ID   T132E_DANRE             Reviewed;        1073 AA.
AC   L7VG99;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Transmembrane protein 132E;
DE   Flags: Precursor;
GN   Name=tmem132e;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25331638; DOI=10.1002/humu.22712;
RA   Li J., Zhao X., Xin Q., Shan S., Jiang B., Jin Y., Yuan H., Dai P.,
RA   Xiao R., Zhang Q., Xiao J., Shao C., Gong Y., Liu Q.;
RT   "Whole-exome sequencing identifies a variant in TMEM132E causing autosomal-
RT   recessive nonsyndromic hearing loss DFNB99.";
RL   Hum. Mutat. 36:98-105(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Required for normal inner ear hair cell function and hearing.
CC       {ECO:0000269|PubMed:25331638}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC       delayed sound-induced startle response and circular swimming behavior.
CC       Morphants show significantly reduced extracellular receptor potentials
CC       and impaired mechanoelectrical transduction in hair cells of inner ear
CC       relative to controls. {ECO:0000269|PubMed:25331638}.
CC   -!- SIMILARITY: Belongs to the TMEM132 family. {ECO:0000305}.
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DR   EMBL; JX995104; AGC65591.1; -; mRNA.
DR   EMBL; CR388016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FP067411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU929235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001289163.1; NM_001302234.1.
DR   AlphaFoldDB; L7VG99; -.
DR   SMR; L7VG99; -.
DR   STRING; 7955.ENSDARP00000107971; -.
DR   PaxDb; L7VG99; -.
DR   Ensembl; ENSDART00000130565; ENSDARP00000107971; ENSDARG00000090830.
DR   GeneID; 564044; -.
DR   KEGG; dre:564044; -.
DR   CTD; 124842; -.
DR   ZFIN; ZDB-GENE-120926-3; tmem132e.
DR   eggNOG; KOG4789; Eukaryota.
DR   GeneTree; ENSGT00940000158479; -.
DR   HOGENOM; CLU_009871_0_0_1; -.
DR   OrthoDB; 598074at2759; -.
DR   Reactome; R-DRE-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-DRE-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:L7VG99; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000090830; Expressed in retina and 20 other tissues.
DR   ExpressionAtlas; L7VG99; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0060117; P:auditory receptor cell development; IMP:ZFIN.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:ZFIN.
DR   GO; GO:0035677; P:posterior lateral line neuromast hair cell development; IMP:ZFIN.
DR   InterPro; IPR026307; TMEM132.
DR   InterPro; IPR031436; TMEM132_C.
DR   InterPro; IPR031437; TMEM132_M.
DR   InterPro; IPR031435; TMEM132_N.
DR   PANTHER; PTHR13388; PTHR13388; 1.
DR   Pfam; PF16070; TMEM132; 1.
DR   Pfam; PF15706; TMEM132D_C; 1.
DR   Pfam; PF15705; TMEM132D_N; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..1073
FT                   /note="Transmembrane protein 132E"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000433801"
FT   TOPO_DOM        34..899
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        900..920
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        921..1073
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          246..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1001..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        746
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1073 AA;  119140 MW;  15B629396BF2E479 CRC64;
     MGHFVVQGDL PWILCSLRLV IMIIAGKVSP TSSDALFSVP VPSATSSPPE VYLPATFKLS
     NTQLAFFLQE NRAPSYGSQR GHPLQRSESF VVFQTKELPA VNISLGPFTQ DQTLSKDLLQ
     PSSPLDIPGR LTVNWKVRAF IVQSRVYASN PLVQVLFYIA GRDWDDFKIQ DKLPCVRLHA
     FRDVREIKTS CRLQGNLAQC LAQLDLPSTW FNVNVAPLGR RKSSGTDGLE LTGETLQVEL
     YYTLHDPDSN DECGESYPRR GGPSRGESLS QQPLLRIGSI SLYQPSQEQL VVDKQLDKNL
     FLRLPERPLK PGETLNIYLL LVPNSTVEQF TLKVKAKKGV NLLSTKSRSN QWRVEWDMQS
     GAKHSIATVE ASKIKGVSGD MAGSIEIMQL DFEMENFTSQ SVTRRINWNI DYRGQNPTSD
     AEKVVTELTV VQKDIQAIIP LSMDTEIINT AVLTGRTVAI PVKVVSIELN GAVTDVSSSV
     QCKSFNEDIV KVSMNCDYVF VNGKETRGSM NARVIFSYEH LSAPLELTVW VPKLPLKVEL
     SDNRLSFIKG WRVPILPDRR TARDSDDDDD DDRKVSRGCT LQYQRAQIKV LTQFHTTSSE
     GTNQMITMLG PDWQVDVTEL VQDSLKVVDG RVAELADRTV LVANELGSST LKVESPLAVE
     AVLGETQFSV VDEKVSIVEL RVHAISGLAL NLQPSPGNSH TMVAKATGLQ TLSTLKQEAS
     FSIWVYYSDN TAAPLSMYDP KDYNLNGTSA DDKVVTVAQQ PQQRWPVIIA EGEGTGDIVH
     VEMTISETCQ KTKRKSVIAS SSVFVKVRFG TDEDSEEDME METEIDTRMP ANTRRPAIDS
     NVGGAGYEPS NEQPASVPID YTNFPTISNP EEPTEEDEED DEFVHSPRSM TDLEIGMYAL
     LGVFCLAILV FLINCIVFVL KYRHKRIPPE GQANMDHSHH WVFLGNGEPL RTQSDLSPQT
     VESPSNTLEG VQTCCHGDHH SSGSSQTSVQ SQVHGRGDGS SGGSTKDHGE DASSPTSKRK
     RVKFTTFTLP TEDLPYNSIP IANEEDIQWV CQDMGFQDQE ELHDYMRRIK EIA