ATG34_YEAST
ID ATG34_YEAST Reviewed; 412 AA.
AC Q12292; D6W1Y5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Autophagy-related protein 34;
GN Name=ATG34; Synonyms=ATG19-B; OrderedLocusNames=YOL083W; ORFNames=O0957;
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].
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 [2]
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 [3]
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 [4]
RP IDENTIFICATION BY 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AMS1; ATG8 AND ATG11.
RX PubMed=20639194; DOI=10.1074/jbc.m110.143511;
RA Suzuki K., Kondo C., Morimoto M., Ohsumi Y.;
RT "Selective transport of alpha-mannosidase by autophagic pathways:
RT identification of a novel receptor, Atg34p.";
RL J. Biol. Chem. 285:30019-30025(2010).
RN [6]
RP STRUCTURE BY NMR OF 246-348, FUNCTION, DOMAIN AMS1-BINDING, AND INTERACTION
RP 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 AMS1 and delivers them to the pre-autophagosomal structure for eventual
CC engulfment by the autophagosome and targeting to the vacuole.
CC {ECO:0000269|PubMed:20639194, ECO:0000269|PubMed:20659891}.
CC -!- SUBUNIT: Interacts with AMS1, ATG8 and ATG11.
CC {ECO:0000269|PubMed:20639194, ECO:0000269|PubMed:20659891}.
CC -!- INTERACTION:
CC Q12292; P22855: AMS1; NbExp=3; IntAct=EBI-36362, EBI-10398;
CC Q12292; Q12527: ATG11; NbExp=2; IntAct=EBI-36362, EBI-31977;
CC Q12292; P38182: ATG8; NbExp=4; IntAct=EBI-36362, EBI-2684;
CC Q12292; P29295: HRR25; NbExp=2; IntAct=EBI-36362, EBI-8536;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:20639194}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20639194}. Note=Membrane-associated protein found
CC in pre-autophagosomal structure and other perivacuolar punctate
CC structures.
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DR EMBL; X83121; CAA58197.1; -; Genomic_DNA.
DR EMBL; Z74825; CAA99095.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10701.1; -; Genomic_DNA.
DR PIR; S57387; S57387.
DR RefSeq; NP_014558.1; NM_001183337.1.
DR PDB; 2KZK; NMR; -; A=246-348.
DR PDBsum; 2KZK; -.
DR AlphaFoldDB; Q12292; -.
DR BMRB; Q12292; -.
DR SMR; Q12292; -.
DR BioGRID; 34319; 71.
DR DIP; DIP-1598N; -.
DR IntAct; Q12292; 18.
DR MINT; Q12292; -.
DR STRING; 4932.YOL083W; -.
DR iPTMnet; Q12292; -.
DR MaxQB; Q12292; -.
DR PaxDb; Q12292; -.
DR PRIDE; Q12292; -.
DR EnsemblFungi; YOL083W_mRNA; YOL083W; YOL083W.
DR GeneID; 854071; -.
DR KEGG; sce:YOL083W; -.
DR SGD; S000005443; ATG34.
DR VEuPathDB; FungiDB:YOL083W; -.
DR GeneTree; ENSGT01030000240271; -.
DR HOGENOM; CLU_055007_0_0_1; -.
DR InParanoid; Q12292; -.
DR BioCyc; YEAST:G3O-33486-MON; -.
DR EvolutionaryTrace; Q12292; -.
DR PRO; PR:Q12292; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12292; protein.
DR GO; GO:0034270; C:Cvt complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IGI:SGD.
DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IGI:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:0031503; P:protein-containing complex localization; IGI:SGD.
DR InterPro; IPR024543; Atg19/Atg34_C.
DR Pfam; PF12744; ATG19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..412
FT /note="Autophagy-related protein 34"
FT /id="PRO_0000235927"
FT REGION 246..348
FT /note="AMS1-binding"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:2KZK"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2KZK"
SQ SEQUENCE 412 AA; 46655 MW; 5F339CC6AC2824D5 CRC64;
MKIAVETTLF DFFVIDQFKK STFSAPNTKV DTIKGCINKF IEQFNVYDEQ HIFWQPPGKS
NVRLLSNAND FGQLGNFLHK KIKCNIFIGE EALRKYDLNI CGPYDKFVEN SDPSVKKVVN
RDDVMLSRKC LNIISEQLSI LEKSISKAQN QVLQSSEVEG KKCIILPEDK PELIKFFSKF
ETSVQLQEVY EGYKVYEKLL QKFGGQKKRM ESFLNENTPM SGAEAIKQIN ISEELKEKGE
RLTTPNDPLL HVEVSNEDNS LHFILYNKTN IIIPGNCTFE FSSQISEVFS IKMGPHEIGI
KGQKELWFFP SLPTPLSNYT MKVVNQDGET ILVGKCADSN EITLKSPLAS FSTGSFQTGS
FHTLQDPTNV FRADALSSPD ESSIMSTPFL GETDEVYNSG STLSRPFTWE EI
