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MSC3_YEAST
ID   MSC3_YEAST              Reviewed;         728 AA.
AC   Q05812; D6VYL9; Q7LIF4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Meiotic sister-chromatid recombination protein 3;
GN   Name=MSC3; OrderedLocusNames=YLR219W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   FUNCTION.
RX   PubMed=10511544; DOI=10.1093/genetics/153.2.621;
RA   Thompson D.A., Stahl F.W.;
RT   "Genetic control of recombination partner preference in yeast meiosis.
RT   Isolation and characterization of mutants elevated for meiotic unequal
RT   sister-chromatid recombination.";
RL   Genetics 153:621-641(1999).
RN   [4]
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-155 AND SER-363, AND
RP   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   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-64; SER-127; SER-151;
RP   SER-155; THR-646 AND SER-660, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- FUNCTION: May be involved in the control of meiotic sister-chromatid
CC       recombination. {ECO:0000269|PubMed:10511544}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095};
CC       Peripheral membrane protein {ECO:0000269|PubMed:14562095}. Note=Cell
CC       periphery.
CC   -!- MISCELLANEOUS: Present with 131 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U19027; AAB67420.1; -; Genomic_DNA.
DR   EMBL; U14913; AAB67423.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09535.1; -; Genomic_DNA.
DR   PIR; S48569; S48569.
DR   RefSeq; NP_013320.1; NM_001182106.1.
DR   AlphaFoldDB; Q05812; -.
DR   BioGRID; 31486; 87.
DR   DIP; DIP-6321N; -.
DR   IntAct; Q05812; 8.
DR   MINT; Q05812; -.
DR   STRING; 4932.YLR219W; -.
DR   iPTMnet; Q05812; -.
DR   MaxQB; Q05812; -.
DR   PaxDb; Q05812; -.
DR   PRIDE; Q05812; -.
DR   TopDownProteomics; Q05812; -.
DR   EnsemblFungi; YLR219W_mRNA; YLR219W; YLR219W.
DR   GeneID; 850916; -.
DR   KEGG; sce:YLR219W; -.
DR   SGD; S000004209; MSC3.
DR   VEuPathDB; FungiDB:YLR219W; -.
DR   eggNOG; ENOG502RZHH; Eukaryota.
DR   HOGENOM; CLU_380449_0_0_1; -.
DR   InParanoid; Q05812; -.
DR   OMA; INGYEYV; -.
DR   BioCyc; YEAST:G3O-32333-MON; -.
DR   PRO; PR:Q05812; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05812; protein.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
PE   1: Evidence at protein level;
KW   Cell membrane; DNA recombination; Meiosis; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..728
FT                   /note="Meiotic sister-chromatid recombination protein 3"
FT                   /id="PRO_0000096595"
FT   REGION          33..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..324
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         363
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         646
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   728 AA;  80530 MW;  1962D638DB602B71 CRC64;
     MVFGFTKRDR RVPDLSRYDY YYQNHEDYNK SPQLSAAAAS AASAASPDRT NYSRSHSLVS
     HAPSIPRQRS SVKSPGRRLS TSSAAPPTSR AAAKQYSQKT YSLRSQRSGE YHLHPPGYTT
     NGSRMNSMTS GANVRRNYGK NKSTAGNNND SRANSITVKT TQVTDPSGRT QSITKKTIRK
     INGYEYVETT TTTKNLVPLG DSQRHFDEFS ENYMLQDDDI LEEQASDNIH DIIEENETDN
     EKPYSPVSES HLQDDSELNV EKPDFPLGSY FHHKYSTDVM PLEEESSLSN FSDALDYIPP
     THQTSSKYIH NKRKQASTTR RKKRPPAVKN AEAEAKKPLT EAEMYLKALE VAKRNVYHTD
     AASDNASAPL GSNKSRKSRM GQKMTLRSSS DSPTATANLV KSNVEVQPKR FTSSFFSRNT
     KSAPHEVHNH SVSTHFKSNK AVDPVPEPKS ANTGLTDKEM YDQALKIAQA RYYNSHGIQP
     EAVDNSTTAA KPRQVGVSHL GSTGSIPPNE QHYLGDSEIP VQSEVHEYEP IPLQKTKTTG
     SSKNKFKTMF DKVLQFSQEN YGYQHKKEQG EQTPVTRNAE ESFPAASISE GVTTAKPSSN
     EGVMTNPVVT DSPSPLQQQI DSTTASSNGQ SQGNVPTSAV ASTTRTRSPE LQDNLKSSSS
     LLQDQTPQRQ EDATDPTTSS TNELSAAEPT MVTSTHATKT IQAQTQDPPT KHKKSSFFTK
     LFKKKSSR
 
 
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