ID   CLVS1_XENLA             Reviewed;         332 AA.
AC   Q5M7E1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Clavesin-1;
DE   AltName: Full=Retinaldehyde-binding protein 1-like 1;
GN   Name=clvs1; Synonyms=rlbp1l1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) 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; BC088689; AAH88689.1; -; mRNA.
DR   RefSeq; NP_001088883.1; NM_001095414.1.
DR   RefSeq; XP_018122140.1; XM_018266651.1.
DR   RefSeq; XP_018122141.1; XM_018266652.1.
DR   AlphaFoldDB; Q5M7E1; -.
DR   SMR; Q5M7E1; -.
DR   DNASU; 496227; -.
DR   GeneID; 496227; -.
DR   KEGG; xla:496227; -.
DR   CTD; 496227; -.
DR   Xenbase; XB-GENE-5740452; clvs1.L.
DR   OMA; LCECNIC; -.
DR   OrthoDB; 1182715at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 496227; Expressed in testis and 3 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: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; IPR028634; Clavesin-1.
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:SF72; PTHR10174:SF72; 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..332
FT                   /note="Clavesin-1"
FT                   /id="PRO_0000297658"
FT   DOMAIN          96..257
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          300..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  38530 MW;  B919E636A6CC1251 CRC64;
     MTHLHAGLNP ETIEKGRLEL NENPDTLHQD IQQVRDMIIT RPDIGFLRTD DAFILRFLRA
     RKFNQMEAFR LLAQYFQYRQ LNLDMFKNLK ADDPGIKRAL MDGFPGVLEN RDHYGRKILL
     LFAANWDQSR NSFVDILRAI LLSLEVLIED QELQINGFIL IIDWSNFSFK QASKLTPSIL
     RLAIEGLQDS FPARFGGVHF VNQPWYIHAL YTIIKPFLKD KTRKRIFLHG NNLNSLHQLI
     HPDCLPSEFG GTLPPYDMGT WARTLLGPDY NDENEYTHSS YNVIHVKHVP AIVEGEDSPK
     YMKRSHSVVE PGTLRHEEER ENENTQPLLA LD