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Database: UniProt
Entry: HSV2_SCHPO
LinkDB: HSV2_SCHPO
Original site: HSV2_SCHPO 
ID   HSV2_SCHPO              Reviewed;         364 AA.
AC   Q9P3W2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=SVP1-like protein 2;
GN   Name=hsv2; Synonyms=atg18c; ORFNames=SPAC458.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA   Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA   Du L.L.;
RT   "Global analysis of fission yeast mating genes reveals new autophagy
RT   factors.";
RL   PLoS Genet. 9:E1003715-E1003715(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       Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735};
CC       Peripheral membrane protein {ECO:0000269|PubMed:23950735}.
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   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB93848.1; -; Genomic_DNA.
DR   RefSeq; NP_594700.1; NM_001020128.2.
DR   AlphaFoldDB; Q9P3W2; -.
DR   SMR; Q9P3W2; -.
DR   BioGRID; 279761; 10.
DR   STRING; 284812.Q9P3W2; -.
DR   MaxQB; Q9P3W2; -.
DR   PaxDb; 4896-SPAC458-06-1; -.
DR   EnsemblFungi; SPAC458.06.1; SPAC458.06.1:pep; SPAC458.06.
DR   GeneID; 2543338; -.
DR   KEGG; spo:SPAC458.06; -.
DR   PomBase; SPAC458.06; -.
DR   VEuPathDB; FungiDB:SPAC458.06; -.
DR   eggNOG; KOG2111; Eukaryota.
DR   HOGENOM; CLU_025895_2_1_1; -.
DR   InParanoid; Q9P3W2; -.
DR   OMA; QWALATF; -.
DR   PhylomeDB; Q9P3W2; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   PRO; PR:Q9P3W2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
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:0000324; C:fungal-type vacuole; ISO:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
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:0016236; P:macroautophagy; IMP:PomBase.
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; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..364
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051032"
FT   REPEAT          173..213
FT                   /note="WD 1"
FT   REPEAT          218..257
FT                   /note="WD 2"
SQ   SEQUENCE   364 AA;  41011 MW;  F99A708532A8480E CRC64;
     MSTINTVSLN QDASCMSVAL DTGYKIFQIN PLKLRAQRQF NDGGLSIVKM LFRSNVLLLV
     GGGGNPKYAP NKLIVWDDVK ERPVKELELN FEIKGICFDG KLLAIATASK LFLYQFGNNL
     KLQRCLDTQN PKGLCAMVTT VEKTAIVFPS RKVGQLQILF LFKDHMNTSI VPAHDSEISC
     LGISKTGSKI ASSSTNGTLI RIWNSETGEK ICEFRRGYQH TAVCQLAFSP DELLLACASK
     KETLHIFSLH GSPNTIRQLT SEEPYEEASE FKSSTTEPRQ THWKRKLLKL IDSGKRAHWR
     IQLYQSNPVL LHWLDEMTIL ICYKDAAYQK LKLTIEESSK SVEHANQHVC FHYDYTLEAD
     GSLC
//
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