T237B_DANRE
ID T237B_DANRE Reviewed; 413 AA.
AC Q66IE4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Transmembrane protein 237B;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog B;
GN Name=tmem237b; Synonyms=als2cr4b; ORFNames=zgc:101660;
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 TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22152675; DOI=10.1016/j.ajhg.2011.11.005;
RA Huang L., Szymanska K., Jensen V.L., Janecke A.R., Innes A.M., Davis E.E.,
RA Frosk P., Li C., Willer J.R., Chodirker B.N., Greenberg C.R., McLeod D.R.,
RA Bernier F.P., Chudley A.E., Muller T., Shboul M., Logan C.V., Loucks C.M.,
RA Beaulieu C.L., Bowie R.V., Bell S.M., Adkins J., Zuniga F.I., Ross K.D.,
RA Wang J., Ban M.R., Becker C., Nurnberg P., Douglas S., Craft C.M.,
RA Akimenko M.A., Hegele R.A., Ober C., Utermann G., Bolz H.J., Bulman D.E.,
RA Katsanis N., Blacque O.E., Doherty D., Parboosingh J.S., Leroux M.R.,
RA Johnson C.A., Boycott K.M.;
RT "TMEM237 is mutated in individuals with a Joubert syndrome related disorder
RT and expands the role of the TMEM family at the ciliary transition zone.";
RL Am. J. Hum. Genet. 89:713-730(2011).
CC -!- FUNCTION: Component of the transition zone in primary cilia. Required
CC for ciliogenesis. {ECO:0000269|PubMed:22152675}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell projection, cilium {ECO:0000250}.
CC Note=Localizes to the transition zone. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Fishes lacking both tmem237a and tmem237b display
CC defects in midsomitic embryos, including shortening of the anterior-
CC posterior axis and small anterior structures, kinking of the notochord,
CC and broadening and thinning of the somite.
CC {ECO:0000269|PubMed:22152675}.
CC -!- SIMILARITY: Belongs to the TMEM237 family. {ECO:0000305}.
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DR EMBL; CU570787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081384; AAH81384.1; -; mRNA.
DR RefSeq; NP_001004636.1; NM_001004636.1.
DR AlphaFoldDB; Q66IE4; -.
DR STRING; 7955.ENSDARP00000010454; -.
DR PaxDb; Q66IE4; -.
DR Ensembl; ENSDART00000005573; ENSDARP00000010454; ENSDARG00000074248.
DR GeneID; 447898; -.
DR KEGG; dre:447898; -.
DR CTD; 447898; -.
DR ZFIN; ZDB-GENE-040912-63; tmem237b.
DR eggNOG; ENOG502QTW0; Eukaryota.
DR GeneTree; ENSGT00390000005159; -.
DR HOGENOM; CLU_061097_0_0_1; -.
DR InParanoid; Q66IE4; -.
DR OMA; FGLYCHG; -.
DR OrthoDB; 1428687at2759; -.
DR PhylomeDB; Q66IE4; -.
DR TreeFam; TF329703; -.
DR PRO; PR:Q66IE4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000074248; Expressed in retina and 32 other tissues.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IGI:ZFIN.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISS:UniProtKB.
DR InterPro; IPR029409; TMEM237.
DR PANTHER; PTHR28388; PTHR28388; 1.
DR Pfam; PF15383; TMEM237; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..413
FT /note="Transmembrane protein 237B"
FT /id="PRO_0000415832"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45969 MW; E68806A1760B24AD CRC64;
MDPEAKVSSS RRRDLPPIPQ GQRRTPRALP SMPSQDTAEE MPAPKSRKKK AKRDAESVDE
PDDGGMEMGG LASRRQSECP EPLTPEPLDN PPQRRKKKKK AQAIDAEGDQ TDLVSNGDTL
DQNTDEEVTR KPKKRKVKPK VTETQSNNEL DVEDDDVITD PQSPIPQHSL FSAPQGPSQP
VGKVFVEKSR RFQAADRVEQ WKPSGPIEQS IMDIRSMWTT RDVSMRVHSG FRVIGLFSHG
FLAGYAVWNI IVVYVLAGDQ MSSLSNLLQQ FHTLAYPAQS LLYLLLALST VSAFDRVNLA
KAPAAMRSLL RLSPVALASV FYFSALVLSL SQQMTSDRIN LYKYSSYNTT LWPPGSESSI
LYPWITVNLV VSLLVGLAWI LMSTSPDIDN TEAFLMSMEM EYPNSEEKGN VTA