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ATG17_YEAST
ID   ATG17_YEAST             Reviewed;         417 AA.
AC   Q06410; D6VZ59;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Autophagy-related protein 17;
GN   Name=ATG17; Synonyms=APG17; OrderedLocusNames=YLR423C;
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   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 complex.";
RL   J. Cell Biol. 150:1507-1513(2000).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11489916; DOI=10.1083/jcb.200104057;
RA   Drees B.L., Sundin B.A., Brazeau E., Caviston J.P., Chen G.-C., Guo W.,
RA   Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R.,
RA   McKenzie A. III, Brennwald P.J., Longtine M., Bi E., Chan C., Novick P.,
RA   Boone C., Pringle J.R., Davis T.N., Fields S., Drubin D.G.;
RT   "A protein interaction map for cell polarity development.";
RL   J. Cell Biol. 154:549-571(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=11486014; DOI=10.1128/mcb.21.17.5742-5752.2001;
RA   Wang Z., Wilson W.A., Fujino M.A., Roach P.J.;
RT   "Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the
RT   yeast homolog of AMP-activated protein kinase, and the cyclin-dependent
RT   kinase Pho85p.";
RL   Mol. Cell. Biol. 21:5742-5752(2001).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG20 AND SNX4.
RX   PubMed=12048214; DOI=10.1074/jbc.m204736200;
RA   Nice D.C. III, Sato T.K., Stromhaug P.E., Emr S.D., Klionsky D.J.;
RT   "Cooperative binding of the cytoplasm to vacuole targeting pathway
RT   proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-
RT   autophagosomal structure is required for selective autophagy.";
RL   J. Biol. Chem. 277:30198-30207(2002).
RN   [7]
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   [8]
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   [9]
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   [10]
RP   INTERACTION WITH ATG11.
RX   PubMed=15659643; DOI=10.1091/mbc.e04-11-1035;
RA   Yorimitsu T., Klionsky D.J.;
RT   "Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to
RT   vacuole targeting pathway.";
RL   Mol. Biol. Cell 16:1593-1605(2005).
RN   [11]
RP   FUNCTION, INTERACTION WITH ATG1 AND ATG13, AND MUTAGENESIS OF CYS-24.
RX   PubMed=15743910; DOI=10.1091/mbc.e04-08-0669;
RA   Kabeya Y., Kamada Y., Baba M., Takikawa H., Sasaki M., Ohsumi Y.;
RT   "Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy.";
RL   Mol. Biol. Cell 16:2544-2553(2005).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG1 AND ATG13.
RX   PubMed=15901835; DOI=10.1091/mbc.e04-10-0894;
RA   Cheong H., Yorimitsu T., Reggiori F., Legakis J.E., Wang C.W.,
RA   Klionsky D.J.;
RT   "Atg17 regulates the magnitude of the autophagic response.";
RL   Mol. Biol. Cell 16:3438-3453(2005).
RN   [13]
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   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CIS1.
RX   PubMed=17362880; DOI=10.1016/j.bbrc.2007.02.150;
RA   Kabeya Y., Kawamata T., Suzuki K., Ohsumi Y.;
RT   "Cis1/Atg31 is required for autophagosome formation in Saccharomyces
RT   cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 356:405-410(2007).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18625846; DOI=10.1083/jcb.200711112;
RA   Geng J., Baba M., Nair U., Klionsky D.J.;
RT   "Quantitative analysis of autophagy-related protein stoichiometry by
RT   fluorescence microscopy.";
RL   J. Cell Biol. 182:129-140(2008).
RN   [16]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18077553; DOI=10.1091/mbc.e07-08-0826;
RA   Cheong H., Nair U., Geng J., Klionsky D.J.;
RT   "The Atg1 kinase complex is involved in the regulation of protein
RT   recruitment to initiate sequestering vesicle formation for nonspecific
RT   autophagy in Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 19:668-681(2008).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG29.
RX   PubMed=18287526; DOI=10.1091/mbc.e07-10-1048;
RA   Kawamata T., Kamada Y., Kabeya Y., Sekito T., Ohsumi Y.;
RT   "Organization of the pre-autophagosomal structure responsible for
RT   autophagosome formation.";
RL   Mol. Biol. Cell 19:2039-2050(2008).
RN   [18]
RP   FUNCTION.
RX   PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA   Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA   Millen J., Goldfarb D.S., Thumm M.;
RT   "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT   genes.";
RL   Mol. Biol. Cell 19:4492-4505(2008).
