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UniProtKB/Swiss-Prot entry Q12142


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ATG9_YEAST
Primary accession number Q12142
Secondary accession numbers None
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 61)
Name and origin of the protein
Protein name Autophagy-related protein 9
Synonym Cytoplasm to vacuole targeting protein 7
Gene name
Name: ATG9
Synonyms: APG9, AUT9, CVT7
OrderedLocusNames: YDL149W
ORFNames: D1560
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(199612)12:15<1587::AID-YEA46>3.0.CO;2-6; PubMed=8972581 [NCBI, ExPASy, EBI, Israel, Japan]
Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
"Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
Yeast 12:1587-1592(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
FUNCTION.
DOI=10.1016/0014-5793(93)80398-E; PubMed=8224160 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukada M., Ohsumi Y.;
"Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae.";
FEBS Lett. 333:169-174(1993).
[4]
FUNCTION.
DOI=10.1083/jcb.131.3.591; PubMed=7593182 [NCBI, ExPASy, EBI, Israel, Japan]
Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.;
"Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway.";
J. Cell Biol. 131:591-602(1995).
[5]
FUNCTION.
DOI=10.1074/jbc.271.30.17621; PubMed=8663607 [NCBI, ExPASy, EBI, Israel, Japan]
Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J.;
"Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway.";
J. Biol. Chem. 271:17621-17624(1996).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1128/JB.182.8.2125-2133.2000; PubMed=10735854 [NCBI, ExPASy, EBI, Israel, Japan]
Lang T., Reiche S., Straub M., Bredschneider M., Thumm M.;
"Autophagy and the cvt pathway both depend on AUT9.";
J. Bacteriol. 182:2125-2133(2000).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1083/jcb.148.3.465; PubMed=10662773 [NCBI, ExPASy, EBI, Israel, Japan]
Noda T., Kim J., Huang W.-P., Baba M., Tokunaga C., Ohsumi Y., Klionsky D.J.;
"Apg9p/Cvt7p is an integral membrane protein required for transport vesicle formation in the Cvt and autophagy pathways.";
J. Cell Biol. 148:465-480(2000).
[8]
FUNCTION.
DOI=10.1093/emboj/20.21.5971; PubMed=11689437 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
"The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation.";
EMBO J. 20:5971-5981(2001).
[9]
INTERACTION WITH ATG2.
DOI=10.1074/jbc.M102342200; PubMed=11382760 [NCBI, ExPASy, EBI, Israel, Japan]
Wang C.-W., Kim J., Huang W.-P., Abeliovich H., Stromhaug P.E., Dunn W.A. Jr., Klionsky D.J.;
"Apg2 is a novel protein required for the cytoplasm to vacuole targeting, autophagy, and pexophagy pathways.";
J. Biol. Chem. 276:30442-30451(2001).
[10]
NOMENCLATURE.
DOI=10.1016/S1534-5807(03)00296-X; PubMed=14536056 [NCBI, ExPASy, EBI, Israel, Japan]
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
"A unified nomenclature for yeast autophagy-related genes.";
Dev. Cell 5:539-545(2003).
[11]
FUNCTION, AND INTERACTION WITH ATG23.
DOI=10.1074/jbc.M309238200; PubMed=14504273 [NCBI, ExPASy, EBI, Israel, Japan]
Tucker K.A., Reggiori F., Dunn W.A. Jr., Klionsky D.J.;
"Atg23 is essential for the cytoplasm to vacuole targeting pathway and efficient autophagy but not pexophagy.";
J. Biol. Chem. 278:48445-48452(2003).
[12]
SUBCELLULAR LOCATION, INTERACTION WITH ATG18, AND TRAFFICKING.
DOI=10.1016/S1534-5807(03)00402-7; PubMed=14723849 [NCBI, ExPASy, EBI, Israel, Japan]
Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.;
"The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure.";
Dev. Cell 6:79-90(2004).
[13]
TOPOLOGY [LARGE SCALE ANALYSIS].
DOI=10.1073/pnas.0604075103; PubMed=16847258 [NCBI, ExPASy, EBI, Israel, Japan]
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; SER-112 AND SER-787, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Recruites ATG23 and ATG8 to the pre-autophagosomal structure.
  • SUBUNIT: Interacts with ATG18, ATG2 and ATG23.
  • SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane protein. Preautophagosomal structure membrane; Multi-pass membrane protein. Note=The proper trafficking of ATG9 between the pre-autophagosomal structure and the other cytoplasmic vesicles requires ATG2, ATG18, ATG23, the ATG1-ATG13 complex and the phosphatidylinositol 3-kinase complex I.
  • SIMILARITY: Belongs to the ATG9 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X97751; CAA66342.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74197; CAA98723.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S67697; S67697.
RefSeq NP_010132.1; -.
3D structure databases
ModBase Q12142.
Protein-protein interaction databases
DIP DIP:1938N; -.
IntAct Q12142; 90.
Organism-specific databases
CYGD YDL149w; -.
SGD S000002308; ATG9.
Yeast-GFP YDL149W.
Gene expression databases
ArrayExpress Q12142; -.
GermOnline YDL149W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030659; Cellular component: cytoplasmic vesicle membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005624; Cellular component: membrane fraction (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0034045; Cellular component: pre-autophagosomal structure membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000045; Biological process: autophagic vacuole formation (inferred from mutant phenotype from SGD).
GO:0032258; Biological process: CVT pathway (inferred from mutant phenotype from SGD).
GO:0034727; Biological process: piecemeal microautophagy of nucleus (inferred from mutant phenotype from SGD).
GO:0051260; Biological process: protein homooligomerization (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR007241; Autophagy-rel_prot_9.
Graphical view of domain structure.
PANTHER PTHR13038; APG9; 1.
Pfam PF04109; APG9; 1.
Pfam graphical view of domain structure.
Genome annotation databases
Ensembl YDL149W; Saccharomyces cerevisiae. [Contig view]
GeneID 851406; -.
GenomeReviews Z71256_GR; YDL149W.
KEGG sce:YDL149W; -.
NMPDR fig|4932.3.peg.869; -.
Phylogenomic databases
HOGENOM Q12142; -.
OMA Q12142; EYTHYLP.
Other
NextBio 968579; -.
ProtoNet Q12142.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autophagy; Complete proteome; Cytoplasmic vesicle; Membrane; Phosphoprotein; Protein transport; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   997  997     Autophagy-related protein 9. PRO_0000119839
TOPO_DOM   1   318  318     Cytoplasmic (Probable). 
TRANSMEM   319   339  21     Potential. 
TOPO_DOM   340   376  37     Lumenal (Probable). 
TRANSMEM   377   397  21     Potential. 
TOPO_DOM   398   538  141     Cytoplasmic (Probable). 
TRANSMEM   539   559  21     Potential. 
TOPO_DOM   560   620  61     Lumenal (Probable). 
TRANSMEM   621   641  21     Potential. 
TOPO_DOM   642   656  15     Cytoplasmic (Probable). 
TRANSMEM   657   677  21     Potential. 
TOPO_DOM   678   723  46     Lumenal (Probable). 
TRANSMEM   724   744  21     Potential. 
TOPO_DOM   745   997  253     Cytoplasmic (Probable). 
COMPBIAS   907   978  72     Asn-rich. 
MOD_RES   111   111        Phosphothreonine. 
MOD_RES   112   112        Phosphoserine. 
MOD_RES   787   787        Phosphoserine. 
Sequence information
Length: 997 AA [This is the length of the unprocessed precursor] Molecular weight: 115403 Da [This is the MW of the unprocessed precursor] CRC64: E900AD5E3AC5D111 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MERDEYQLPN SHGKNTFLSR IFGLQSDEVN PSLNSQEMSN FPLPDIERGS SLLHSTNDSR 

