NPR2_YEAST
ID NPR2_YEAST Reviewed; 615 AA.
AC P39923; D3DLI8; Q6B264;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Nitrogen permease regulator 2;
GN Name=NPR2; OrderedLocusNames=YEL062W;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7867803; DOI=10.1016/0014-5793(95)00038-b;
RA Rousselet G., Simon M., Ripoche P., Buhler J.-M.;
RT "A second nitrogen permease regulator in Saccharomyces cerevisiae.";
RL FEBS Lett. 359:215-219(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP INVOLVEMENT IN CISPLATIN RESISTANCE.
RX PubMed=12869630; DOI=10.1124/mol.64.2.259;
RA Schenk P.W., Brok M., Boersma A.W., Brandsma J.A., Den Dulk H., Burger H.,
RA Stoter G., Brouwer J., Nooter K.;
RT "Anticancer drug resistance induced by disruption of the Saccharomyces
RT cerevisiae NPR2 gene: a novel component involved in cisplatin- and
RT doxorubicin-provoked cell kill.";
RL Mol. Pharmacol. 64:259-268(2003).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP 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 FUNCTION, AND INTERACTION WITH NPR3.
RX PubMed=19521502; DOI=10.1371/journal.pgen.1000515;
RA Neklesa T.K., Davis R.W.;
RT "A genome-wide screen for regulators of TORC1 in response to amino acid
RT starvation reveals a conserved Npr2/3 complex.";
RL PLoS Genet. 5:E1000515-E1000515(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP 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 [11]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26510498; DOI=10.1091/mbc.e15-08-0581;
RA Kim A., Cunningham K.W.;
RT "A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane
RT permeabilization in response to endoplasmic reticulum membrane stress.";
RL Mol. Biol. Cell 26:4631-4645(2015).
CC -!- FUNCTION: Component of the SEA complex which coats the vacuolar
CC membrane and is involved in intracellular trafficking, autophagy,
CC response to nitrogen starvation, and amino acid biogenesis
CC (PubMed:21454883). Mediates inactivation of the TORC1 complex in
CC response to amino acid starvation (PubMed:19521502, PubMed:26510498).
CC Post-transcriptional regulator of nitrogen permeases (PubMed:19521502).
CC May be involved in putative NPR1-dependent phosphorylation of nitrogen
CC permeases or in the processing and targeting of nitrogen permeases at
CC the level of the endoplasmic reticulum (PubMed:19521502).
CC {ECO:0000269|PubMed:19521502, ECO:0000269|PubMed:21454883,
CC ECO:0000269|PubMed:26510498}.
CC -!- SUBUNIT: Component of the SEA complex composed of at least IML1/SEA1,
CC RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1. Forms a
CC heterodimer with NPR3. {ECO:0000269|PubMed:21454883}.
CC -!- INTERACTION:
CC P39923; P38742: NPR3; NbExp=4; IntAct=EBI-12212, EBI-24336;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:21454883};
CC Peripheral membrane protein {ECO:0000269|PubMed:21454883}.
CC -!- INDUCTION: By urea and proline.
CC -!- DISRUPTION PHENOTYPE: TORC1 abnormally activated in presence of
CC rapamycin. {ECO:0000269|PubMed:26510498}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NPR2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65025.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT92885.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA55721.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X79105; CAA55721.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18795; AAB65025.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY692866; AAT92885.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006939; DAA07592.1; -; Genomic_DNA.
DR PIR; S44938; S44938.
DR RefSeq; NP_010852.4; NM_001178877.3.
DR AlphaFoldDB; P39923; -.
DR SMR; P39923; -.
DR BioGRID; 36667; 152.
DR ComplexPortal; CPX-3231; SEA complex.
DR DIP; DIP-1985N; -.
DR IntAct; P39923; 29.
DR MINT; P39923; -.
DR STRING; 4932.YEL062W; -.
DR iPTMnet; P39923; -.
DR MaxQB; P39923; -.
DR PaxDb; P39923; -.
DR PRIDE; P39923; -.
DR TopDownProteomics; P39923; -.
DR EnsemblFungi; YEL062W_mRNA; YEL062W; YEL062W.
DR GeneID; 856647; -.
DR KEGG; sce:YEL062W; -.
DR SGD; S000000788; NPR2.
DR VEuPathDB; FungiDB:YEL062W; -.
DR eggNOG; KOG3789; Eukaryota.
DR GeneTree; ENSGT00390000001414; -.
DR HOGENOM; CLU_014995_3_0_1; -.
DR InParanoid; P39923; -.
DR OMA; IDVNWDP; -.
DR BioCyc; YEAST:G3O-30177-MON; -.
DR PRO; PR:P39923; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39923; protein.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IDA:SGD.
DR GO; GO:1990130; C:GATOR1 complex; IDA:SGD.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:SGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR GO; GO:1903833; P:positive regulation of cellular response to amino acid starvation; IMP:SGD.
DR GO; GO:0015824; P:proline transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:SGD.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:0015840; P:urea transport; IMP:SGD.
DR InterPro; IPR009348; NPR2.
DR PANTHER; PTHR12991; PTHR12991; 1.
DR Pfam; PF06218; NPR2; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Transport; Vacuole.
FT CHAIN 1..615
FT /note="Nitrogen permease regulator 2"
FT /id="PRO_0000213321"
FT REGION 143..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 225
FT /note="D -> G (in Ref. 4; AAT92885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 69859 MW; 58CA4983B0BAF7BA CRC64;
MLSYFQGFVP IHTIFYSVFH PTEGSKIKYE FPPNNLKNHG INFNTFKNYI IPKPILCHKL
ITFKYGTYRI VCYPVTINSP IYARNFFSFN FVFVFPYDCE TSPYEPAITR LGKMFKVLEE
QNQLLSKSER DPVFFDLKVL ENSTTTPSTA GPSSTPNPSS NTTPTHPTSE KDTKDMRSSR
YSDLIKDLGL PQSAFSIQDL LMRIFQDLNN YSECLIPIDE GNAVDIKIFP LLRPPTTCVS
LEDVPLSSVN LKKIIDVNWD PTMMSIVPYI DGLNSIAKIS KLSNSDPGLV IECIRHLIYY
KCVTLSDIFQ FSNIYAPSSL IRNFLTDPLM ASDCQSYVTF PEVSKISNLP LNKSLGSGDQ
DSPSFSVRRK SKSSSIPSNP DSRTTSFSST SRVSQNSSLN SSFSSIYKDW RQSQTSCSSS
NIHVINNRNR FLPTRSCLFD LYRSLSQGQT LKTWYESKYM ILKENNIDIR RFITFGLEKR
IIYRCYSFPV MINAGSREPK EMTPIITKDL VNNDKLLEKR NHNHLLSATG SRNTAQSGNL
KPERPSKVSF EMQRVSSLAT GKSTMPKLSD EEEGILEESI RNAETFDKIC VLLSKPKLEV
ESYLNELGEF KVINS