RN   [19]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18298591; DOI=10.1111/j.1600-0854.2008.00715.x;
RA   Bugnicourt A., Mari M., Reggiori F., Haguenauer-Tsapis R., Galan J.M.;
RT   "Irs4p and Tax4p: two redundant EH domain proteins involved in autophagy.";
RL   Traffic 9:755-769(2008).
RN   [20]
RP   FUNCTION.
RX   PubMed=19223769; DOI=10.4161/auto.5.5.8091;
RA   Yorimitsu T., He C., Wang K., Klionsky D.J.;
RT   "Tap42-associated protein phosphatase type 2A negatively regulates
RT   induction of autophagy.";
RL   Autophagy 5:616-624(2009).
RN   [21]
RP   FUNCTION.
RX   PubMed=19061865; DOI=10.1016/j.bbrc.2008.11.084;
RA   Kageyama T., Suzuki K., Ohsumi Y.;
RT   "Lap3 is a selective target of autophagy in yeast, Saccharomyces
RT   cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 378:551-557(2009).
RN   [22]
RP   IDENTIFICATION IN THE ATG17-ATG29-ATG31 COMPLEX, AND INTERACTION WITH THE
RP   ATG1-ATG13 COMPLEX.
RX   PubMed=19755117; DOI=10.1016/j.bbrc.2009.09.034;
RA   Kabeya Y., Noda N.N., Fujioka Y., Suzuki K., Inagaki F., Ohsumi Y.;
RT   "Characterization of the Atg17-Atg29-Atg31 complex specifically required
RT   for starvation-induced autophagy in Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 389:612-615(2009).
RN   [23]
RP   FUNCTION, AND INTERACTION WITH ATG9.
RX   PubMed=19371383; DOI=10.1111/j.1365-2443.2009.01299.x;
RA   Sekito T., Kawamata T., Ichikawa R., Suzuki K., Ohsumi Y.;
RT   "Atg17 recruits Atg9 to organize the pre-autophagosomal structure.";
RL   Genes Cells 14:525-538(2009).
RN   [24]
RP   FUNCTION, AND INTERACTION WITH ATG13.
RX   PubMed=19805182; DOI=10.1073/pnas.0903316106;
RA   Stephan J.S., Yeh Y.Y., Ramachandran V., Deminoff S.J., Herman P.K.;
RT   "The Tor and PKA signaling pathways independently target the Atg1/Atg13
RT   protein kinase complex to control autophagy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17049-17054(2009).
RN   [25]
RP   FUNCTION.
RX   PubMed=20439775; DOI=10.1534/genetics.110.116566;
RA   Yeh Y.Y., Wrasman K., Herman P.K.;
RT   "Autophosphorylation within the Atg1 activation loop is required for both
RT   kinase activity and the induction of autophagy in Saccharomyces
RT   cerevisiae.";
RL   Genetics 185:871-882(2010).
RN   [26]
RP   FUNCTION.
RX   PubMed=20729555; DOI=10.1074/jbc.m110.147264;
RA   LeBlanc M.A., McMaster C.R.;
RT   "Lipid binding requirements for oxysterol-binding protein Kes1 inhibition
RT   of autophagy and endosome-trans-Golgi trafficking pathways.";
RL   J. Biol. Chem. 285:33875-33884(2010).
RN   [27]
RP   INTERACTION WITH COG1; COG3 AND COG4.
RX   PubMed=20065092; DOI=10.1083/jcb.200904075;
RA   Yen W.L., Shintani T., Nair U., Cao Y., Richardson B.C., Li Z.,
RA   Hughson F.M., Baba M., Klionsky D.J.;
RT   "The conserved oligomeric Golgi complex is involved in double-membrane
RT   vesicle formation during autophagy.";
RL   J. Cell Biol. 188:101-114(2010).
RN   [28]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG1.
RX   PubMed=19995911; DOI=10.1128/mcb.01344-09;
RA   Kamada Y., Yoshino K., Kondo C., Kawamata T., Oshiro N., Yonezawa K.,
RA   Ohsumi Y.;
RT   "Tor directly controls the Atg1 kinase complex to regulate autophagy.";
RL   Mol. Cell. Biol. 30:1049-1058(2010).
RN   [29]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21703229; DOI=10.1016/j.bbrc.2011.06.061;
RA   Yamagata M., Obara K., Kihara A.;
RT   "Sphingolipid synthesis is involved in autophagy in Saccharomyces
RT   cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 410:786-791(2011).
RN   [30]
RP   FUNCTION, AND INTERACTION WITH ATG13.
RX   PubMed=21712380; DOI=10.1074/jbc.m111.250324;
RA   Yeh Y.Y., Shah K.H., Herman P.K.;
RT   "An Atg13 protein-mediated self-association of the Atg1 protein kinase is
RT   important for the induction of autophagy.";
RL   J. Biol. Chem. 286:28931-28939(2011).
