TMM47_MOUSE
ID TMM47_MOUSE Reviewed; 181 AA.
AC Q9JJG6; B1AUN5; Q3TS34; Q3UZL4; Q8C0H5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transmembrane protein 47;
DE AltName: Full=Transmembrane 4 superfamily member 10;
GN Name=Tmem47; Synonyms=Tm4sf10; ORFNames=MNCb-0941;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Head, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17195181; DOI=10.1002/dvdy.21052;
RA Bruggeman L.A., Martinka S., Simske J.S.;
RT "Expression of TM4SF10, a Claudin/EMP/PMP22 family cell junction protein,
RT during mouse kidney development and podocyte differentiation.";
RL Dev. Dyn. 236:596-605(2007).
RN [6]
RP FUNCTION, INTERACTION WITH FYB1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21881001; DOI=10.1152/ajpcell.00166.2011;
RA Azhibekov T.A., Wu Z., Padiyar A., Bruggeman L.A., Simske J.S.;
RT "TM4SF10 and ADAP interaction in podocytes: role in Fyn activity and
RT nephrin phosphorylation.";
RL Am. J. Physiol. 301:C1351-C1359(2011).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26990309; DOI=10.1002/dvdy.24404;
RA Dong Y., Simske J.S.;
RT "The vertebrate claudin/PMP22/EMP22/MP20 family protein TMEM47 regulates
RT epithelial cell junction maturation and morphogenesis.";
RL Dev. Dyn. 245:653-666(2016).
CC -!- FUNCTION: Regulates cell junction organization in epithelial cells. May
CC play a role in the transition from adherens junction to tight junction
CC assembly. May regulate F-actin polymerization required for tight
CC junctional localization dynamics and affect the junctional localization
CC of PARD6B (PubMed:26990309). During podocyte differentiation may
CC negatively regulate activity of FYN and subsequently the abundance of
CC nephrin (PubMed:21881001). {ECO:0000269|PubMed:21881001,
CC ECO:0000269|PubMed:26990309}.
CC -!- SUBUNIT: Interacts with CTNNB1, CTNNA1, PRKCI, PARD6B (By similarity).
CC Interacts with FYB1. {ECO:0000250|UniProtKB:Q9XSV3,
CC ECO:0000269|PubMed:21881001}.
CC -!- INTERACTION:
CC Q9JJG6; O35601: Fyb1; NbExp=4; IntAct=EBI-11685657, EBI-7353747;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell junction {ECO:0000269|PubMed:17195181,
CC ECO:0000269|PubMed:26990309}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9XSV3}. Note=In undifferentiated cultured
CC podocytes localizes to the perinuclear region and translocates to the
CC cell membrane after Cadherin appearance at cell-cell contacts. Upon
CC differentiation of cultured podocytes, protein disappears from cell
CC contacts and expression ceases. Re-expressed upon induced podocyte
CC injury. Colocalizes with FYB1 at cell-cell contacts in podocytes.
CC {ECO:0000269|PubMed:17195181, ECO:0000269|PubMed:21881001}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JJG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJG6-2; Sequence=VSP_034861;
CC -!- TISSUE SPECIFICITY: Expressed in podocytes (at protein level).
CC {ECO:0000269|PubMed:21881001}.
CC -!- DEVELOPMENTAL STAGE: Expression in kidney peaks at postnatal day 4 and
CC declines to undetectable levels by day 15. In adults very low
CC expression detected in the basal region of lateral membranes of few
CC tubule segments (at protein level). {ECO:0000269|PubMed:17195181}.
CC -!- SIMILARITY: Belongs to the TMEM47 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE21843.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB041540; BAA95025.1; -; mRNA.
DR EMBL; AK030761; BAC27126.1; -; mRNA.
DR EMBL; AK031346; BAC27357.1; -; mRNA.
DR EMBL; AK076147; BAC36217.1; -; mRNA.
DR EMBL; AK133790; BAE21843.1; ALT_FRAME; mRNA.
DR EMBL; AK162304; BAE36842.1; -; mRNA.
DR EMBL; AL671873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019751; AAH19751.1; -; mRNA.
DR CCDS; CCDS30254.1; -. [Q9JJG6-1]
DR RefSeq; NP_620090.1; NM_138751.2. [Q9JJG6-1]
DR AlphaFoldDB; Q9JJG6; -.
DR SMR; Q9JJG6; -.
DR IntAct; Q9JJG6; 3.
DR STRING; 10090.ENSMUSP00000026760; -.
DR iPTMnet; Q9JJG6; -.
DR PhosphoSitePlus; Q9JJG6; -.
DR MaxQB; Q9JJG6; -.
DR PaxDb; Q9JJG6; -.
DR PRIDE; Q9JJG6; -.
DR ProteomicsDB; 259584; -. [Q9JJG6-1]
DR ProteomicsDB; 259585; -. [Q9JJG6-2]
DR Antibodypedia; 71106; 33 antibodies from 9 providers.
DR DNASU; 192216; -.
DR Ensembl; ENSMUST00000026760; ENSMUSP00000026760; ENSMUSG00000025666. [Q9JJG6-1]
DR Ensembl; ENSMUST00000171953; ENSMUSP00000129793; ENSMUSG00000025666. [Q9JJG6-1]
DR GeneID; 192216; -.
DR KEGG; mmu:192216; -.
DR UCSC; uc009tre.2; mouse. [Q9JJG6-1]
DR CTD; 83604; -.
DR MGI; MGI:2177570; Tmem47.
DR VEuPathDB; HostDB:ENSMUSG00000025666; -.
DR eggNOG; KOG4671; Eukaryota.
DR GeneTree; ENSGT00530000063484; -.
DR HOGENOM; CLU_120054_1_0_1; -.
DR InParanoid; Q9JJG6; -.
DR OMA; EWSCNST; -.
DR OrthoDB; 1307601at2759; -.
DR PhylomeDB; Q9JJG6; -.
DR TreeFam; TF312855; -.
DR BioGRID-ORCS; 192216; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9JJG6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JJG6; protein.
DR Bgee; ENSMUSG00000025666; Expressed in median eminence of neurohypophysis and 248 other tissues.
DR Genevisible; Q9JJG6; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR InterPro; IPR015664; P53_induced.
DR PANTHER; PTHR14399; PTHR14399; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BQJ4"
FT CHAIN 2..181
FT /note="Transmembrane protein 47"
FT /id="PRO_0000072574"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQJ4"
FT VAR_SEQ 76..181
FT /note="DWQIATLALLLGGAAIILIAFLVGLISICVGSRRRFYRPVAVMLFAAVVLQV
FT CSLVLYPIKFIETVSLKIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY -> G
FT ERPHPTSGAAPLAPAWPSWAPPLPPPLWEPPPPLSFAPLPASLPYLLGPWTPGPSCMCP
FT SLEGVRVGKTPETSYALYSSLAHPSSFGVTRLLFWAIVIIEGENHVAV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034861"
SQ SEQUENCE 181 AA; 19995 MW; C797B52D502F676C CRC64;
MASAGSGMEE VRVSVLTPLK LVGLVCIFLA LCLDLGAVLS PAWVTADHQY YLSLWESCRK
PANLDIWHCE STLGSDWQIA TLALLLGGAA IILIAFLVGL ISICVGSRRR FYRPVAVMLF
AAVVLQVCSL VLYPIKFIET VSLKIYHEFN WGYGLAWGAT IFSFGGAILY CLNPKNYEDY
Y
