ID   HSV2_CANGA              Reviewed;         445 AA.
AC   Q6FXC1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=SVP1-like protein 2;
GN   Name=HSV2; OrderedLocusNames=CAGL0B02101g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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DR   EMBL; CR380948; CAG57961.1; -; Genomic_DNA.
DR   RefSeq; XP_445061.1; XM_445061.1.
DR   AlphaFoldDB; Q6FXC1; -.
DR   SMR; Q6FXC1; -.
DR   STRING; 5478.XP_445061.1; -.
DR   EnsemblFungi; CAG57961; CAG57961; CAGL0B02101g.
DR   GeneID; 2886497; -.
DR   KEGG; cgr:CAGL0B02101g; -.
DR   CGD; CAL0127752; CAGL0B02101g.
DR   VEuPathDB; FungiDB:CAGL0B02101g; -.
DR   eggNOG; KOG2111; Eukaryota.
DR   HOGENOM; CLU_025895_0_1_1; -.
DR   InParanoid; Q6FXC1; -.
DR   OMA; WSFCKFQ; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..445
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051026"
FT   REPEAT          218..258
FT                   /note="WD 1"
FT   REPEAT          263..302
FT                   /note="WD 2"
FT   REGION          301..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  50429 MW;  F11710D94A8256C6 CRC64;
     MDVREAIQQE AGAETGFASV TFNQDESCFS CANEQGFLVY NTFPLSLKLT KEFKQTPERG
     AGIGYSQMLY RTNYIALVGG GQRPRYSLNR VVIWDDLQQK ESFSLKFMSI VRKVVLSRVH
     LVVALENELF IYSFHSTPKL LCPPIKTAPF GPFDFKVVTI EGKATDQAKV TSLLAYPSAK
     LTGQLHVADL SKLRSNQNNN QDMALTSESF LPTTIIKAHK APIRNVRINN QGTMVATASR
     KGTLIRIFST HNGILLKEFR RGLDRAEIYD MCFSPLGTRL AVVSDKQTLH VFQIAPMAEG
     TLNPANPEDH QSSGSNGHIK ANTNQVHSLR NIVPTSWKPK YLDSVWSMCK VHLRNPKLRN
     NVNDLAFNED RCTIAWCRQN RSHTFKNGNH FNENEENKLV LVWKNSRIWE KYVILEKEAP
     NSNDGIKGPS PLTEWELVRE SWREL