RN   [31]
RP   INTERACTION WITH ATG13.
RX   PubMed=22885598; DOI=10.1038/emboj.2012.225;
RA   Kraft C., Kijanska M., Kalie E., Siergiejuk E., Lee S.S., Semplicio G.,
RA   Stoffel I., Brezovich A., Verma M., Hansmann I., Ammerer G., Hofmann K.,
RA   Tooze S., Peter M.;
RT   "Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8
RT   regulates autophagy.";
RL   EMBO J. 31:3691-3703(2012).
RN   [32]
RP   INTERACTION WITH ATG1.
RX   PubMed=22778255; DOI=10.1074/jbc.c112.387514;
RA   Nakatogawa H., Ohbayashi S., Sakoh-Nakatogawa M., Kakuta S., Suzuki S.W.,
RA   Kirisako H., Kondo-Kakuta C., Noda N.N., Yamamoto H., Ohsumi Y.;
RT   "The autophagy-related protein kinase Atg1 interacts with the ubiquitin-
RT   like protein Atg8 via the Atg8 family interacting motif to facilitate
RT   autophagosome formation.";
RL   J. Biol. Chem. 287:28503-28507(2012).
RN   [33]
RP   FUNCTION.
RX   PubMed=22768199; DOI=10.1371/journal.pone.0040013;
RA   Mijaljica D., Prescott M., Devenish R.J.;
RT   "A late form of nucleophagy in Saccharomyces cerevisiae.";
RL   PLoS ONE 7:E40013-E40013(2012).
RN   [34]
RP   FUNCTION.
RX   PubMed=23169651; DOI=10.1073/pnas.1218065109;
RA   Dotiwala F., Eapen V.V., Harrison J.C., Arbel-Eden A., Ranade V.,
RA   Yoshida S., Haber J.E.;
RT   "DNA damage checkpoint triggers autophagy to regulate the initiation of
RT   anaphase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:E41-E49(2013).
CC   -!- FUNCTION: Autophagy-specific protein that functions with ATG13, ATG29,
CC       and CIS1/ATG31 in response to autophagy-inducing signals as a scaffold
CC       to recruit other ATG proteins to organize pre-autophagosomal structure
CC       (PAS) formation. Modulates the timing and magnitude of the autophagy
CC       response, such as the size of the sequestering vesicles, through
CC       interacting with and regulating ATG1 kinase activity. Plays
CC       particularly a role in pexophagy and nucleophagy. With ATG13, is
CC       required for ATG1 activation by autophosphorylation of 'Thr-226'.
CC       Recruits ATG9 to the pre-autophagosomal structure. Also plays a role in
CC       regulation of filamentous growth. {ECO:0000269|PubMed:10995454,
CC       ECO:0000269|PubMed:11486014, ECO:0000269|PubMed:12048214,
CC       ECO:0000269|PubMed:15743910, ECO:0000269|PubMed:15901835,
CC       ECO:0000269|PubMed:17362880, ECO:0000269|PubMed:17700056,
CC       ECO:0000269|PubMed:18077553, ECO:0000269|PubMed:18287526,
CC       ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:19061865,
CC       ECO:0000269|PubMed:19223769, ECO:0000269|PubMed:19371383,
CC       ECO:0000269|PubMed:19805182, ECO:0000269|PubMed:19995911,
CC       ECO:0000269|PubMed:20439775, ECO:0000269|PubMed:20729555,
CC       ECO:0000269|PubMed:21712380, ECO:0000269|PubMed:22768199,
CC       ECO:0000269|PubMed:23169651}.
CC   -!- SUBUNIT: Forms a complex with ATG13, ATG29 and CIS1/ATG31. The ATG17-
CC       ATG29-ATG31 complex interacts with the ATG1-ATG13 complex. Forms a
CC       complex with SNX4 and ATG20. Interacts with ATG11 and the conserved
CC       oligomeric Golgi (COG) complex subunits COG1, COG3 and COG4.
CC       {ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:12048214,
CC       ECO:0000269|PubMed:15659643, ECO:0000269|PubMed:15743910,
CC       ECO:0000269|PubMed:15901835, ECO:0000269|PubMed:17362880,
CC       ECO:0000269|PubMed:18287526, ECO:0000269|PubMed:19371383,
CC       ECO:0000269|PubMed:19755117, ECO:0000269|PubMed:19805182,
CC       ECO:0000269|PubMed:19995911, ECO:0000269|PubMed:20065092,
CC       ECO:0000269|PubMed:21712380, ECO:0000269|PubMed:22778255,
CC       ECO:0000269|PubMed:22885598}.
