ID   T237A_DANRE             Reviewed;         377 AA.
AC   F1Q930;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Transmembrane protein 237A;
DE   AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog A;
GN   Name=tmem237a; Synonyms=als2cr4a;
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   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; BX571704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001306065.1; NM_001319136.1.
DR   AlphaFoldDB; F1Q930; -.
DR   STRING; 7955.ENSDARP00000007797; -.
DR   PaxDb; F1Q930; -.
DR   Ensembl; ENSDART00000017593; ENSDARP00000007797; ENSDARG00000041735.
DR   GeneID; 557237; -.
DR   KEGG; dre:557237; -.
DR   CTD; 557237; -.
DR   ZFIN; ZDB-GENE-070402-3; tmem237a.
DR   eggNOG; ENOG502QTW0; Eukaryota.
DR   GeneTree; ENSGT00390000005159; -.
DR   HOGENOM; CLU_061097_0_0_1; -.
DR   InParanoid; F1Q930; -.
DR   OMA; THCACAR; -.
DR   OrthoDB; 1428687at2759; -.
DR   PhylomeDB; F1Q930; -.
DR   TreeFam; TF329703; -.
DR   PRO; PR:F1Q930; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 9.
DR   Bgee; ENSDARG00000041735; Expressed in retina and 12 other tissues.
DR   ExpressionAtlas; F1Q930; baseline and differential.
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   3: Inferred from homology;
KW   Cell projection; Cilium; Cilium biogenesis/degradation; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..377
FT                   /note="Transmembrane protein 237A"
FT                   /id="PRO_0000415831"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  42869 MW;  FDE1F289276155E3 CRC64;
     MCVTSRADKM PSVKPKKKKI KKEINEVEEP EAGPEPAIEM EGLESRRQSE SREPLTPEPH
     DNPPLKKKKK KKTHTFENEG EQQDHPNGDV QESPTDGEEV TKKSKKKRKN KMMENQSHNE
     LGVEEDDIIT DVHAPISQRS LFSAPLSHSH PIGKVFVEKN RRFQATDLSH DHLEEYMEVR
     PMWNTRDVAM RVHSGFRIIG LFSHGFLAGY AVWNIIVVYV LAGEQMTTLP NLLQQYHSLA
     YPAQSLLYLL LAISTVSAFD RVNLAKASMA LRGFLTLDPA ALASFLYFAA LILSLSQQMT
     SDRIHLYPTA NETLWPPGLE HQILQPWIVV NLVVALLVGL AWVFVATRPD MDYTEEFLMA
     MEVEEYPRHD DKHELAA