ID   CLVS1_RAT               Reviewed;         354 AA.
AC   A6JFQ6;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Clavesin-1 {ECO:0000303|PubMed:19651769};
DE   AltName: Full=Retinaldehyde-binding protein 1-like 1;
GN   Name=Clvs1 {ECO:0000303|PubMed:19651769};
GN   Synonyms=Rlbp1l1 {ECO:0000250|UniProtKB:Q8IUQ0};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19651769; DOI=10.1074/jbc.m109.034884;
RA   Katoh Y., Ritter B., Gaffry T., Blondeau F., Honing S., McPherson P.S.;
RT   "The clavesin family: neuron-specific lipid- and clathrin-binding Sec14
RT   proteins regulating lysosomal morphology.";
RL   J. Biol. Chem. 284:27646-27654(2009).
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). {ECO:0000250|UniProtKB:Q8IUQ0,
CC       ECO:0000269|PubMed:19651769}.
CC   -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin.
CC       {ECO:0000250|UniProtKB:Q8IUQ0}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:19651769}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:19651769}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q8IUQ0}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8IUQ0}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle {ECO:0000269|PubMed:19651769}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain with no expression detected in
CC       non-neuronal tissues (at protein level). {ECO:0000269|PubMed:19651769}.
CC   -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane
CC       and for binding PtdIns(3,5)P2. {ECO:0000250|UniProtKB:Q8IUQ0}.
CC   -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC       localization. {ECO:0000250|UniProtKB:Q8IUQ0}.
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DR   EMBL; CH473984; EDM11652.1; -; Genomic_DNA.
DR   RefSeq; NP_001102439.1; NM_001108969.1.
DR   AlphaFoldDB; A6JFQ6; -.
DR   SMR; A6JFQ6; -.
DR   STRING; 10116.ENSRNOP00000009744; -.
DR   PaxDb; A6JFQ6; -.
DR   PeptideAtlas; A6JFQ6; -.
DR   PRIDE; A6JFQ6; -.
DR   Ensembl; ENSRNOT00000009744; ENSRNOP00000009744; ENSRNOG00000006919.
DR   GeneID; 366311; -.
DR   KEGG; rno:366311; -.
DR   UCSC; RGD:1564200; rat.
DR   CTD; 157807; -.
DR   RGD; 1564200; Clvs1.
DR   eggNOG; KOG1471; Eukaryota.
DR   InParanoid; A6JFQ6; -.
DR   OrthoDB; 1182715at2759; -.
DR   PhylomeDB; A6JFQ6; -.
DR   Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR   PRO; PR:A6JFQ6; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Proteomes; UP000234681; Chromosome 5.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA: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; IDA: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; IMP: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   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Endosome; Golgi apparatus; Lipid-binding; Membrane;
KW   Reference proteome.
FT   CHAIN           1..354
FT                   /note="Clavesin-1"
FT                   /id="PRO_0000389619"
FT   DOMAIN          118..279
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          317..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  40667 MW;  C4A8C46E62368ACC CRC64;
     MGPVSVLPKP QSISTWEGDL AKMTHLQAGL SPDTIEKARL ELNENPDVLH QDIQQVRDMI
     ITRPDIGFLR TDDAFILRFL RARKFHQADA FRLLAQYFQY RQLNLDMFKN FKADDPGIKR
     ALIDGFPGVL ENRDHYGRKI LLLFAANWDQ SRNSFTDILR AILLSLEVLI EDPELQINGF
     ILIIDWSNFS FKQASKLTPS ILKLAIEGLQ DSFPARFGGV HFVNQPWYIH ALYTLIKPFL
     KDKTRKRIFL HGNNLNSLHQ LIHPEFLPSE FGGTLPPYDM GTWARTLLGP DYSDENDYTH
     TSYNAMYVKH TCSNLERECS PKPMKRSQSV VEAGTLKHEE KGENENTQPL LALD