T161B_DANRE
ID T161B_DANRE Reviewed; 484 AA.
AC Q7SY10;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Transmembrane protein 161B;
GN Name=tmem161b; ORFNames=si:dkey-195m1.1, zgc:63626;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=33597309; DOI=10.1073/pnas.2018220118;
RA Koopman C.D., De Angelis J., Iyer S.P., Verkerk A.O., Da Silva J.,
RA Berecki G., Jeanes A., Baillie G.J., Paterson S., Uribe V., Ehrlich O.V.,
RA Robinson S.D., Garric L., Petrou S., Simons C., Vetter I., Hogan B.M.,
RA de Boer T.P., Bakkers J., Smith K.A.;
RT "The zebrafish grime mutant uncovers an evolutionarily conserved role for
RT Tmem161b in the control of cardiac rhythm.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Essential for maintaining normal cardiac rhythm in the
CC developing heart and for neonatal survival (PubMed:33597309). Inhibits
CC potassium and calcium currents in the cardiomyocytes, this assists in
CC timely action potential repolarization and thereby maintains normal
CC cardiac rhythm (PubMed:33597309). {ECO:0000269|PubMed:33597309}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33597309};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutants display highly specific cardiac
CC arrhythmia and die by 15 days post-fertilization (dpf)
CC (PubMed:33597309). Exhibit skipped ventricular beats, irregular beats
CC and slower heart rate but their hearts are morphologically
CC indistinguishable from wild-type counterparts (PubMed:33597309).
CC Increased potassium and calcium currents observed in isolated
CC cardiomyocytes (PubMed:33597309). {ECO:0000269|PubMed:33597309}.
CC -!- SIMILARITY: Belongs to the TMEM161 family. {ECO:0000305}.
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DR EMBL; BX470189; CAM15252.1; -; Genomic_DNA.
DR EMBL; CR405703; CAM15252.1; JOINED; Genomic_DNA.
DR EMBL; CR405703; CAM16671.1; -; Genomic_DNA.
DR EMBL; BX470189; CAM16671.1; JOINED; Genomic_DNA.
DR EMBL; BC055170; AAH55170.1; -; mRNA.
DR RefSeq; NP_998536.1; NM_213371.1.
DR AlphaFoldDB; Q7SY10; -.
DR STRING; 7955.ENSDARP00000072863; -.
DR PaxDb; Q7SY10; -.
DR Ensembl; ENSDART00000078401; ENSDARP00000072863; ENSDARG00000055989.
DR GeneID; 406680; -.
DR KEGG; dre:406680; -.
DR CTD; 153396; -.
DR ZFIN; ZDB-GENE-040426-2693; tmem161b.
DR eggNOG; KOG3978; Eukaryota.
DR GeneTree; ENSGT00390000000672; -.
DR HOGENOM; CLU_027277_0_0_1; -.
DR InParanoid; Q7SY10; -.
DR OMA; RFALMPI; -.
DR OrthoDB; 734854at2759; -.
DR PhylomeDB; Q7SY10; -.
DR TreeFam; TF314570; -.
DR PRO; PR:Q7SY10; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000055989; Expressed in mature ovarian follicle and 31 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IMP:UniProtKB.
DR GO; GO:0002027; P:regulation of heart rate; IMP:UniProtKB.
DR InterPro; IPR019395; Transmembrane_161A/B.
DR PANTHER; PTHR13624; PTHR13624; 1.
DR Pfam; PF10268; Tmemb_161AB; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..484
FT /note="Transmembrane protein 161B"
FT /id="PRO_0000288091"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 54687 MW; 364E67A3E170656F CRC64;
MGVISVQLVV TMVMASVIQK IIPHYSFARW LLCSGSLRWY QHPTEDELRT LAGKQQKGGK
SKKDRKYNGH LENKPMTIPK DIDLQLETKC IAEVDTLALH YFPEFQWLVD FTVAATVVYL
ITELYFCVAE PSGEMNISVV WSLLVLAFVM KILFSLTAHY FRLEEGGERS LCITFAFFFF
VKAMAILIVT ENYLEFGLET GFANFSESAV QFLENQGLES QGPISKLTFK LILALLCALI
GAFLTFPGLR LAQMHLDALT LNNCKVTQTL LHINFLAPLI MVLLWVKPIT KDYITNPTFG
KDNVPLMSEK TYDTLRLWVI LLLCVLRLAM MRHHLQAYLN LAQKGVLQMK KEAGRISTVD
LQKMVARVFY YLCVIALQYI APLVMLLHTT LLLKTLGGHS WVIYSDESLP CLSNEDSSPA
EVGQSQMEAS QTVAQLSVAL GGLRTVFSPL LFRGLLSFFT WWIAACLFST SLFGLFYHQY
LMAA
