ID   HSV2_ASHGO              Reviewed;         401 AA.
AC   Q75AQ4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=SVP1-like protein 2;
GN   Name=HSV2; OrderedLocusNames=ADL134W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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}.
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DR   EMBL; AE016817; AAS51786.1; -; Genomic_DNA.
DR   RefSeq; NP_983962.1; NM_209315.1.
DR   AlphaFoldDB; Q75AQ4; -.
DR   SMR; Q75AQ4; -.
DR   STRING; 33169.AAS51786; -.
DR   EnsemblFungi; AAS51786; AAS51786; AGOS_ADL134W.
DR   GeneID; 4620104; -.
DR   KEGG; ago:AGOS_ADL134W; -.
DR   eggNOG; KOG2111; Eukaryota.
DR   HOGENOM; CLU_025895_0_1_1; -.
DR   InParanoid; Q75AQ4; -.
DR   OMA; WSFCKFQ; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
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:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006497; P:protein lipidation; 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; -; 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..401
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051024"
FT   REPEAT          222..262
FT                   /note="WD 1"
FT   REPEAT          267..306
FT                   /note="WD 2"
SQ   SEQUENCE   401 AA;  45318 MW;  4E5C9031C031F1E3 CRC64;
     MKTRNPIVVQ RKNGPPRFLH VNFNQDQECF SCATEKGFEI YNTDPIQCSV KRRFSHNGMS
     GIGYTRMLYR TNYIGLVGGG ASPRFSTNKI AIWDDIQQRD SVSIRFNSPV HELFLSRQYI
     VVVLAQSIDV YTFSGSPSRV CPVISNIHNG IADFVTCSKM RRASGPQDVE HALSQKHVIA
     GILAYPSGIR PGQIHIADLS NIQTPSVADA SATHLPTSII KAHKNPIHLV KLSPQGTMVA
     TCSVEGTLIR VFSIASGSLI HEFRRGLDRA LIYDMQWNGK GDKLAVVSDK FTLHIFQINE
     DLDKRHLLKG WFPKVKYLQG VWSMCSTKLD RSLLTHDEDT CKVGWIGDEA LSLLWQKSGM
     WEKYVIMEKL REYKVDETLH SGAPDGRRQL YDLVRESWRQ L