BGH3_MOUSE
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 03-AUG-2022, entry version 156.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P82198; -.
DR PRIDE; P82198; -.
DR ProteomicsDB; 273680; -.
DR Antibodypedia; 1982; 419 antibodies from 40 providers.
DR DNASU; 21810; -.
DR Ensembl; ENSMUST00000045173; ENSMUSP00000037719; ENSMUSG00000035493.
DR GeneID; 21810; -.
DR KEGG; mmu:21810; -.
DR UCSC; uc011zae.1; mouse.
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; LHQVDRP; -.
DR OrthoDB; 926852at2759; -.
DR PhylomeDB; P82198; -.
DR TreeFam; TF316269; -.
DR BioGRID-ORCS; 21810; 1 hit in 73 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 381 other tissues.
DR ExpressionAtlas; P82198; baseline and differential.
DR Genevisible; P82198; MM.
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:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
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; 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
