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HSV2_YEAST
ID   HSV2_YEAST              Reviewed;         448 AA.
AC   P50079; D6VV05;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=SVP1-like protein 2;
GN   Name=HSV2; OrderedLocusNames=YGR223C; ORFNames=G8530;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8701610;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA   van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT   "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT   region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 12:385-390(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=11536337; DOI=10.1002/yea.764;
RA   Georgakopoulos T., Koutroubas G., Vakonakis I., Tzermia M., Prokova V.,
RA   Voutsina A., Alexandraki D.;
RT   "Functional analysis of the Saccharomyces cerevisiae
RT   YFR021w/YGR223c/YPL100w ORF family suggests relations to
RT   mitochondrial/peroxisomal functions and amino acid signalling pathways.";
RL   Yeast 18:1155-1171(2001).
RN   [5]
RP   INTERACTION WITH PIP2, AND SUBCELLULAR LOCATION.
RX   PubMed=15103325; DOI=10.1038/sj.emboj.7600203;
RA   Dove S.K., Piper R.C., McEwen R.K., Yu J.W., King M.C., Hughes D.C.,
RA   Thuring J., Holmes A.B., Cooke F.T., Michell R.H., Parker P.J.,
RA   Lemmon M.A.;
RT   "Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate
RT   effectors.";
RL   EMBO J. 23:1922-1933(2004).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18769150; DOI=10.4161/auto.6801;
RA   Krick R., Henke S., Tolstrup J., Thumm M.;
RT   "Dissecting the localization and function of Atg18, Atg21 and Ygr223c.";
RL   Autophagy 4:896-910(2008).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX   PubMed=19756047; DOI=10.1038/msb.2009.64;
RA   Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT   "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT   new roles for protein glycosylation in eukaryotes.";
RL   Mol. Syst. Biol. 5:308-308(2009).
CC   -!- FUNCTION: Involved in piecemeal microautophagy of the nucleus
CC       (micronucleophagy). {ECO:0000269|PubMed:11536337,
CC       ECO:0000269|PubMed:18769150}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein.
CC       Prevacuolar compartment membrane; Peripheral membrane protein.
CC       Note=Recruitment to endosomes depends on binding to
CC       phosphatidylinositol 3-phosphate.
CC   -!- DOMAIN: Contains a beta-propeller domain involved in specific binding
CC       of phosphatidylinositol 3,5-bisphosphate.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; X87941; CAA61171.1; -; Genomic_DNA.
DR   EMBL; Z73008; CAA97251.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08316.1; -; Genomic_DNA.
DR   PIR; S57686; S57686.
DR   RefSeq; NP_011739.1; NM_001181352.1.
DR   AlphaFoldDB; P50079; -.
DR   SMR; P50079; -.
DR   BioGRID; 33476; 108.
DR   DIP; DIP-5556N; -.
DR   IntAct; P50079; 7.
DR   MINT; P50079; -.
DR   STRING; 4932.YGR223C; -.
DR   iPTMnet; P50079; -.
DR   MaxQB; P50079; -.
DR   PaxDb; P50079; -.
DR   PRIDE; P50079; -.
DR   EnsemblFungi; YGR223C_mRNA; YGR223C; YGR223C.
DR   GeneID; 853138; -.
DR   KEGG; sce:YGR223C; -.
DR   SGD; S000003455; HSV2.
DR   VEuPathDB; FungiDB:YGR223C; -.
DR   eggNOG; KOG2111; Eukaryota.
DR   GeneTree; ENSGT00940000157510; -.
DR   HOGENOM; CLU_025895_0_1_1; -.
DR   InParanoid; P50079; -.
DR   OMA; WSFCKFQ; -.
DR   BioCyc; YEAST:G3O-30904-MON; -.
DR   Reactome; R-SCE-1632852; Macroautophagy.
DR   PRO; PR:P50079; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P50079; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
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; IMP:SGD.
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   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   1: Evidence at protein level;
KW   Endosome; Glycoprotein; Membrane; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..448
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051034"
FT   REPEAT          222..262
FT                   /note="WD 1"
FT   REPEAT          267..306
FT                   /note="WD 2"
FT   REGION          416..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  51235 MW;  A4287FAB80AA68DF CRC64;
     MDVRRPIREA VNNRRKPKFL SVSFNQDDSC FSVALENGFR IFNTDPLTSK LSKTFKESAT
     NQSRGTGIGY TRMLYRTNYI ALVGGGKRPR HALNKLIIWD DLLQKETITL KFMSSIKDVF
     LSRIHIVVVL ENTIEIFQFQ TNPQRICPIL DIPPNGSVDY VVCSSKHLQS QASQSQSKIL
     EIIAFPSNKC VGQIQVADLS QIKYNSQNPK ESALLPTSII KAHKNPIKLV RLNRQGTMVA
     TCSVQGTLIR IFSTHNGTLI KEFRRGVDKA DIYEMSFSPN GSKLAVLSNK QTLHIFQIFE
     TTNTETNTPD HSRANGSSHP LKNYIPKGLW RPKYLDSVWS ICNAHLKNPI FDAHRNDNSG
     DVTHDNEFYK DRCRIGWCQD SNNREQDDSL VLVWQNSGIW EKFVILEKEQ QDSSKTHYSL
     NESLRNEDTK SAGEPTRWEL VRESWREL
 
 
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