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 27-MAR-2024, entry version 94.
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.ENSMFAP00000033574; -.
DR Ensembl; ENSMFAT00000007802.2; ENSMFAP00000033574.1; ENSMFAG00000003285.2.
DR GeneID; 102115352; -.
DR KEGG; mcf:102115352; -.
DR CTD; 134829; -.
DR VEuPathDB; HostDB:ENSMFAG00000003285; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000157632; -.
DR OMA; QNERLCD; -.
DR OrthoDB; 2943211at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000003285; Expressed in cerebellum and 3 other cell types or 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; 1.20.5.1200; Alpha-tocopherol transfer; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 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; ALPHA-TOCOPHEROL TRANSFER PROTEIN-RELATED; 1.
DR PANTHER; PTHR10174:SF73; CLAVESIN-2; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR PRINTS; PR00180; CRETINALDHBP.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 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
//
