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 27-MAR-2024, entry version 148. 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). RN [13] {ECO:0007744|PDB:5XJG} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 229-321 IN COMPLEX WITH VAC8, RP FUNCTION, DOMAIN, AND INTERACTION WITH VAC8. RX PubMed=28533415; DOI=10.1073/pnas.1701030114; RA Jeong H., Park J., Kim H.I., Lee M., Ko Y.J., Lee S., Jun Y., Lee C.; RT "Mechanistic insight into the nucleus-vacuole junction based on the Vac8p- RT Nvj1p crystal structure."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E4539-E4548(2017). RN [14] {ECO:0007744|PDB:5H2C} RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 139-165 IN COMPLEX WITH OSH1, RP FUNCTION, AND INTERACTION WITH OSH1. RX PubMed=28319008; DOI=10.1016/j.str.2017.02.010; RA Manik M.K., Yang H., Tong J., Im Y.J.; RT "Structure of yeast OSBP-related protein Osh1 reveals key determinants for RT lipid transport and protein targeting at the nucleus-vacuole junction."; RL Structure 25:617-629.e3(2017). CC -!- FUNCTION: Involved in the formation of nucleus-vacuole junctions (NVJs) CC during piecemeal microautophagy of the nucleus (PMN) (PubMed:10888680, CC PubMed:12529432, PubMed:16912077). NVJs are interorganelle interfaces CC mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole CC membrane (PubMed:10888680, PubMed:12529432, PubMed:16912077). Together, CC NVJ1 and VAC8 form Velcro-like patches through which teardrop-like CC portions of the nucleus are pinched off into the vacuolar lumen and CC degraded by the PMN process (PubMed:10888680, PubMed:12529432, CC PubMed:16912077, PubMed:28533415). Acts also as an outer-nuclear CC membrane receptor for OSH1 and TSC13 (PubMed:15367582, PubMed:15958487, CC PubMed:16912077, PubMed:28319008). {ECO:0000269|PubMed:10888680, CC ECO:0000269|PubMed:12529432, ECO:0000269|PubMed:15367582, CC ECO:0000269|PubMed:15958487, ECO:0000269|PubMed:16912077, CC ECO:0000269|PubMed:28319008, ECO:0000269|PubMed:28533415}. CC -!- SUBUNIT: Interacts with OSH1, TSC13 and VAC8. CC {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:12529432, CC ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:15958487, CC ECO:0000269|PubMed:16912077, ECO:0000269|PubMed:28533415}. 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 -!- DOMAIN: The extended 80 Angstroms-longloop of NVJ1 specifically binds CC the highly conserved innergroove formed by the armadillo repeats of CC VAC8. {ECO:0000269|PubMed:28533415}. CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 79. 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; 4932-YHR195W; -. DR PeptideAtlas; P38881; -. DR EnsemblFungi; YHR195W_mRNA; YHR195W; YHR195W. DR GeneID; 856602; -. DR KEGG; sce:YHR195W; -. DR AGR; SGD:S000001238; -. 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 OrthoDB; 2027684at2759; -. DR BioCyc; YEAST:G3O-31223-MONOMER; -. DR BioGRID-ORCS; 856602; 0 hits in 10 CRISPR screens. DR PRO; PR:P38881; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P38881; Protein. DR GO; GO:0016020; C:membrane; IDA:SGD. DR GO; GO:0005635; C:nuclear envelope; IDA:SGD. DR GO; GO:0005640; C:nuclear outer membrane; NAS: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; NAS: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 //