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 25-MAY-2022, entry version 128.
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; 4896.SPAC458.06.1; -.
DR MaxQB; Q9P3W2; -.
DR PaxDb; Q9P3W2; -.
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; MGTTNYL; -.
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:0032991; C:protein-containing complex; NAS:PomBase.
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:0006914; P:autophagy; IMP:PomBase.
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:0016236; P:macroautophagy; IMP:PomBase.
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 Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 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
