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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
 
 
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