TMM47_HUMAN
ID TMM47_HUMAN Reviewed; 181 AA.
AC Q9BQJ4; Q5JR44;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transmembrane protein 47;
DE AltName: Full=Brain cell membrane protein 1;
DE AltName: Full=Transmembrane 4 superfamily member 10;
GN Name=TMEM47; Synonyms=BCMP1, TM4SF10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=24603971; DOI=10.1371/journal.pone.0090852;
RA Utami K.H., Hillmer A.M., Aksoy I., Chew E.G., Teo A.S., Zhang Z.,
RA Lee C.W., Chen P.J., Seng C.C., Ariyaratne P.N., Rouam S.L., Soo L.S.,
RA Yousoof S., Prokudin I., Peters G., Collins F., Wilson M., Kakakios A.,
RA Haddad G., Menuet A., Perche O., Tay S.K., Sung K.W., Ruan X., Ruan Y.,
RA Liu E.T., Briault S., Jamieson R.V., Davila S., Cacheux V.;
RT "Detection of chromosomal breakpoints in patients with developmental delay
RT and speech disorders.";
RL PLoS ONE 9:E90852-E90852(2014).
RN [6]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
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. During podocyte differentiation may negatively regulate
CC activity of FYN and subsequently the abundance of nephrin (By
CC similarity). {ECO:0000250|UniProtKB:Q9JJG6,
CC ECO:0000250|UniProtKB:Q9XSV3}.
CC -!- SUBUNIT: Interacts with CTNNB1, CTNNA1, PRKCI, PARD6B, FYB1.
CC {ECO:0000250|UniProtKB:Q9JJG6, ECO:0000250|UniProtKB:Q9XSV3}.
CC -!- INTERACTION:
CC Q9BQJ4; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-13370320, EBI-18304435;
CC Q9BQJ4; P42858: HTT; NbExp=3; IntAct=EBI-13370320, EBI-466029;
CC Q9BQJ4; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-13370320, EBI-17498703;
CC Q9BQJ4; Q96L08: SUSD3; NbExp=3; IntAct=EBI-13370320, EBI-18194029;
CC Q9BQJ4; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-13370320, EBI-11724423;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9XSV3}. Note=Colocalizes with FYB1 at cell-cell
CC contacts in podocytes. {ECO:0000250|UniProtKB:Q9JJG6}.
CC -!- TISSUE SPECIFICITY: Expressed in adult brain, fetal brain, cerebellum,
CC heart, lung, prostate and thyroid. {ECO:0000269|PubMed:24603971}.
CC -!- SIMILARITY: Belongs to the TMEM47 family. {ECO:0000305}.
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DR EMBL; AL136550; CAB66485.1; -; mRNA.
DR EMBL; AL596285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039242; AAH39242.1; -; mRNA.
DR CCDS; CCDS14235.1; -.
DR RefSeq; NP_113630.1; NM_031442.3.
DR AlphaFoldDB; Q9BQJ4; -.
DR SMR; Q9BQJ4; -.
DR BioGRID; 123695; 9.
DR IntAct; Q9BQJ4; 5.
DR STRING; 9606.ENSP00000275954; -.
DR TCDB; 8.A.16.4.4; the ca(+) channel auxiliary subunit Gama1-Gama8 (ccaGama) family.
DR iPTMnet; Q9BQJ4; -.
DR PhosphoSitePlus; Q9BQJ4; -.
DR SwissPalm; Q9BQJ4; -.
DR BioMuta; TMEM47; -.
DR DMDM; 51316912; -.
DR EPD; Q9BQJ4; -.
DR jPOST; Q9BQJ4; -.
DR MassIVE; Q9BQJ4; -.
DR PaxDb; Q9BQJ4; -.
DR PeptideAtlas; Q9BQJ4; -.
DR PRIDE; Q9BQJ4; -.
DR ProteomicsDB; 78693; -.
DR Antibodypedia; 71106; 33 antibodies from 9 providers.
DR DNASU; 83604; -.
DR Ensembl; ENST00000275954.4; ENSP00000275954.3; ENSG00000147027.4.
DR GeneID; 83604; -.
DR KEGG; hsa:83604; -.
DR MANE-Select; ENST00000275954.4; ENSP00000275954.3; NM_031442.4; NP_113630.1.
DR UCSC; uc004ddh.3; human.
DR CTD; 83604; -.
DR DisGeNET; 83604; -.
DR GeneCards; TMEM47; -.
DR HGNC; HGNC:18515; TMEM47.
DR HPA; ENSG00000147027; Low tissue specificity.
DR MIM; 300698; gene.
DR neXtProt; NX_Q9BQJ4; -.
DR OpenTargets; ENSG00000147027; -.
DR PharmGKB; PA134971248; -.
DR VEuPathDB; HostDB:ENSG00000147027; -.
DR eggNOG; KOG4671; Eukaryota.
DR GeneTree; ENSGT00530000063484; -.
DR HOGENOM; CLU_120054_1_0_1; -.
DR InParanoid; Q9BQJ4; -.
DR OMA; EWSCNST; -.
DR OrthoDB; 1307601at2759; -.
DR PhylomeDB; Q9BQJ4; -.
DR TreeFam; TF312855; -.
DR PathwayCommons; Q9BQJ4; -.
DR SignaLink; Q9BQJ4; -.
DR BioGRID-ORCS; 83604; 10 hits in 694 CRISPR screens.
DR ChiTaRS; TMEM47; human.
DR GeneWiki; TMEM47; -.
DR GenomeRNAi; 83604; -.
DR Pharos; Q9BQJ4; Tdark.
DR PRO; PR:Q9BQJ4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9BQJ4; protein.
DR Bgee; ENSG00000147027; Expressed in choroid plexus epithelium and 204 other tissues.
DR ExpressionAtlas; Q9BQJ4; baseline and differential.
DR Genevisible; Q9BQJ4; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
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; Cell junction; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052"
FT CHAIN 2..181
FT /note="Transmembrane protein 47"
FT /id="PRO_0000072573"
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:0000269|PubMed:25489052"
SQ SEQUENCE 181 AA; 19998 MW; A73A03FD0C3B3FBB CRC64;
MASAGSGMEE VRVSVLTPLK LVGLVCIFLA LCLDLGAVLS PAWVTADHQY YLSLWESCRK
PASLDIWHCE STLSSDWQIA TLALLLGGAA IILIAFLVGL ISICVGSRRR FYRPVAVMLF
AAVVLQVCSL VLYPIKFIET VSLKIYHEFN WGYGLAWGAT IFSFGGAILY CLNPKNYEDY
Y
