HSV2_CANAL
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 03-AUG-2022, entry version 94.
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}.
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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 PRIDE; Q59P11; -.
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; 966922at2759; -.
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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
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; 3.
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..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
