; mRNA.
DR   EMBL; AK142323; BAE25032.1; -; mRNA.
DR   EMBL; AK151680; BAE30605.1; -; mRNA.
DR   EMBL; AK152365; BAE31155.1; -; mRNA.
DR   EMBL; AK155572; BAE33330.1; -; mRNA.
DR   EMBL; AK155828; BAE33452.1; -; mRNA.
DR   EMBL; AK170495; BAE41834.1; -; mRNA.
DR   CCDS; CCDS36680.1; -.
DR   RefSeq; NP_033395.1; NM_009369.4.
DR   AlphaFoldDB; P82198; -.
DR   SMR; P82198; -.
DR   BioGRID; 204162; 1.
DR   STRING; 10090.ENSMUSP00000037719; -.
DR   iPTMnet; P82198; -.
DR   PhosphoSitePlus; P82198; -.
DR   CPTAC; non-CPTAC-3690; -.
DR   MaxQB; P82198; -.
DR   PaxDb; 10090-ENSMUSP00000037719; -.
DR   ProteomicsDB; 273680; -.
DR   Antibodypedia; 1982; 478 antibodies from 40 providers.
DR   DNASU; 21810; -.
DR   Ensembl; ENSMUST00000045173.10; ENSMUSP00000037719.9; ENSMUSG00000035493.11.
DR   GeneID; 21810; -.
DR   KEGG; mmu:21810; -.
DR   UCSC; uc011zae.1; mouse.
DR   AGR; MGI:99959; -.
DR   CTD; 7045; -.
DR   MGI; MGI:99959; Tgfbi.
DR   VEuPathDB; HostDB:ENSMUSG00000035493; -.
DR   eggNOG; KOG1437; Eukaryota.
DR   GeneTree; ENSGT00530000063860; -.
DR   HOGENOM; CLU_017611_1_0_1; -.
DR   InParanoid; P82198; -.
DR   OMA; NSMERYT; -.
DR   OrthoDB; 523796at2759; -.
DR   PhylomeDB; P82198; -.
DR   TreeFam; TF316269; -.
DR   BioGRID-ORCS; 21810; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Tgfbi; mouse.
DR   PRO; PR:P82198; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P82198; Protein.
DR   Bgee; ENSMUSG00000035493; Expressed in substantia propria of cornea and 382 other cell types or tissues.
DR   ExpressionAtlas; P82198; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0051179; P:localization; ISO:MGI.
DR   Gene3D; 2.30.180.10; FAS1 domain; 4.
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.
DR   Genevisible; P82198; MM.
PE   1: Evidence at protein 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_0000041980"
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;  74597 MW;  2B6E9DBB9C50F52B CRC64;
     MALLMRLLTL ALALSVGPAG TLAGPAKSPY QLVLQHSRLR GRQHGPNVCA VQKVIGTNKK
     YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGEKGCPAA LPLSNLYETM GVVGSTTTQL
     YTDRTEKLRP EMEGPGSFTI FAPSNEAWSS LPAEVLDSLV SNVNIELLNA LRYHMVDRRV
     LTDELKHGMT LTSMYQNSNI QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTIT
     NNIQQIIEIE DTFETLRAAV AASGLNTVLE GDGQFTLLAP TNEAFEKIPA ETLNRILGDP
     EALRDLLNNH ILKSAMCAEA IVAGMSMETL GGTTLEVGCS GDKLTINGKA VISNKDILAT
     NGVIHFIDEL LIPDSAKTLL ELAGESDVST AIDILKQAGL DTHLSGKEQL TFLAPLNSVF
     KDGVPRIDAQ MKTLLLNHMV KEQLASKYLY SGQTLDTLGG KKLRVFVYRN SLCIENSCIA
     AHDKRGRFGT LFTMDRMLTP PMGTVMDVLK GDNRFSMLVA AIQSAGLMEI LNREGVYTVF
     APTNEAFQAM PPEELNKLLA NAKELTNILK YHIGDEILVS GGIGALVRLK SLQGDKLEVS
     SKNNVVSVNK EPVAETDIMA TNGVVYAINT VLQPPANRPQ ERGDELADSA LEIFKQASAY
     SRAAQRSVRL APVYQRLLER MKH
//