ID HSV2_CANAL Reviewed; 595 AA. AC Q59P11; A0A1D8PMA8; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=SVP1-like protein 2; GN Name=HSV2; OrderedLocusNames=CAALFM_C405350WA; GN ORFNames=CaO19.1793, CaO19.9359; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). CC -!- FUNCTION: Involved in mitochondrial or peroxisomal functions and amino CC acid signaling pathways. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. CC Note=Vesicular and vacuolar. {ECO:0000250}. CC -!- DOMAIN: May contain a beta-propeller domain involved in specific CC binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the CC association of the protein to the membrane. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP017626; AOW29274.1; -; Genomic_DNA. DR RefSeq; XP_711441.1; XM_706349.2. DR AlphaFoldDB; Q59P11; -. DR SMR; Q59P11; -. DR STRING; 237561.Q59P11; -. DR EnsemblFungi; C4_05350W_A-T; C4_05350W_A-T-p1; C4_05350W_A. DR GeneID; 3646948; -. DR KEGG; cal:CAALFM_C405350WA; -. DR CGD; CAL0000194175; orf19.9359. DR VEuPathDB; FungiDB:C4_05350W_A; -. DR eggNOG; KOG2111; Eukaryota. DR HOGENOM; CLU_025895_0_1_1; -. DR InParanoid; Q59P11; -. DR OMA; WSFCKFQ; -. DR OrthoDB; 391429at2759; -. DR PRO; PR:Q59P11; -. DR Proteomes; UP000000559; Chromosome 4. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central. DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central. DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central. DR GO; GO:0044804; P:nucleophagy; IBA:GO_Central. DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR048720; PROPPIN. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR11227:SF18; WD REPEAT DOMAIN PHOSPHOINOSITIDE-INTERACTING PROTEIN 3; 1. DR PANTHER; PTHR11227; WD-REPEAT PROTEIN INTERACTING WITH PHOSPHOINOSIDES WIPI -RELATED; 1. DR Pfam; PF21032; PROPPIN; 1. DR SMART; SM00320; WD40; 3. DR SUPFAM; SSF50978; WD40 repeat-like; 1. PE 3: Inferred from homology; KW Cytoplasmic vesicle; Membrane; Protein transport; Reference proteome; KW Repeat; Transport; Vacuole; WD repeat. FT CHAIN 1..595 FT /note="SVP1-like protein 2" FT /id="PRO_0000051025" FT REPEAT 30..68 FT /note="WD 1" FT REPEAT 389..429 FT /note="WD 2" FT REPEAT 434..473 FT /note="WD 3" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 76..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 264..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 467..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 595 AA; 64279 MW; C7A833CF32C322CA CRC64; MVLAHSINTN PNTNTNTNNT STTSSTTTIP NDSKILCINF NQDQGCFAIS HEQGFLVYNT DPIELRVKRN FIVNSHTTSS RSNHSNGSNS NNNHRNNSTG SNGSVSSSGS NNETTLGYKS THKSASGSGS GSGSGIGHIS MLHRTNYLAL IGGGENPKFP INKLIIWDDL KRKTSLSLEF DTPVLNVLLS RVRIIVVLID QIIVYGFAAP PKKFQTFNTI NNPLGIADLS VNSQQSNVHL YNNYSSNSAQ AQVSGTTTTT HYDFSKRKSL SPTNSSNSSS TSLKENGTNL TTYPSPSSTT SASASVATIT NTPEAATTAN PTTATTTATT TATTTTTTTS AKPLVNGIGS SYQTLAFPGR SMGQIQIVDV GNNHHSGTNI KPTINIIKAH KSNIRCLCLN RTGTLIASAS ITGTIIRIHS TRTTALLYEF RRGIDRAIIT SMKFSHDDSK LAVLSDKHTL HVYNIDETQY PNDGGSGGTK DGGGGGRGSK NRHHLLNGLL PYLPNYFQST WSFCSVNTNK YHTSDLEDNS QQQQQQWVAN GTGGGGVDEG VIGWSGNDSI IIIWKLKKIW EKYVIVETEN HQYDLIRSSW KRLDS //