ID   ATG19_YEAS7             Reviewed;         415 AA.
AC   A6ZNC8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Autophagy-related protein 19;
DE   AltName: Full=Cytoplasm-to-vacuole targeting protein 19;
GN   Name=ATG19; Synonyms=CVT19; ORFNames=SCY_4996;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Also
CC       found in other perivacuolar punctate structures. {ECO:0000250}.
CC   -!- DOMAIN: The coiled coil domain is required for the interaction with
CC       LAP4. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal WXXL motif is crucial for ATG8-binding and Cvt
CC       pathway. {ECO:0000250}.
CC   -!- PTM: Polyubiquitinated at Lys-213 and Lys-216. Deubiquitination by UBP3
CC       is required for full activity of ATG19. {ECO:0000250}.
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DR   EMBL; AAFW02000030; EDN63793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZNC8; -.
DR   BMRB; A6ZNC8; -.
DR   SMR; A6ZNC8; -.
DR   PRIDE; A6ZNC8; -.
DR   EnsemblFungi; EDN63793; EDN63793; SCY_4996.
DR   HOGENOM; CLU_055007_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024543; Atg19/Atg34_C.
DR   Pfam; PF12744; ATG19; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Isopeptide bond; Membrane; Phosphoprotein;
KW   Protein transport; Transport; Ubl conjugation.
FT   CHAIN           1..415
FT                   /note="Autophagy-related protein 19"
FT                   /id="PRO_0000317991"
FT   REGION          21..28
FT                   /note="ATG11-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          126..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..367
FT                   /note="AMS1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          406..415
FT                   /note="ATG8-binding"
FT                   /evidence="ECO:0000250"
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:0000250|UniProtKB:P35193"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35193"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35193"
FT   CROSSLNK        213
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P35193"
FT   CROSSLNK        216
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P35193"
SQ   SEQUENCE   415 AA;  47600 MW;  EE9DAB7F2E6D871D 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 SLQITMDQRD NSLYFQLFNN TNSVLAGNCK LKFTDAGDKP
     TTQIIDMGPH EIGIKEYKEY RYFPYALDLE AGSTIEIENQ YGEVIFLGKY GSSPMINLRP
     PSRLSAESLQ ASQEPFYSFQ IDTLPELDDS SIISTSISLS YDGDDNEKAL TWEEL