CLVS2_RAT
ID CLVS2_RAT Reviewed; 327 AA.
AC A6JUQ6;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Clavesin-2 {ECO:0000303|PubMed:19651769};
DE AltName: Full=Retinaldehyde-binding protein 1-like 2;
GN Name=Clvs2 {ECO:0000303|PubMed:19651769};
GN Synonyms=Rlbp1l2 {ECO:0000312|RGD:1306801};
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:Q5SYC1,
CC ECO:0000269|PubMed:19651769}.
CC -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin.
CC {ECO:0000250|UniProtKB:Q5SYC1}.
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:Q5SYC1}.
CC -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC localization. {ECO:0000250|UniProtKB:Q8IUQ0}.
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DR EMBL; CH474002; EDL87721.1; -; Genomic_DNA.
DR AlphaFoldDB; A6JUQ6; -.
DR SMR; A6JUQ6; -.
DR STRING; 10116.ENSRNOP00000016518; -.
DR iPTMnet; A6JUQ6; -.
DR PhosphoSitePlus; A6JUQ6; -.
DR PaxDb; A6JUQ6; -.
DR PRIDE; A6JUQ6; -.
DR Ensembl; ENSRNOT00000092830; ENSRNOP00000075964; ENSRNOG00000012122.
DR UCSC; RGD:1306801; rat.
DR RGD; 1306801; Clvs2.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000157632; -.
DR HOGENOM; CLU_046597_1_3_1; -.
DR InParanoid; A6JUQ6; -.
DR OMA; TQNYYPE; -.
DR PhylomeDB; A6JUQ6; -.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR PRO; PR:A6JUQ6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000012122; Expressed in brain and 5 other tissues.
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; 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 1: Evidence at protein 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_0000389620"
FT DOMAIN 96..257
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 288..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 327 AA; 37916 MW; EA51B1EBCEDDDAB7 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 YSMPVNEVDK ELSPKSMKRS
QSVVDPTALK RMDKSEEENM QPLLSLD
