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ATG27_YEAST
ID   ATG27_YEAST             Reviewed;         271 AA.
AC   P46989; D6VW11; Q86ZR9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Autophagy-related protein 27;
DE   AltName: Full=Enhancer of VPS34 missorting protein 1;
DE   Flags: Precursor;
GN   Name=ATG27; Synonyms=ETF1; OrderedLocusNames=YJL178C; ORFNames=J0490;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-103.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA   Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA   Gates K., Gaffney T.D., Philippsen P.;
RT   "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT   comparison to the genome of a related fungus: Ashbya gossypii.";
RL   Genome Biol. 4:R45.1-R45.13(2003).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 188-LYS--LYS-193.
RX   PubMed=12186856; DOI=10.1083/jcb.200112050;
RA   Wurmser A.E., Emr S.D.;
RT   "Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the
RT   Vps34 PtdIns 3-kinase in autophagy.";
RL   J. Cell Biol. 158:761-772(2002).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA   Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA   Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT   "A unified nomenclature for yeast autophagy-related genes.";
RL   Dev. Cell 5:539-545(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   SUBCELLULAR LOCATION, IDENTIFICATION IN THE ATG9-ATG23-ATG27 COMPLEX, AND
RP   FUNCTION.
RX   PubMed=17426440; DOI=10.4161/auto.4129;
RA   Legakis J.E., Yen W.L., Klionsky D.J.;
RT   "A cycling protein complex required for selective autophagy.";
RL   Autophagy 3:422-432(2007).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=17135291; DOI=10.1091/mbc.e06-07-0612;
RA   Yen W.-L., Legakis J.E., Nair U., Klionsky D.J.;
RT   "Atg27 is required for autophagy-dependent cycling of Atg9.";
RL   Mol. Biol. Cell 18:581-593(2007).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=23129774; DOI=10.1074/jbc.m112.411454;
RA   Kakuta S., Yamamoto H., Negishi L., Kondo-Kakuta C., Hayashi N., Ohsumi Y.;
RT   "Atg9 vesicles recruit vesicle-tethering proteins Trs85 and Ypt1 to the
RT   autophagosome formation site.";
RL   J. Biol. Chem. 287:44261-44269(2012).
RN   [12]
RP   FUNCTION.
RX   PubMed=22826123; DOI=10.1083/jcb.201202061;
RA   Yamamoto H., Kakuta S., Watanabe T.M., Kitamura A., Sekito T.,
RA   Kondo-Kakuta C., Ichikawa R., Kinjo M., Ohsumi Y.;
RT   "Atg9 vesicles are an important membrane source during early steps of
RT   autophagosome formation.";
RL   J. Cell Biol. 198:219-233(2012).
CC   -!- FUNCTION: Effector of VPS34 phosphatidylinositol 3-phosphate kinase
CC       signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle
CC       formation. Plays a role in ATG protein retrieval from the pre-
CC       autophagosomal structure (PAS) and is especially required for
CC       autophagy-dependent cycling of ATG9. {ECO:0000269|PubMed:12186856,
CC       ECO:0000269|PubMed:17135291, ECO:0000269|PubMed:17426440,
CC       ECO:0000269|PubMed:22826123}.
CC   -!- SUBUNIT: Forms a complex with ATG9 and ATG23.
CC       {ECO:0000269|PubMed:17426440}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I
CC       membrane protein. Golgi apparatus membrane; Single-pass type I membrane
CC       protein. Mitochondrion membrane; Single-pass membrane protein.
CC       Preautophagosomal structure membrane; Single-pass type I membrane
CC       protein. Note=Cycles among the pre-autophagosomal structure (PAS),
CC       mitochondria and Golgi.
CC   -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATG27 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS56577.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA89473.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z49453; CAA89473.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY558251; AAS56577.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY260894; AAP21762.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08627.1; -; Genomic_DNA.
DR   PIR; S56961; S56961.
DR   RefSeq; NP_012357.2; NM_001181611.1.
DR   AlphaFoldDB; P46989; -.
DR   BioGRID; 33583; 166.
DR   DIP; DIP-1606N; -.
DR   IntAct; P46989; 21.
DR   MINT; P46989; -.
DR   STRING; 4932.YJL178C; -.
DR   TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR   MaxQB; P46989; -.
DR   PaxDb; P46989; -.
DR   PRIDE; P46989; -.
DR   TopDownProteomics; P46989; -.
DR   EnsemblFungi; YJL178C_mRNA; YJL178C; YJL178C.
DR   GeneID; 853261; -.
DR   KEGG; sce:YJL178C; -.
DR   SGD; S000003714; ATG27.
DR   VEuPathDB; FungiDB:YJL178C; -.
DR   eggNOG; ENOG502QVJJ; Eukaryota.
DR   HOGENOM; CLU_089705_0_0_1; -.
DR   InParanoid; P46989; -.
DR   OMA; NKGNAID; -.
DR   BioCyc; YEAST:G3O-31613-MON; -.
DR   PRO; PR:P46989; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P46989; protein.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:SGD.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR   GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR   GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IDA:SGD.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   GO; GO:0016050; P:vesicle organization; IMP:SGD.
DR   Gene3D; 2.70.130.10; -; 1.
DR   InterPro; IPR018939; Autophagy-rel_prot_27.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR   InterPro; IPR044865; MRH_dom.
DR   Pfam; PF09451; ATG27; 1.
DR   PROSITE; PS51914; MRH; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasmic vesicle; Disulfide bond; Golgi apparatus; Membrane;
KW   Mitochondrion; Protein transport; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..271
FT                   /note="Autophagy-related protein 27"
FT                   /id="PRO_0000001780"
FT   TOPO_DOM        20..199
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:17135291"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:17135291"
FT   DOMAIN          20..166
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          161..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        22..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        71..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        135..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   MUTAGEN         188..193
FT                   /note="KKPAKK->AAPAAA: Abolishes the binding of
FT                   phosphatidylinositol 3-phosphate and the cytoplasm to
FT                   vacuole transport."
FT                   /evidence="ECO:0000269|PubMed:12186856"
SQ   SEQUENCE   271 AA;  30201 MW;  BD2F3BF4C5904ED2 CRC64;
     MVSKTWICGF ISIITVVQAL SCEKHDVLKK YQVGKFSSLT STERDTPPST TIEKWWINVC
     EEHNVEPPEE CKKNDMLCGL TDVILPGKDA ITTQIIDFDK NIGFNVEETE SALTLTLKGA
     TWGANSFDAK LEFQCNDNMK QDELTSHTWA DKSIQLTLKG PSGCLKSKDD DKKNGDGDNG
     KDGDSEGKKP AKKAGGTSWF TWLFLYALLF TLIYLMVVSF LNTRGGSFQD FRAEFIQRST
     QFLTSLPEFC KEVVSRILGR STAQRGGYSA V
 
 
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