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ATG19_YEAST
ID   ATG19_YEAST             Reviewed;         415 AA.
AC   P35193; D6W1Y6; Q6B1A6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Autophagy-related protein 19;
DE   AltName: Full=Cytoplasm-to-vacuole targeting protein 19;
GN   Name=ATG19; Synonyms=CVT19; OrderedLocusNames=YOL082W;
GN   ORFNames=O0980, YOL01;
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 [GENOMIC DNA].
RX   PubMed=7900427; DOI=10.1002/yea.320101015;
RA   Zumstein E., Griffin H., Schweizer M.;
RT   "Sequence of a 10.27 kb segment on the left arm of chromosome XV from
RT   Saccharomyces cerevisiae includes part of the IRA2 gene and a putative new
RT   gene.";
RL   Yeast 10:1383-1387(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8533473; DOI=10.1002/yea.320111009;
RA   Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT   "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT   than twice as many unknown as known open reading frames.";
RL   Yeast 11:975-986(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LAP4.
RX   PubMed=11382752; DOI=10.1074/jbc.m101438200;
RA   Leber R., Silles E., Sandoval I.V., Mazon M.J.;
RT   "Yol082p, a novel CVT protein involved in the selective targeting of
RT   aminopeptidase I to the yeast vacuole.";
RL   J. Biol. Chem. 276:29210-29217(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LAP4.
RX   PubMed=11430817; DOI=10.1016/s1097-2765(01)00263-5;
RA   Scott S.V., Guan J., Hutchins M.U., Kim J., Klionsky D.J.;
RT   "Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway.";
RL   Mol. Cell 7:1131-1141(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=12479807; DOI=10.1016/s1534-5807(02)00359-3;
RA   Suzuki K., Kamada Y., Ohsumi Y.;
RT   "Studies of cargo delivery to the vacuole mediated by autophagosomes in
RT   Saccharomyces cerevisiae.";
RL   Dev. Cell 3:815-824(2002).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LAP4; AMS1; ATG8 AND
RP   ATG11.
RX   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   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ATG8.
RX   PubMed=11675395; DOI=10.1074/jbc.m109134200;
RA   Kim J., Huang W.-P., Stromhaug P.E., Klionsky D.J.;
RT   "Convergence of multiple autophagy and cytoplasm to vacuole targeting
RT   components to a perivacuolar membrane compartment prior to de novo vesicle
RT   formation.";
RL   J. Biol. Chem. 277:763-773(2002).
RN   [11]
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   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12446664; DOI=10.1074/jbc.m210436200;
RA   Reggiori F., Wang C.-W., Stromhaug P.E., Shintani T., Klionsky D.J.;
RT   "Vps51 is part of the yeast Vps fifty-three tethering complex essential for
RT   retrograde traffic from the early endosome and Cvt vesicle completion.";
RL   J. Biol. Chem. 278:5009-5020(2003).
RN   [13]
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   [14]
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   [15]
RP   FUNCTION.
RX   PubMed=15138258; DOI=10.1074/jbc.m404399200;
RA   Shintani T., Klionsky D.J.;
RT   "Cargo proteins facilitate the formation of transport vesicles in the
RT   cytoplasm to vacuole targeting pathway.";
RL   J. Biol. Chem. 279:29889-29894(2004).
RN   [16]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15194695; DOI=10.1074/jbc.m401066200;
RA   Meiling-Wesse K., Barth H., Voss C., Eskelinen E.-L., Epple U.D., Thumm M.;
RT   "Atg21 is required for effective recruitment of Atg8 to the
RT   preautophagosomal structure during the Cvt pathway.";
RL   J. Biol. Chem. 279:37741-37750(2004).
RN   [17]
RP   FUNCTION, AND BIOTECHNOLOGY.
RX   PubMed=15801807; DOI=10.1021/bp049708y;
RA   Cebollero E., Carrascosa A.V., Gonzalez R.;
RT   "Evidence for yeast autophagy during simulation of sparkling wine aging: a
RT   reappraisal of the mechanism of yeast autolysis in wine.";
RL   Biotechnol. Prog. 21:614-616(2005).
RN   [18]
RP   UBIQUITINATION AT LYS-213 AND LYS-216, INTERACTION WITH UBP3, AND FUNCTION.
RX   PubMed=16186126; DOI=10.1074/jbc.m508064200;
RA   Baxter B.K., Abeliovich H., Zhang X., Stirling A.G., Burlingame A.L.,
RA   Goldfarb D.S.;
RT   "Atg19p ubiquitination and the cytoplasm to vacuole trafficking pathway in
RT   yeast.";
RL   J. Biol. Chem. 280:39067-39076(2005).
