NVJ1_YEAST
ID NVJ1_YEAST Reviewed; 321 AA.
AC P38881; D3DLE3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nucleus-vacuole junction protein 1;
DE Flags: Precursor;
GN Name=NVJ1; Synonyms=VAB36; OrderedLocusNames=YHR195W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 INTERACTION WITH VAC8, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10888680; DOI=10.1091/mbc.11.7.2445;
RA Pan X., Roberts P., Chen Y., Kvam E., Shulga N., Huang K., Lemmon S.,
RA Goldfarb D.S.;
RT "Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through
RT the direct interaction of Vac8p with Nvj1p.";
RL Mol. Biol. Cell 11:2445-2457(2000).
RN [4]
RP FUNCTION.
RX PubMed=12529432; DOI=10.1091/mbc.e02-08-0483;
RA Roberts P., Moshitch-Moshkovitz S., Kvam E., O'Toole E., Winey M.,
RA Goldfarb D.S.;
RT "Piecemeal microautophagy of nucleus in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:129-141(2003).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH OSH1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15367582; DOI=10.1242/jcs.01372;
RA Kvam E., Goldfarb D.S.;
RT "Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein
RT homolog Osh1p in Saccharomyces cerevisiae.";
RL J. Cell Sci. 117:4959-4968(2004).
RN [8]
RP INTERACTION WITH TSC13, AND FUNCTION.
RX PubMed=15958487; DOI=10.1091/mbc.e05-04-0290;
RA Kvam E., Gable K., Dunn T.M., Goldfarb D.S.;
RT "Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-
RT chain fatty acids in the biogenesis of microautophagic vesicles.";
RL Mol. Biol. Cell 16:3987-3998(2005).
RN [9]
RP FUNCTION, DOMAINS, SUBCELLULAR LOCATION, AND INTERACTION WITH OSH1; TSC13
RP AND VAC8.
RX PubMed=16912077; DOI=10.1242/jcs.03093;
RA Kvam E., Goldfarb D.S.;
RT "Structure and function of nucleus-vacuole junctions: outer-nuclear-
RT membrane targeting of Nvj1p and a role in tryptophan uptake.";
RL J. Cell Sci. 119:3622-3633(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-199 AND SER-285, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-298, AND
RP IDENTIFICATION BY 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).
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.
CC {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:12529432,
CC ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:15958487,
CC ECO:0000269|PubMed:16912077}.
CC -!- SUBUNIT: Interacts with OSH1, TSC13 and VAC8.
CC {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:15367582,
CC ECO:0000269|PubMed:15958487, ECO:0000269|PubMed:16912077}.
CC -!- INTERACTION:
CC P38881; P39968: VAC8; NbExp=10; IntAct=EBI-24885, EBI-20212;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:16912077}; Single-pass
CC membrane protein {ECO:0000269|PubMed:10888680,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15367582,
CC ECO:0000269|PubMed:16912077}.
CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U00030; AAB68357.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06887.1; -; Genomic_DNA.
DR PIR; S46679; S46679.
DR RefSeq; NP_012065.3; NM_001179326.3.
DR PDB; 5H2C; X-ray; 3.51 A; B=139-165.
DR PDB; 5XJG; X-ray; 2.40 A; B/D=229-321.
DR PDBsum; 5H2C; -.
DR PDBsum; 5XJG; -.
DR AlphaFoldDB; P38881; -.
DR SMR; P38881; -.
DR BioGRID; 36629; 77.
DR ComplexPortal; CPX-1381; NVJ1-VAC8 nucleus-vacuole junction complex.
DR DIP; DIP-4215N; -.
DR IntAct; P38881; 3.
DR STRING; 4932.YHR195W; -.
DR iPTMnet; P38881; -.
DR MaxQB; P38881; -.
DR PaxDb; P38881; -.
DR PRIDE; P38881; -.
DR EnsemblFungi; YHR195W_mRNA; YHR195W; YHR195W.
DR GeneID; 856602; -.
DR KEGG; sce:YHR195W; -.
DR SGD; S000001238; NVJ1.
DR VEuPathDB; FungiDB:YHR195W; -.
DR eggNOG; ENOG502S8G9; Eukaryota.
DR HOGENOM; CLU_869201_0_0_1; -.
DR InParanoid; P38881; -.
DR OMA; EDNDIHP; -.
DR BioCyc; YEAST:G3O-31223-MON; -.
DR PRO; PR:P38881; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38881; protein.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005640; C:nuclear outer membrane; IC:ComplexPortal.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0006629; P:lipid metabolic process; IC:ComplexPortal.
DR GO; GO:0071562; P:nucleus-vacuole junction assembly; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..321
FT /note="Nucleus-vacuole junction protein 1"
FT /id="PRO_0000202937"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 73..125
FT /note="TSC13-binding"
FT REGION 139..195
FT /note="OSH1-binding"
FT REGION 211..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..321
FT /note="VAC8-binding"
FT REGION 299..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..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:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 321 AA; 36421 MW; 13F54DFE8D1E5875 CRC64;
MTRPPLVRGI FSLGLSVAVL KGVEKTVRKH LERQGWIEPQ KVDYELIFTI DRLKNLVDNK
REALTAEQPD AGELSWRKVF NFISRQSSEL DTRIYVLILL LSFLLPIAWT VLDGDRETTL
EDKDNDCNVD LIENERRLKH YNDGERAVLQ FGKNRSEPII LSYKDMNVLE GEHEFTSKEE
HSNSHLTSKS ENALNQVGSE DLLGCHLEKQ LEEDKNEPNG EADGEDDNNR EKDCSSSSEV
ESQSKCRKES TAEPDSLSRD TRTTSSLKSS TSFPISFKGS IDLKSLNQPS SLLHIQVSPT
KSSNLDAQVN TEQAYSQPFR Y
