NPR3_YEAST
ID NPR3_YEAST Reviewed; 1146 AA.
AC P38742; D3DKU5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Nitrogen permease regulator 3;
DE AltName: Full=Required for meiotic nuclear division protein 11;
DE Flags: Precursor;
GN Name=NPR3; Synonyms=RMD11; OrderedLocusNames=YHL023C;
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 FUNCTION.
RX PubMed=12586695; DOI=10.1093/genetics/163.1.47;
RA Enyenihi A.H., Saunders W.S.;
RT "Large-scale functional genomic analysis of sporulation and meiosis in
RT Saccharomyces cerevisiae.";
RL Genetics 163:47-54(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, 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 [8]
RP FUNCTION, AND INTERACTION WITH NPR2.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, 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 [10]
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).
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. Mediates
CC inactivation of the TORC1 complex in response to amino acid starvation.
CC Required for meiotic nuclear division. {ECO:0000269|PubMed:12586695,
CC ECO:0000269|PubMed:19521502, ECO:0000269|PubMed:21454883}.
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 NPR2. {ECO:0000269|PubMed:21454883}.
CC -!- INTERACTION:
CC P38742; P39923: NPR2; NbExp=4; IntAct=EBI-24336, EBI-12212;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:21454883};
CC Peripheral membrane protein {ECO:0000269|PubMed:21454883}.
CC -!- SIMILARITY: Belongs to the NPR3 family. {ECO:0000305}.
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DR EMBL; U11582; AAB65076.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06662.1; -; Genomic_DNA.
DR PIR; S46837; S46837.
DR RefSeq; NP_011840.1; NM_001179103.1.
DR AlphaFoldDB; P38742; -.
DR BioGRID; 36399; 381.
DR ComplexPortal; CPX-3231; SEA complex.
DR DIP; DIP-2087N; -.
DR IntAct; P38742; 21.
DR MINT; P38742; -.
DR STRING; 4932.YHL023C; -.
DR iPTMnet; P38742; -.
DR MaxQB; P38742; -.
DR PaxDb; P38742; -.
DR PRIDE; P38742; -.
DR EnsemblFungi; YHL023C_mRNA; YHL023C; YHL023C.
DR GeneID; 856362; -.
DR KEGG; sce:YHL023C; -.
DR SGD; S000001015; NPR3.
DR VEuPathDB; FungiDB:YHL023C; -.
DR eggNOG; ENOG502QW35; Eukaryota.
DR GeneTree; ENSGT00390000015916; -.
DR HOGENOM; CLU_014314_0_0_1; -.
DR InParanoid; P38742; -.
DR OMA; ARTDYVW; -.
DR BioCyc; YEAST:G3O-31043-MON; -.
DR PRO; PR:P38742; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38742; 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; IC:ComplexPortal.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IGI: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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:SGD.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR GO; GO:0038202; P:TORC1 signaling; IBA:GO_Central.
DR InterPro; IPR005365; Npr3.
DR PANTHER; PTHR13153; PTHR13153; 1.
DR Pfam; PF03666; NPR3; 1.
PE 1: Evidence at protein level;
KW Meiosis; Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Signal; Transport; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1146
FT /note="Nitrogen permease regulator 3"
FT /id="PRO_0000202882"
FT REGION 90..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 1146 AA; 129973 MW; 8580F0C58982D51E CRC64;
MDECLPNSCL LGVHLVISTH SGPQIVYHYP PSNTAFLTNN PTKHQHLYGN HANLNKNTST
NKEEKLFNSG STKTASQIAL NESAKSYNTA ITPSMTNTNT NNVTLPPTRS HANTVGSQSS
IPAATNGVGY RKTDIEDTSR TFQYQETESE TSSSGLSDSE LSTDYLDISS DSFSISSSLS
SSSLSSSPSS SSSSSPPQDG LSRTNSSFQS TDSMSPTSPQ MIMENDSISV AESYLDSGTN
NKSRAASKRS QNFFHKLSTK KSTDSKTHSP VRKLKSKPSQ STKKGNKLLK NTSNETDGNA
FTGSCSISSK KSLSSTGEHN QELRNSSLND TPGQSPHHYH HRYHHYHKNA ATSQRNSHTQ
YDVEEEDMEV SAMLQDGKIS MNEIFFEEEN FQDINKILEF DNDFVAEFCS PEREMCNTRF
EFTVDNFCFL GLPIHVDSQG RWRKSKHKNK TRSKRSSSTT TNISRKKSIA SKISSLSENT
LKKVNSGEAD TVYDSNIGHE ASTDTPNLRI NTDVSGNEFE REKEDLGKNM NMFHVCFVMN
PHLIEYNKRI DDMYQFVVTR LSLLLRYVQS KTSYISSECH IILKEKERVL KHSKTYQSIR
GAGNKGKYLY QRILAKSSLA RALTECVDKI QRNEIACLEI NDDKVISLQI PIQNEFEKMP
NFKLQPVLRG SYLTSILNMK FLEKSSLRIE SQNRQNDQAQ FSDTNNNIYR FGNNINSTGH
CGAANVDDGD DNESNYYCDD NDDLLNYALL LLDEPNNIIS SLETFSYQDD IGTIILKHLV
RNIQPNIPLR SYRYLITDLL DNPSSLDDLT TETNSLESSI LRSCALHLMY WRHARIVIPL
SSKYTYIVSP LAPIQGYTID DYKSTSQNDG NVKKMDDREN NKSGSDRVPL IYQNSMLFRS
KFPSLPSLPI FLSLLSTDKP QAYSNIIPSR EHKPVYLNAL AWLIQYGYVT QLLTFINIRV
DKHIKMAVDE DLEKEGFRKT NTARRPSMDY KKTDKKLDDE DGQSRDANAS EACSGKNEGM
QSNDNNKDVD EKDNENDSRV DDRDDNEIAI ADEEEILHFE YDDPEMQHDY TIILEPERAT
AIEKRWLYRC IYGQPSDIQI LFNKLLKYFN GKVPMELVII KEEISRHDLK KLLNALDKYL
IEIHHW
