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ATG23_YEAST
ID   ATG23_YEAST             Reviewed;         453 AA.
AC   Q06671; D6VZ66;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Autophagy-related protein 23;
DE   AltName: Full=Cytoplasm to vacuole targeting protein 23;
GN   Name=ATG23; Synonyms=CVT23; OrderedLocusNames=YLR431C;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG9.
RX   PubMed=14504273; DOI=10.1074/jbc.m309238200;
RA   Tucker K.A., Reggiori F., Dunn W.A. Jr., Klionsky D.J.;
RT   "Atg23 is essential for the cytoplasm to vacuole targeting pathway and
RT   efficient autophagy but not pexophagy.";
RL   J. Biol. Chem. 278:48445-48452(2003).
RN   [5]
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   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14723849; DOI=10.1016/s1534-5807(03)00402-7;
RA   Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.;
RT   "The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from
RT   the pre-autophagosomal structure.";
RL   Dev. Cell 6:79-90(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=14734026; DOI=10.1016/s1567-1356(03)00207-1;
RA   Meiling-Wesse K., Bratsika F., Thumm M.;
RT   "ATG23, a novel gene required for maturation of proaminopeptidase I, but
RT   not for autophagy.";
RL   FEMS Yeast Res. 4:459-465(2004).
RN   [8]
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   [9]
RP   FUNCTION.
RX   PubMed=17700056; DOI=10.4161/auto.4784;
RA   Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.;
RT   "Overexpression of autophagy-related genes inhibits yeast filamentous
RT   growth.";
RL   Autophagy 3:604-609(2007).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18497569; DOI=10.4161/auto.6308;
RA   Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.;
RT   "Localization of autophagy-related proteins in yeast using a versatile
RT   plasmid-based resource of fluorescent protein fusions.";
RL   Autophagy 4:792-800(2008).
CC   -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicle
CC       formation and efficient autophagy. Plays a role in ATG protein
CC       retrieval from the pre-autophagosomal structure (PAS) and is especially
CC       required for autophagy-dependent cycling of ATG9. Also plays a role in
CC       regulation of filamentous growth. {ECO:0000269|PubMed:14504273,
CC       ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:14734026,
CC       ECO:0000269|PubMed:17426440, ECO:0000269|PubMed:17700056}.
CC   -!- SUBUNIT: Forms a complex with ATG9 and ATG27.
CC       {ECO:0000269|PubMed:17426440}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane;
CC       Peripheral membrane protein. Membrane; Peripheral membrane protein.
CC       Note=Found in pre-autophagosomal structure and other punctate
CC       structures. Correct localization of ATG23 to the membranes is strictly
CC       dependent of ATG9. Cycling through the pre-autophagosomal structure and
CC       correct location to other punctate structures is ATG1- and ATG13-
CC       dependent.
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATG23 family. {ECO:0000305}.
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DR   EMBL; U21094; AAB67517.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09732.1; -; Genomic_DNA.
DR   PIR; S59401; S59401.
DR   RefSeq; NP_013535.1; NM_001182319.1.
DR   AlphaFoldDB; Q06671; -.
DR   SASBDB; Q06671; -.
DR   SMR; Q06671; -.
DR   BioGRID; 31690; 130.
DR   IntAct; Q06671; 1.
DR   STRING; 4932.YLR431C; -.
DR   TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR   iPTMnet; Q06671; -.
DR   MaxQB; Q06671; -.
DR   PaxDb; Q06671; -.
DR   PRIDE; Q06671; -.
DR   EnsemblFungi; YLR431C_mRNA; YLR431C; YLR431C.
DR   GeneID; 851151; -.
DR   KEGG; sce:YLR431C; -.
DR   SGD; S000004423; ATG23.
DR   VEuPathDB; FungiDB:YLR431C; -.
DR   eggNOG; ENOG502RZQ0; Eukaryota.
DR   HOGENOM; CLU_051067_0_0_1; -.
DR   InParanoid; Q06671; -.
DR   OMA; EMSEMIN; -.
DR   BioCyc; YEAST:G3O-32490-MON; -.
DR   PRO; PR:Q06671; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06671; protein.
DR   GO; GO:0019898; C:extrinsic component of membrane; 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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR   GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD.
PE   1: Evidence at protein level;
KW   Autophagy; Coiled coil; Cytoplasm; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..453
FT                   /note="Autophagy-related protein 23"
FT                   /id="PRO_0000064727"
FT   REGION          381..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          144..213
FT                   /evidence="ECO:0000255"
FT   COILED          272..302
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        406..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  51540 MW;  D6F497DE0677FA20 CRC64;
     MELNQVLEKK EQILQYLGTL VGLHEKALSD VNSASQVTSI RKDITICLND LCRINDLLVS
     HDGLLKREIG SLLRDKQELL ELNEREQLLW KERKSWHIKQ ETDAAPADYV IDKDAIITIS
     SHHRTSLNKY IESVGAENTI LSNTDDSDAM IEEVQNAESS ADQMIRNYKL LQLSHKQAKS
     EIIRLETLLR DFKKDNKFIE EELKRQSGRI RSEMGNIDFH LSKIEESKHQ LMKRIGFESP
     LTQEKSLSEK IFNLRLSSAD EDYNERQTIN MKNFVHMKDL IELKIEDLQE QLMRNKNESS
     TVLTQRELWL DCQKKVGDLE SKLITKLRSS SNSKIPPNEM SEMINSTIQY LNNLLDSSDE
     KLTTTLISNE RDVLSKACEE LHSESTTAQD GSSALPSKPI DIHKSHKGSN ASSNLKQPST
     PSFLVASKSP PKIGISESVV NANKNDAISK KVE
 
 
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