        70         80         90        100        110        120 
EDVDENDLRV PESDQGTSTE EEDEVDEEQV QAYAPQISDG LDGDHQLNSV TSKENVLETE 

       130        140        150        160        170        180 
KSNLERLVEG STDDSVPKVG QLSSEEEEDN EFINNDGFDD DTPLFQKSKI HEFSSKKSNT 

       190        200        210        220        230        240 
IEDGKRPLFF RHILQNNRPQ RDTQKLFTSS NAIHHDKDKS ANNGPRNING NQKHGTKYFG 

       250        260        270        280        290        300 
SATQPRFTGS PLNNTNRFTK LFPLRKPNLL SNISVLNNTP EDRINTLSVK ERALWKWANV 

       310        320        330        340        350        360 
ENLDIFLQDV YNYYLGNGFY CIILEKILNI CTLLFVVFVS TYMGHCVDYS KLPTSHRVSD 

       370        380        390        400        410        420 
IIIDKCYSNS ITGFTKFFLW MFYFFVILKI VQLYFDVQKL SELQNFYKYL LNISDDELQT 

       430        440        450        460        470        480 
LPWQNVIQQL MYLKDQNAMT ANVVEVKAKN RIDAHDVANR IMRRENYLIA LYNSDILNLS 

       490        500        510        520        530        540 
LPIPLFRTNV LTKTLEWNIN LCVMGFVFNE SGFIKQSILK PSQREFTREE LQKRFMLAGF 

       550        560        570        580        590        600 
LNIILAPFLV TYFVLLYFFR YFNEYKTSPG SIGARQYTPI AEWKFREYNE LYHIFKKRIS 

       610        620        630        640        650        660 
LSTTLANKYV DQFPKEKTNL FLKFVSFICG SFVAILAFLT VFDPENFLNF EITSDRSVIF 

       670        680        690        700        710        720 
YITILGAIWS VSRNTITQEY HVFDPEETLK ELYEYTHYLP KEWEGRYHKE EIKLEFCKLY 

       730        740        750        760        770        780 
NLRIVILLRE LTSLMITPFV LWFSLPSSAG RIVDFFRENS EYVDGLGYVC KYAMFNMKNI 

       790        800        810        820        830        840 
DGEDTHSMDE DSLTKKIAVN GSHTLNSKRR SKFTAEDHSD KDLANNKMLQ SYVYFMDDYS 

       850        860        870        880        890        900 
NSENLTGKYQ LPAKKGYPNN EGDSFLNNKY SWRKQFQPGQ KPELFRIGKH ALGPGHNISP 

       910        920        930        940        950        960 
AIYSTRNPGK NWDNNNNGDD IKNGTNNATA KNDDNNGNND HEYVLTESFL DSGAFPNHDV 

       970        980        990 
IDHNKMLNSN YNGNGILNKG GVLGLVKEYY KKSDVGR 

Q12142 in FASTA format

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