ID   ATG11_YEAST             Reviewed;        1178 AA.
AC   Q12527;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Autophagy-related protein 11;
DE   AltName: Full=Cytoplasm to vacuole targeting protein 9;
GN   Name=ATG11; Synonyms=CVT9; OrderedLocusNames=YPR049C;
GN   ORFNames=YP9499.07c;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   FUNCTION.
RX   PubMed=8663607; DOI=10.1074/jbc.271.30.17621;
RA   Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J.;
RT   "Genetic and phenotypic overlap between autophagy and the cytoplasm to
RT   vacuole protein targeting pathway.";
RL   J. Biol. Chem. 271:17621-17624(1996).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH ATG1.
RX   PubMed=10995454; DOI=10.1083/jcb.150.6.1507;
RA   Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.;
RT   "Tor-mediated induction of autophagy via an Apg1 protein kinase
RT   complex.";
RL   J. Cell Biol. 150:1507-1513(2000).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21206022; PubMed=11309418; DOI=10.1083/jcb.153.2.381;
RA   Kim J., Kamada Y., Stromhaug P.E., Guan J., Hefner-Gravink A.,
RA   Baba M., Scott S.V., Ohsumi Y., Dunn W.A. Jr., Klionsky D.J.;
RT   "Cvt9/Gsa9 functions in sequestering selective cytosolic cargo
RT   destined for the vacuole.";
RL   J. Cell Biol. 153:381-396(2001).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH ATG19.
RX   MEDLINE=22368321; PubMed=12479808; DOI=10.1016/S1534-5807(02)00373-8;
RA   Shintani T., Huang W.-P., Stromhaug P.E., Klionsky D.J.;
RT   "Mechanism of cargo selection in the cytoplasm to vacuole targeting
RT   pathway.";
RL   Dev. Cell 3:825-837(2002).
RN   [6]
RP   NOMENCLATURE.
RX   MEDLINE=22912406; 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.,
RA   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   MEDLINE=22923954; 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   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613 AND SER-935, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and
CC       pexophagy. Recruites the ATG19-prAPE1 complex to the pre-
CC       autophagosome, the site of vesicle/autophagosome formation.
CC       Required for the Cvt vesicles completion.
CC   -!- SUBUNIT: Homodimer and potential homooligomers. Interacts with
CC       ATG1 kinase and the ATG19 cargo protein transporter.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-31977, EBI-31977;
CC       P53104:ATG1; NbExp=1; IntAct=EBI-31977, EBI-2657;
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Note=Punctate structures.
CC   -!- MISCELLANEOUS: Present with 86 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the ATG11 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z71255; CAA94996.1; -; Genomic_DNA.
DR   EMBL; Z49219; CAA89169.1; -; Genomic_DNA.
DR   PIR; S54073; S54073.
DR   RefSeq; NP_015374.1; -.
DR   DIP; DIP:1492N; -.
DR   IntAct; Q12527; 16.
DR   PRIDE; Q12527; -.
DR   Ensembl; YPR049C; Saccharomyces cerevisiae.
DR   GeneID; 856162; -.
DR   GenomeReviews; U00094_GR; YPR049C.
DR   KEGG; sce:YPR049C; -.
DR   NMPDR; fig|4932.3.peg.6510; -.
DR   CYGD; YPR049c; -.
DR   SGD; S000006253; ATG11.
DR   HOGENOM; Q12527; -.
DR   OMA; Q12527; YGLYLIE.
DR   NextBio; 981307; -.
DR   ArrayExpress; Q12527; -.
DR   GermOnline; YPR049C; Saccharomyces cerevisiae.
DR   GO; GO:0019898; C:extrinsic to membrane; IDA:SGD.
DR   GO; GO:0000407; C:pre-autophagosomal structure; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0032947; F:protein complex scaffold; IGI:SGD.
DR   GO; GO:0032258; P:CVT pathway; IGI:SGD.
DR   GO; GO:0030242; P:peroxisome degradation; IMP:SGD.
DR   GO; GO:0034727; P:piecemeal microautophagy of nucleus; IMP:SGD.
DR   GO; GO:0034497; P:protein localization to pre-autophagosomal ...; IMP:SGD.
DR   InterPro; IPR019460; Autophagy-rel_prot_11.
DR   Pfam; PF10377; ATG11; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Coiled coil; Complete proteome; Membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1   1178       Autophagy-related protein 11.
FT                                /FTId=PRO_0000124554.
FT   COILED      538    572       Potential.
FT   COILED      696    850       Potential.
FT   COMPBIAS    598    610       Asn-rich.
FT   COMPBIAS   1050   1099       Ser-rich.
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     935    935       Phosphoserine.
SQ   SEQUENCE   1178 AA;  135025 MW;  A904B92E9AE79449 CRC64;
     MADADEYSTA PTQQEITPLQ TTATIINAIS GECITTNVDF FVSLDKFKQF IARKWKIPPD
     QLLILLPYGN KLKPSMFKEL LINRSFTLND FYVYDRRLFS LVSKPTPTNL LTSKDSNPMN
     SPNSNDLTET LEYLIKNSHI SQYQGSDTIM IKPMPSPLED ADVDLSRLNY HSVTSLLTTN
     LGWLSALEID VHYFKSLIPD IIAHIKRIFD GLTVCSQYLK LYCFDVESLY NSNVQFLNQL
     VDNGMTSKWE KCFNDTLSKL TALEGDSLQK FINIESLLEN EKSVKILNHS INGKLNKIKR
     EIDENASFRD IITVNIDRLR QMFTPNESKF ELEDQMAESF EVLVSEMRTR SRNVLDKEEE
     EFNSQEFLKS MNVMLEKDKK ESVKTLFTIS QALYSQIGEL IDLKKSLQKH AVAILGNIAF
     TQMEILGIKR LLLNECNKDL ELYKKYEVEF AQVEDLPLIY GLYLIEKYRR LSWFQQILSF
     ISNFNQDLEL FKQNELRTRN KWVKNFGSIA TVFCEDLLSS SDFKRLNEYH SHTSPPNEDE
     EDENENSIAN YRQDLVKVSQ AIDNYMTQIK ETDVSEPIID LLSKTLFETK RFHIIYSNFK
     NNNNNSSNGN SISPEGSIAL KSDDVVKGYK TRIKKLESLL HEFQYSDIGH WPQGVLNTHL
     KPFRGSATSI NKKKFLGASV LLEPANISEV NIDSVSQANN HQIQELESNV DDLLHQLQLL
     KEENNRKSMQ ISEMGKKISD LEVEKTAYRE TLTNLNQELA RLTNEEQSHR TEIFTLNASF
     KKQLNDIISQ DNEKIEKLTG DYDDVSKSRE RLQMDLDESN KKHEQEVNLL KADIERLGKQ
     IVTSEKSYAE TNSSSMEKGE KFETIPLAED PGRENQISAY TQTLQDRIFD IISTNIFILE
     NIGLLLTFDN NNNIQIRRVK GLKKGTAQSN ILDESTQMLD AHDNSLIKSP VFQKLKDEYE
     LIKSVANGSE KDTQQSIFLG NITQLYDNKL YEVAVIRRFK DIETLAKKLT KENKIKRTLL
     ERFQREKVTL RNFQIGDLAL FLPTRENVNS VGSMSSSTSS LSSSFSSVDL STPPPLDAMS
     IQSSPSVIHS NVINQASISG RDKNKLMRPW AAFTAFEEST RYFLKDEKGL TKGKEWFVGR
     IVTLEHFVAD SPSNNPFRLP KGSVWFQVTA VVVSYQGV
//