RN   [19]
RP   FUNCTION, SUBCELLULAR LOCATION, AND 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   [20]
RP   FUNCTION.
RX   PubMed=17132049; DOI=10.1371/journal.pbio.0040423;
RA   Bernales S., McDonald K.L., Walter P.;
RT   "Autophagy counterbalances endoplasmic reticulum expansion during the
RT   unfolded protein response.";
RL   PLoS Biol. 4:E423-E423(2006).
RN   [21]
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   [22]
RP   FUNCTION, INTERACTION WITH ATG8 AND ATG11, AND SUBCELLULAR LOCATION.
RX   PubMed=17192412; DOI=10.1091/mbc.e06-08-0683;
RA   Chang C.Y., Huang W.P.;
RT   "Atg19 mediates a dual interaction cargo sorting mechanism in selective
RT   autophagy.";
RL   Mol. Biol. Cell 18:919-929(2007).
RN   [23]
RP   FUNCTION.
RX   PubMed=17238920; DOI=10.1111/j.1365-2958.2006.05580.x;
RA   Mazon M.J., Eraso P., Portillo F.;
RT   "Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-
RT   associated degradation requires Atg19 and the Cvt/autophagy pathway.";
RL   Mol. Microbiol. 63:1069-1077(2007).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [25]
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).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [27]
RP   INTERACTION WITH ATG8.
RX   PubMed=19398890; DOI=10.4161/auto.5.4.7696;
RA   Ho K.H., Chang H.E., Huang W.P.;
RT   "Mutation at the cargo-receptor binding site of Atg8 also affects its
RT   general autophagy regulation function.";
RL   Autophagy 5:461-471(2009).
RN   [28]
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   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [30]
RP   FUNCTION.
RX   PubMed=21228276; DOI=10.1074/jbc.m110.177618;
RA   Kario E., Amar N., Elazar Z., Navon A.;
RT   "A new autophagy-related checkpoint in the degradation of an ERAD-M
RT   target.";
RL   J. Biol. Chem. 286:11479-11491(2011).
RN   [31]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH APE4.
RX   PubMed=21343297; DOI=10.1074/jbc.m110.173906;
RA   Yuga M., Gomi K., Klionsky D.J., Shintani T.;
RT   "Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by
RT   selective autophagy in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 286:13704-13713(2011).
RN   [32]
RP   INTERACTION WITH LAP4.
RX   PubMed=22123825; DOI=10.1074/jbc.m111.311696;
RA   Morales Quinones M., Winston J.T., Stromhaug P.E.;
RT   "Propeptide of aminopeptidase 1 protein mediates aggregation and vesicle
RT   formation in cytoplasm-to-vacuole targeting pathway.";
RL   J. Biol. Chem. 287:10121-10133(2012).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 412-415 IN COMPLEX WITH ATG8,
RP   DOMAIN, MUTAGENESIS OF TRP-412 AND LEU-415, AND FUNCTION.
RX   PubMed=19021777; DOI=10.1111/j.1365-2443.2008.01238.x;
RA   Noda N.N., Kumeta H., Nakatogawa H., Satoo K., Adachi W., Ishii J.,
RA   Fujioka Y., Ohsumi Y., Inagaki F.;
RT   "Structural basis of target recognition by Atg8/LC3 during selective
RT   autophagy.";
RL   Genes Cells 13:1211-1218(2008).
RN   [34]
RP   STRUCTURE BY NMR OF 254-367, FUNCTION, DOMAIN, AND INTERACTION WITH AMS1.
RX   PubMed=20659891; DOI=10.1074/jbc.m110.143545;
RA   Watanabe Y., Noda N.N., Kumeta H., Suzuki K., Ohsumi Y., Inagaki F.;
RT   "Selective transport of alpha-mannosidase by autophagic pathways:
RT   structural basis for cargo recognition by Atg19 and Atg34.";
RL   J. Biol. Chem. 285:30026-30033(2010).