CC   -!- INTERACTION:
CC       Q06410; Q06628: ATG13; NbExp=6; IntAct=EBI-30856, EBI-36188;
CC       Q06410; Q12421: ATG31; NbExp=3; IntAct=EBI-30856, EBI-34768;
CC       Q06410; P47057: SNX4; NbExp=2; IntAct=EBI-30856, EBI-17610;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane;
CC       Peripheral membrane protein.
CC   -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATG17 family. {ECO:0000305}.
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DR   EMBL; U20939; AAB67509.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09725.1; -; Genomic_DNA.
DR   PIR; S53410; S53410.
DR   RefSeq; NP_013527.3; NM_001182311.3.
DR   AlphaFoldDB; Q06410; -.
DR   SMR; Q06410; -.
DR   BioGRID; 31682; 207.
DR   ComplexPortal; CPX-1676; ATG1 kinase complex.
DR   ComplexPortal; CPX-397; Atg17-Atg31-Atg29 complex.
DR   DIP; DIP-1490N; -.
DR   IntAct; Q06410; 85.
DR   MINT; Q06410; -.
DR   STRING; 4932.YLR423C; -.
DR   iPTMnet; Q06410; -.
DR   MaxQB; Q06410; -.
DR   PaxDb; Q06410; -.
DR   PRIDE; Q06410; -.
DR   EnsemblFungi; YLR423C_mRNA; YLR423C; YLR423C.
DR   GeneID; 851142; -.
DR   KEGG; sce:YLR423C; -.
DR   SGD; S000004415; ATG17.
DR   VEuPathDB; FungiDB:YLR423C; -.
DR   eggNOG; ENOG502QQDW; Eukaryota.
DR   HOGENOM; CLU_051526_0_0_1; -.
DR   InParanoid; Q06410; -.
DR   OMA; YLPENIW; -.
DR   BioCyc; YEAST:G3O-32483-MON; -.
DR   PRO; PR:Q06410; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06410; protein.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA: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:0032991; C:protein-containing complex; IPI:ComplexPortal.
DR   GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD.
DR   GO; GO:0060090; F:molecular adaptor activity; IGI:SGD.
DR   GO; GO:0030295; F:protein kinase activator activity; IMP:SGD.
DR   GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR   GO; GO:0032147; P:activation of protein kinase activity; IMP:SGD.
DR   GO; GO:0000045; P:autophagosome assembly; IDA:SGD.
DR   GO; GO:0006914; P:autophagy; IDA:ComplexPortal.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR   GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR   GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR   GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
DR   GO; GO:0045772; P:positive regulation of autophagosome size; IMP:SGD.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IDA:SGD.
DR   GO; GO:0006468; P:protein phosphorylation; IC:ComplexPortal.
DR   GO; GO:0042594; P:response to starvation; IC:ComplexPortal.
DR   InterPro; IPR007240; Atg17.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR28005; PTHR28005; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Coiled coil; Cytoplasm; Membrane; Reference proteome.
FT   CHAIN           1..417
FT                   /note="Autophagy-related protein 17"
FT                   /id="PRO_0000124566"
FT   COILED          146..221
FT                   /evidence="ECO:0000255"
FT   COILED          353..384
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         24
FT                   /note="C->R: Decreases affinity for ATG13."
FT                   /evidence="ECO:0000269|PubMed:15743910"
SQ   SEQUENCE   417 AA;  48656 MW;  71504B6C76549B75 CRC64;
     MNEADVTKFV NNARKTLTDA QLLCSSANLR IVDIKKKLSS WQLSISKLNF LIVGLRQQGK
     FLYTILKEGI GTKLIQKQWN QAVLVVLVDE MKYWQYEITS KVQRLDGIVN ELSISEKDDT
     DPSKLGDYIS RDNVNLLNDK LKEVPVIERQ IENIKLQYEN MVRKVNKELI DTKLTDVTQK
     FQSKFGIDNL METNVAEQFS RELTDLEKDL AEIMNSLTQH FDKTLLLQDK KIDNDEREEL
     FKVVQGDDKE LYNIFKTLHE VIDDVDKTIL NLGQFLQAKI KEKTELHSEV SEIINDFNRN
     LEYLLIFKDI SNLIDSFKNS CTQDIQTTKE LCEFYDNFEE SYGNLVLEAK RRKDVANRMK
     TILKDCEKQL QNLDAQDQEE RQNFIAENGT YLPETIWPGK IDDFSSLYTL NYNVKNP
 
 
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