ID   CLVS2_MACFA             Reviewed;         327 AA.
AC   Q95KF7; Q9BE37;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Clavesin-2;
DE   AltName: Full=Retinaldehyde-binding protein 1-like 2;
GN   Name=CLVS2; Synonyms=RLBP1L2; ORFNames=QccE-21404, QtrA-13887;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Temporal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (APR-2001) 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   -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin.
CC       {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; AB060190; BAB41140.1; -; mRNA.
DR   EMBL; AB060902; BAB46902.1; -; mRNA.
DR   RefSeq; NP_001306321.1; NM_001319392.1.
DR   RefSeq; XP_005551772.1; XM_005551715.2.
DR   AlphaFoldDB; Q95KF7; -.
DR   SMR; Q95KF7; -.
DR   STRING; 9541.XP_005551772.1; -.
DR   Ensembl; ENSMFAT00000007802; ENSMFAP00000033574; ENSMFAG00000003285.
DR   GeneID; 102115352; -.
DR   KEGG; mcf:102115352; -.
DR   CTD; 134829; -.
DR   VEuPathDB; HostDB:ENSMFAG00000003285; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   GeneTree; ENSGT00940000157632; -.
DR   OMA; TQNYYPE; -.
DR   OrthoDB; 872816at2759; -.
DR   Proteomes; UP000233100; Chromosome 4.
DR   Bgee; ENSMFAG00000003285; Expressed in cerebellum 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; 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   Phosphoprotein; Reference proteome.
FT   CHAIN           1..327
FT                   /note="Clavesin-2"
FT                   /id="PRO_0000297652"
FT   DOMAIN          96..257
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          287..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A6JUQ6"
FT   CONFLICT        101
FT                   /note="K -> R (in Ref. 1; BAB46902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="I -> T (in Ref. 1; BAB41140)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="H -> R (in Ref. 1; BAB41140)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  38000 MW;  FF40A5A222A4DB1C CRC64;
     MTHLQAGLSP ETLEKARLEL NENPDTLHQD IQEVRDMVIT RPDIGFLRTD DAFILRFLRA
     RKFHHFEAFR LLAQYFEYRQ QNLDMFKSFK ATDPGIKQAL KDGFPGGLAN LDHYGRKILV
     LFAANWDQSR YTLVDILRAI LLSLEAMIED PELQVNGFVL IIDWSNFTFK QASKLTPSML
     RLAIEGLQDS FPARFGGIHF VNQPWYIHAL YTVIRPFLKE KTRKRIFLHG NNLNSLHQLI
     HPEILPSEFG GMLPPYDMGT WARTLLDHEY DDDSEYNVDS YSMPVKEVEK ELSPKSMKRS
     QSVVDPTVLK RMDKNEEENM QPLLSLD