CC   -!- FUNCTION: Cargo-receptor protein involved in the cytoplasm to vacuole
CC       transport (Cvt) and in autophagy. Recognizes cargo proteins, such as
CC       APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal
CC       structure for eventual engulfment by the autophagosome and targeting to
CC       the vacuole. Involved in the organization of the preautophagosomal
CC       structure (PAS). ATG19 association with cargo protein is required to
CC       localize ATG11 to the PAS. Also involved in endoplasmic reticulum-
CC       specific autophagic process, in selective removal of ER-associated
CC       degradation (ERAD) substrates, and is essential for the survival of
CC       cells subjected to severe ER stress. Also plays a role in regulation of
CC       filamentous growth. {ECO:0000269|PubMed:11382752,
CC       ECO:0000269|PubMed:11430817, ECO:0000269|PubMed:12479807,
CC       ECO:0000269|PubMed:12479808, ECO:0000269|PubMed:15138258,
CC       ECO:0000269|PubMed:15659643, ECO:0000269|PubMed:15801807,
CC       ECO:0000269|PubMed:16186126, ECO:0000269|PubMed:17132049,
CC       ECO:0000269|PubMed:17192412, ECO:0000269|PubMed:17238920,
CC       ECO:0000269|PubMed:17700056, ECO:0000269|PubMed:19021777,
CC       ECO:0000269|PubMed:19061865, ECO:0000269|PubMed:20659891,
CC       ECO:0000269|PubMed:21228276}.
CC   -!- SUBUNIT: Interacts with the vacuolar aminopeptidase 1 (LAP4) precursor
CC       and mature forms. Also interacts with AMS1, APE4, ATG8 ATG11, and UBP3.
CC       {ECO:0000269|PubMed:11382752, ECO:0000269|PubMed:11430817,
CC       ECO:0000269|PubMed:11675395, ECO:0000269|PubMed:12479808,
CC       ECO:0000269|PubMed:15659643, ECO:0000269|PubMed:16186126,
CC       ECO:0000269|PubMed:17192412, ECO:0000269|PubMed:19021777,
CC       ECO:0000269|PubMed:19398890, ECO:0000269|PubMed:20659891,
CC       ECO:0000269|PubMed:21343297, ECO:0000269|PubMed:22123825}.
CC   -!- INTERACTION:
CC       P35193; P14904: APE1; NbExp=3; IntAct=EBI-29291, EBI-2571;
CC       P35193; P53104: ATG1; NbExp=2; IntAct=EBI-29291, EBI-2657;
CC       P35193; Q12527: ATG11; NbExp=5; IntAct=EBI-29291, EBI-31977;
CC       P35193; P38182: ATG8; NbExp=5; IntAct=EBI-29291, EBI-2684;
CC       P35193; P29295: HRR25; NbExp=2; IntAct=EBI-29291, EBI-8536;
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000269|PubMed:11382752, ECO:0000269|PubMed:11430817,
CC       ECO:0000269|PubMed:11675395, ECO:0000269|PubMed:12446664,
CC       ECO:0000269|PubMed:12479808, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15194695, ECO:0000269|PubMed:15659643,
CC       ECO:0000269|PubMed:17192412, ECO:0000269|PubMed:18497569,
CC       ECO:0000269|PubMed:21343297}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11382752, ECO:0000269|PubMed:11430817,
CC       ECO:0000269|PubMed:11675395, ECO:0000269|PubMed:12446664,
CC       ECO:0000269|PubMed:12479808, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15194695, ECO:0000269|PubMed:15659643,
CC       ECO:0000269|PubMed:17192412, ECO:0000269|PubMed:18497569,
CC       ECO:0000269|PubMed:21343297}. Note=Also found in other perivacuolar
CC       punctate structures.
CC   -!- DOMAIN: The coiled coil domain is required for the interaction with
CC       LAP4.
CC   -!- DOMAIN: The C-terminal WXXL motif is crucial for ATG8-binding and Cvt
CC       pathway.
CC   -!- PTM: Polyubiquitinated at Lys-213 and Lys-216. Deubiquitination by UBP3
CC       is required for full activity of ATG19. {ECO:0000269|PubMed:16186126}.
CC   -!- BIOTECHNOLOGY: ATG19 is important for yeast autolysis which is the
CC       source of several molecules responsible for the quality of wines aged
CC       in contact with yeast cells. {ECO:0000269|PubMed:15801807}.
CC   -!- MISCELLANEOUS: Present with 1250 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X75449; CAA53201.1; -; Genomic_DNA.
DR   EMBL; X83121; CAA58199.1; -; Genomic_DNA.
DR   EMBL; Z74824; CAA99094.1; -; Genomic_DNA.
DR   EMBL; AY693174; AAT93193.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10702.1; -; Genomic_DNA.
DR   PIR; S48253; S48253.
DR   RefSeq; NP_014559.1; NM_001183336.1.
