ID   CLVS2_DANRE             Reviewed;         329 AA.
AC   Q5SPP0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Clavesin-2;
DE   AltName: Full=Retinaldehyde-binding protein 1-like 2;
GN   Name=clvs2; Synonyms=rlbp1l2; ORFNames=si:ch211-199i15.4;
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=Brain;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for normal morphology of late endosomes and/or
CC       lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate
CC       (PtdIns(3,5)P2) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early
CC       endosome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000250}.
CC   -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane
CC       and for binding PtdIns(3,5)P2. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC       localization. {ECO:0000250}.
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DR   EMBL; AL845421; CAI11724.1; -; Genomic_DNA.
DR   EMBL; BC116475; AAI16476.1; -; mRNA.
DR   RefSeq; NP_001020716.1; NM_001025545.2.
DR   AlphaFoldDB; Q5SPP0; -.
DR   SMR; Q5SPP0; -.
DR   STRING; 7955.ENSDARP00000069597; -.
DR   PaxDb; Q5SPP0; -.
DR   PRIDE; Q5SPP0; -.
DR   Ensembl; ENSDART00000075112; ENSDARP00000069597; ENSDARG00000053122.
DR   GeneID; 566769; -.
DR   KEGG; dre:566769; -.
DR   CTD; 134829; -.
DR   ZFIN; ZDB-GENE-041014-313; clvs2.
DR   eggNOG; KOG1471; Eukaryota.
DR   GeneTree; ENSGT00940000157632; -.
DR   HOGENOM; CLU_046597_1_3_1; -.
DR   InParanoid; Q5SPP0; -.
DR   OMA; TQNYYPE; -.
DR   OrthoDB; 872816at2759; -.
DR   PhylomeDB; Q5SPP0; -.
DR   Reactome; R-DRE-432720; Lysosome Vesicle Biogenesis.
DR   PRO; PR:Q5SPP0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000053122; Expressed in retina and 4 other tissues.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; -; 1.
DR   InterPro; IPR028636; Clavesin-2.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   PANTHER; PTHR10174:SF73; PTHR10174:SF73; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF46938; SSF46938; 1.
DR   SUPFAM; SSF52087; SSF52087; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Endosome; Golgi apparatus; Lipid-binding; Membrane;
KW   Reference proteome.
FT   CHAIN           1..329
FT                   /note="Clavesin-2"
FT                   /id="PRO_0000297654"
FT   DOMAIN          96..257
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          293..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  38120 MW;  760ED137A0BB6C77 CRC64;
     MTHLQAGLSP ETLEKAKVEL KENPDTLHQD IQEVRDMIIT RPDIGFLRTD DAFILRFLRA
     RKFNHFEAFR LLAQYFEYRQ QNLDMFKNLK ATDPGIKQAL KDGFPGVLSN LDRYGRKILV
     LFAANWDQSR YTFVDILRAI LLSLEAMIED PELQVNGFVL IIDWSNFTFK QASKLTPSML
     RLAIEGLQDS FPARFGGIHF VNQPWYIHAL YTVIRPFLKD KTRKRIFMHG NNLNSLHQLI
     LPEILPSELG GMLPPYDMGT WARTLLDHAY DEETDYCPES YTLSVKDLEK DLSPKTMKRS
     QSVVEPGVLK RPEKVKSEEE NMQPLLSLD