ID   TM231_DANRE             Reviewed;         309 AA.
AC   Q7T316; E9QBY7; F1QPZ2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Transmembrane protein 231;
GN   Name=tmem231; ORFNames=zgc:64166;
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=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transmembrane component of the tectonic-like complex, a
CC       complex localized at the transition zone of primary cilia and acting as
CC       a barrier that prevents diffusion of transmembrane proteins between the
CC       cilia and plasma membranes. Required for ciliogenesis and sonic
CC       hedgehog/SHH signaling (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Note=Localizes to the
CC       transition zone of primary cilia; SEPT2 is required for localization to
CC       the transition zone. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TMEM231 family. {ECO:0000305}.
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DR   EMBL; BX890570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC053293; AAH53293.1; -; mRNA.
DR   RefSeq; NP_956681.1; NM_200387.1.
DR   AlphaFoldDB; Q7T316; -.
DR   STRING; 7955.ENSDARP00000061995; -.
DR   PaxDb; Q7T316; -.
DR   Ensembl; ENSDART00000061996; ENSDARP00000061995; ENSDARG00000042272.
DR   GeneID; 393358; -.
DR   KEGG; dre:393358; -.
DR   CTD; 79583; -.
DR   ZFIN; ZDB-GENE-040426-1386; tmem231.
DR   eggNOG; KOG4838; Eukaryota.
DR   GeneTree; ENSGT00390000015366; -.
DR   HOGENOM; CLU_070969_0_0_1; -.
DR   InParanoid; Q7T316; -.
DR   OMA; QLPARYH; -.
DR   OrthoDB; 1247968at2759; -.
DR   PhylomeDB; Q7T316; -.
DR   TreeFam; TF312969; -.
DR   PRO; PR:Q7T316; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 25.
DR   Bgee; ENSDARG00000042272; Expressed in testis and 28 other tissues.
DR   ExpressionAtlas; Q7T316; baseline.
DR   GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
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:0036038; C:MKS complex; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR019306; TMEM231.
DR   PANTHER; PTHR14605; PTHR14605; 1.
DR   Pfam; PF10149; TM231; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..309
FT                   /note="Transmembrane protein 231"
FT                   /id="PRO_0000317524"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        32
FT                   /note="G -> C (in Ref. 2; AAH53293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="N -> S (in Ref. 2; AAH53293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="R -> Q (in Ref. 2; AAH53293)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  35538 MW;  AC1142471944EA3B CRC64;
     MAFYDVYAHP ALIRYRTCVC TRATLFVCVV LGLTYISPLL VAYRSQGFWL KRNSYEEQPV
     VKFQYDLILL GVTDTTGNYL AWSTFPNFNR LIGDNLRIPE ISAQEEDKNQ DGKSDVLLLQ
     ISVPLKPAEQ MFSVQLLLTF SYQLFRMSTV VMQTLAFIQH SSPVPGSQLF ICGDLRLNQR
     TPLPHRGLHS TYNVSVIDGS SPFASTYDLT NIIRLYQQRN LTTHLSGVIP VWTVGRAANA
     PFQISAQIHY PVEMIDYRPG FWETIKFAWI QYVSVLLIFL WVFQHIQTFI FQNQVLPTIT
     IPPFKQHRS