DR   PDB; 2KZB; NMR; -; A=254-367.
DR   PDB; 2ZPN; X-ray; 2.70 A; E/F/G/H=412-415.
DR   PDB; 5JGE; X-ray; 1.91 A; A/B/D/E=160-187.
DR   PDBsum; 2KZB; -.
DR   PDBsum; 2ZPN; -.
DR   PDBsum; 5JGE; -.
DR   AlphaFoldDB; P35193; -.
DR   BMRB; P35193; -.
DR   SMR; P35193; -.
DR   BioGRID; 34320; 87.
DR   DIP; DIP-1407N; -.
DR   ELM; P35193; -.
DR   IntAct; P35193; 21.
DR   MINT; P35193; -.
DR   STRING; 4932.YOL082W; -.
DR   iPTMnet; P35193; -.
DR   MaxQB; P35193; -.
DR   PaxDb; P35193; -.
DR   PRIDE; P35193; -.
DR   EnsemblFungi; YOL082W_mRNA; YOL082W; YOL082W.
DR   GeneID; 854072; -.
DR   KEGG; sce:YOL082W; -.
DR   SGD; S000005442; ATG19.
DR   VEuPathDB; FungiDB:YOL082W; -.
DR   GeneTree; ENSGT01030000240271; -.
DR   HOGENOM; CLU_055007_0_0_1; -.
DR   InParanoid; P35193; -.
DR   OMA; CREDAHE; -.
DR   BioCyc; YEAST:G3O-33485-MON; -.
DR   EvolutionaryTrace; P35193; -.
DR   PRO; PR:P35193; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P35193; protein.
DR   GO; GO:0034270; C:Cvt complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
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:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0031503; P:protein-containing complex localization; IMP:SGD.
DR   GO; GO:0061912; P:selective autophagy; IMP:SGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR   GO; GO:0016050; P:vesicle organization; IMP:SGD.
DR   InterPro; IPR024543; Atg19/Atg34_C.
DR   Pfam; PF12744; ATG19; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Coiled coil; Isopeptide bond; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..415
FT                   /note="Autophagy-related protein 19"
FT                   /id="PRO_0000064722"
FT   REGION          21..28
FT                   /note="ATG11-binding"
FT   REGION          126..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..367
FT                   /note="AMS1-binding"
FT   REGION          406..415
FT                   /note="ATG8-binding"
FT   COILED          157..187
FT                   /evidence="ECO:0000255"
FT   MOTIF           412..415
FT                   /note="WXXL"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   CROSSLNK        213
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:16186126"
FT   CROSSLNK        216
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:16186126"
FT   MUTAGEN         412
FT                   /note="W->A: Impairs vacuolar transport of LAP4."
FT                   /evidence="ECO:0000269|PubMed:19021777"
FT   MUTAGEN         415
FT                   /note="L->A: Impairs vacuolar transport of LAP4."
FT                   /evidence="ECO:0000269|PubMed:19021777"
FT   CONFLICT        412
FT                   /note="W -> R (in Ref. 5; AAT93193)"
FT                   /evidence="ECO:0000305"
FT   HELIX           161..184
FT                   /evidence="ECO:0007829|PDB:5JGE"
FT   STRAND          262..269
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          272..279
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          281..283
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          295..299
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          318..322
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          342..348
FT                   /evidence="ECO:0007829|PDB:2KZB"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:2KZB"
SQ   SEQUENCE   415 AA;  47599 MW;  B49DA1DF83A04070 CRC64;
     MNNSKTNQQM NTSMGYPLTV YDECNKFQLI VPTLDANIML WCIGQLSLLN DSNGCKHLFW
     QPNDKSNVRI LLNNYDYGHL FKYLQCQRKC SVYIGEGTLK KYNLTISTSF DNFLDLTPSE
     EKESLCREDA HEDPVSPKAG SEEEISPNST SNVVVSRECL DNFMKQLLKL EESLNKLELE
     QKVTNKEPNH RISGTIDIPE DRSELVNFFT ELKTVKQLED VFQRYHDYER LSQECDSKTE
     IASDHSKKET KIEVEPPNER SLQITMNQRD NSLYFQLFNN TNSVLAGNCK LKFTDAGDKP
     TTQIIDMGPH EIGIKEYKEY RYFPYALDLE AGSTIEIENQ YGEVIFLGKY GSSPMINLRP
     PSRLSAESLQ ASQEPFYSFQ IDTLPELDDS SIISTSISLS YDGDDNEKAL TWEEL
 
 
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