ID   NVJ1_YEAS7              Reviewed;         321 AA.
AC   A6ZTA1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Nucleus-vacuole junction protein 1;
DE   Flags: Precursor;
GN   Name=NVJ1; Synonyms=VAB36; ORFNames=SCY_2585;
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: Involved in the formation of nucleus-vacuole (NV) junctions
CC       during piecemeal microautophagy of the nucleus (PMN). NV junctions are
CC       interorganelle interfaces mediated by NVJ1 in the nuclear envelope and
CC       VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like
CC       patches through which teardrop-like portions of the nucleus are pinched
CC       off into the vacuolar lumen and degraded by the PMN process. Acts also
CC       as an outer-nuclear membrane receptor for OSH1 and TSC13 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with OSH1, TSC13 and VAC8. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
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DR   EMBL; AAFW02000082; EDN62432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZTA1; -.
DR   SMR; A6ZTA1; -.
DR   PRIDE; A6ZTA1; -.
DR   EnsemblFungi; EDN62432; EDN62432; SCY_2585.
DR   HOGENOM; CLU_869201_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Autophagy; Membrane; Nucleus; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..321
FT                   /note="Nucleus-vacuole junction protein 1"
FT                   /id="PRO_0000320430"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          73..125
FT                   /note="TSC13-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          139..195
FT                   /note="OSH1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          174..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..321
FT                   /note="VAC8-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          299..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38881"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38881"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38881"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38881"
SQ   SEQUENCE   321 AA;  36364 MW;  131FE7543643FFF5 CRC64;
     MTRPPLVRGI FSLGLSVAVL KGVEKTVRKH LERQGWIEPQ KVDYELIFTI DRLKNLVDNK
     REALTAEQPD AGELSWRKVF NFISRQSSEL DARIYVLILL LSFLLPIAWT VLDGDRETTL
     EDKDNDCNVD LIENERRLKH YNDGERAVLQ FGKNRSEPII LSYKDMNVLE GEHEFTSKEE
     HSNSHLTSKS ENALSQVGSE DLLGCHLEKQ LEEDKNEPNG EADGEDDNNR EKDCSSSSEV
     ESQSKCRKES TAEPDSLSRD TRTTSSLKSS TSFPISFKGS IDLKSLNQPS SLLHIQVSPT
     KSSNLDAQVN TEQAYSQPFR Y