NVJ2_YEAST
ID NVJ2_YEAST Reviewed; 770 AA.
AC Q06833; D6W491;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nucleus-vacuole junction protein 2 {ECO:0000303|PubMed:22250200};
GN Name=NVJ2 {ECO:0000303|PubMed:22250200, ECO:0000312|SGD:S000006295};
GN OrderedLocusNames=YPR091C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-669; SER-720 AND
RP SER-723, AND IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-669, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-669 AND SER-723, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-669; SER-717;
RP SER-720 AND SER-723, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=22250200; DOI=10.1242/jcs.085118;
RA Toulmay A., Prinz W.A.;
RT "A conserved membrane-binding domain targets proteins to organelle contact
RT sites.";
RL J. Cell Sci. 125:49-58(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-340 AND ILE-472.
RX PubMed=28011845; DOI=10.1083/jcb.201606059;
RA Liu L.K., Choudhary V., Toulmay A., Prinz W.A.;
RT "An inducible ER-Golgi tether facilitates ceramide transport to alleviate
RT lipotoxicity.";
RL J. Cell Biol. 216:131-147(2017).
CC -!- FUNCTION: During endoplasmic reticulum (ER) stress or when cellular
CC ceramide levels increase, induces contacts between the ER and medial-
CC Golgi complex to facilitate non-vesicular transport of ceramides from
CC the ER to the Golgi complex where they are converted to complex
CC sphingolipids, preventing toxic ceramide accumulation.
CC {ECO:0000269|PubMed:28011845}.
CC -!- INTERACTION:
CC Q06833; P47068: BBC1; NbExp=2; IntAct=EBI-37290, EBI-3437;
CC Q06833; P39743: RVS167; NbExp=3; IntAct=EBI-37290, EBI-14500;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass type II membrane protein
CC {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:22250200}; Single-
CC pass type II membrane protein {ECO:0000305}. Note=Enriched at the
CC nucleus-vacuole junction where it becomes increasingly concentrated as
CC cells enter into the late-logarithmic growth phase (PubMed:22250200).
CC During endoplasmic reticulum (ER) stress, localizes to ER-Golgi
CC contacts (PubMed:28011845). {ECO:0000269|PubMed:22250200,
CC ECO:0000269|PubMed:28011845}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC ProRule:PRU01194, ECO:0000269|PubMed:22250200}.
CC -!- MISCELLANEOUS: Present with 36500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U51033; AAB68138.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11507.1; -; Genomic_DNA.
DR PIR; S69075; S69075.
DR RefSeq; NP_015416.1; NM_001184188.1.
DR AlphaFoldDB; Q06833; -.
DR BioGRID; 36260; 80.
DR IntAct; Q06833; 6.
DR MINT; Q06833; -.
DR STRING; 4932.YPR091C; -.
DR iPTMnet; Q06833; -.
DR MaxQB; Q06833; -.
DR PaxDb; Q06833; -.
DR PRIDE; Q06833; -.
DR EnsemblFungi; YPR091C_mRNA; YPR091C; YPR091C.
DR GeneID; 856207; -.
DR KEGG; sce:YPR091C; -.
DR SGD; S000006295; NVJ2.
DR VEuPathDB; FungiDB:YPR091C; -.
DR eggNOG; KOG2238; Eukaryota.
DR GeneTree; ENSGT00940000173509; -.
DR HOGENOM; CLU_012852_2_0_1; -.
DR InParanoid; Q06833; -.
DR OMA; MDDIVFY; -.
DR BioCyc; YEAST:G3O-34233-MON; -.
DR PRO; PR:Q06833; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06833; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:UniProtKB.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR031468; SMP_LBD.
DR Pfam; PF10296; MMM1; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid transport; Lipid-binding;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..770
FT /note="Nucleus-vacuole junction protein 2"
FT /id="PRO_0000257815"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..770
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 114..266
FT /note="PH"
FT DOMAIN 304..504
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT REGION 541..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 340
FT /note="L->A: Failure to mediate ceramide transport; when
FT associated with A-472."
FT /evidence="ECO:0000269|PubMed:28011845"
FT MUTAGEN 472
FT /note="I->A: Failure to mediate ceramide transport; when
FT associated with A-340."
FT /evidence="ECO:0000269|PubMed:28011845"
SQ SEQUENCE 770 AA; 87324 MW; E4A1EF69AA49E06A CRC64;
MASLKVFLAV YLLGGITFLP LVLFTLYKIH LLYSNLKSAS KKELDHDTAD EIDEKTRLLA
RDIDPEFKAR KLEEQLGVKV FNKGWITVTK QYYYHSSEVA VILKNSNNNK DSDTALQEQI
LQRTDLKKKQ RFFAVLRHGN LFLYKDDSQN ANLVHAISLQ NRFITIWPRF DELGKEELPD
ASLFTKRTCI AIFKNDLVSI DSKNHNVILP HFDPLTSAES NNGDISTNDT THEYQSQFHS
SNQFFLYFDN NMDKEDWYYQ LINASKNSNS LSTGLLDPNV SANAAHLKTK DMLQLIQDIN
STENQLTTKW LNALLGRLFL SLQQTDTLNK FIHEKICKKL NKIKTPGFLD DLVVEKVDVG
DSAPLFTSPE LLELSPEGST KIAIDVQYRG NLTIIIATKA SINLGSRFKQ REVSLQLSIK
IKEFSGPLLF LIKPPPSNRI WYAFRTEPIM DFEIEPIVSS SKLSYNVVTN AIKSKFAEAV
KESLVVPFMD DIVFYPTPNE VYRGGIWEEQ DPEAAARART AAAASDMNNT SAKEHLEALQ
EGGMKTQSRI KKALRPERKK ENLKDLVDAS GVATKTTTQT TVTTATNDDV SSSENSTKSR
KYFKNSIKKI GRWYKDNVGN SSDTEDMDEI DVQDKKNDDS ADERESDNPI LTSNPKMISN
RRPVPRRPSQ PLNTLSPKLE GRKEKDTENF PVPPSASNMN ASKMFANKEN RKFSVSSNDS
QNSLKNGDPH VKASKLESSQ AFVKKTSQNR FNDGFFKQDL EFEEQREPKL
