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MSN5_YEAST
ID   MSN5_YEAST              Reviewed;        1224 AA.
AC   P52918; D6VSW7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Protein MSN5;
GN   Name=MSN5; OrderedLocusNames=YDR335W; ORFNames=D9651.5;
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.
RC   STRAIN=ATCC 204508 / S288c;
RA   Alepuz P.M., Estruch F.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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   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   INTERACTION WITH CEX1.
RX   PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
RA   McGuire A.T., Mangroo D.;
RT   "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae
RT   nuclear tRNA export machinery.";
RL   EMBO J. 26:288-300(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- SUBUNIT: Interacts with CEX1. {ECO:0000269|PubMed:17203074}.
CC   -!- INTERACTION:
CC       P52918; P07270: PHO4; NbExp=2; IntAct=EBI-11420, EBI-13378;
CC   -!- MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X93302; CAA63705.1; -; mRNA.
DR   EMBL; U51032; AAB64771.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12177.1; -; Genomic_DNA.
DR   PIR; S70100; S70100.
DR   RefSeq; NP_010622.1; NM_001180643.1.
DR   AlphaFoldDB; P52918; -.
DR   SMR; P52918; -.
DR   BioGRID; 32392; 421.
DR   DIP; DIP-1459N; -.
DR   IntAct; P52918; 29.
DR   MINT; P52918; -.
DR   STRING; 4932.YDR335W; -.
DR   TCDB; 9.A.50.1.1; the nuclear t-rna exporter (trna-e) family.
DR   CarbonylDB; P52918; -.
DR   iPTMnet; P52918; -.
DR   MaxQB; P52918; -.
DR   PaxDb; P52918; -.
DR   PRIDE; P52918; -.
DR   EnsemblFungi; YDR335W_mRNA; YDR335W; YDR335W.
DR   GeneID; 851935; -.
DR   KEGG; sce:YDR335W; -.
DR   SGD; S000002743; MSN5.
DR   VEuPathDB; FungiDB:YDR335W; -.
DR   eggNOG; KOG2020; Eukaryota.
DR   GeneTree; ENSGT00940000153408; -.
DR   HOGENOM; CLU_003712_0_0_1; -.
DR   InParanoid; P52918; -.
DR   OMA; WPDDPDR; -.
DR   BioCyc; YEAST:G3O-29891-MON; -.
DR   PRO; PR:P52918; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P52918; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0042565; C:RNA nuclear export complex; IBA:GO_Central.
DR   GO; GO:0005049; F:nuclear export signal receptor activity; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006611; P:protein export from nucleus; IDA:SGD.
DR   GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0071528; P:tRNA re-export from nucleus; IGI:SGD.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045478; Exportin-5_C.
DR   InterPro; IPR045065; XPO1/5.
DR   InterPro; IPR040018; XPO5.
DR   PANTHER; PTHR11223; PTHR11223; 1.
DR   PANTHER; PTHR11223:SF3; PTHR11223:SF3; 1.
DR   Pfam; PF19273; Exportin-5; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..1224
FT                   /note="Protein MSN5"
FT                   /id="PRO_0000096599"
FT   REGION          1200..1224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        886
FT                   /note="D -> G (in Ref. 1; CAA63705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1011
FT                   /note="S -> R (in Ref. 1; CAA63705)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1224 AA;  142118 MW;  C47A6767CBA44486 CRC64;
     MDSTGASQIV SALDVIYSPK SNNSQRQEAQ KFLDEVKLCS ESPFWGYEIA LQNPTNSILK
     YFGLGLLDHA VKKNWNDYDE GKRVALRKWV MELNFGVQDY DTRYIKEKLA TLWVEVAKRT
     WGEALKQTNP TEEQLLTSWV DMDNNLFELW NINQSSRELA LIIFRILFED VFLLDDLIVL
     KRMTVIQPLC VMIVCPIEVF AIKYKFSDKW TKFKANEEGW FSVWIPELNN ALQQNNSEYI
     IRLLETLKTC LNWPLTEVIV RNDVLSSLLT CLSSNIPRAQ SMALDSIHIL LTRPYSNESH
     YQMTIDRVFD NMDLLDSVYE SLLFDPTDDI DETKYPIIKK FVDMISCLYV CVPKIKETNG
     QIQKYFKLVL KTTYNPSLIV SGLTLDLWCT CLRNDEYLPK LEKYVIPDLL QFAADALVYY
     EQIDGHISKK FAEIDFQSKS EFQTFCSTYR KRIRDIIRLI SCVELDLTYD WLNNRLNNYF
     SSPFGQQVLS STFLDHKLEP YLGALSQYMI VECFINGCIR WKIWYPTGDD YDEKLDSILQ
     KLEILSNQLI ALNLREPLLL KKQIQNFALF LTMLKDNVLF TLLEKIITSA TMDYPEINLE
     ERGAESDAVR DLRYACGIEL NRMALLMPES LKKIYPDLES VIARIMPNLS YHEKISFKSF
     LLIIVLKSSL DMKEERFAAI VDPELLAWSD KTTVVGLSDL HWFMERLGIV QIAEYFQRRD
     IDENSDLLSI PIDDEGKELK SELTKRWQSL FPVRATRMFI HYSMQSIKTD EEFKMLQDLW
     RPRIVPILPY ITRLLYQLQS YHDPDNWKGL PTVVQSFVKY STIERFWEAG ASNKSKDEFI
     DEHMKAMQTL RDFADSVGHI IRYTREYTLL VLSAISSLGS VFYLLDESPD LLLNSIAIFK
     PGSNEISPGV STHGWKHIMN IAIRPILKGC PKDCLGKFMP AFLPKLFEIL DLLLCQKWSS
     HMNDMDMNPV PTDDDQMTEE ILEENLLRQL TTVVVRIVID CVGQGNANPN SAKSRLNNHQ
     MEMRKIIFND LNTLAPFLKL LNHLISFKDT KCSFNSILVM KCCLTSVLNQ NNTVDEYFTF
     EVMKNLLLNV LCNSAFKDSF HEALYAFTVI FLTLCKEYPS ARAFLFEISN GYNIDELYRN
     LRSVDEYKTQ RALMIDFIDW VKSTSGKEDG NVDHAGDERK RQEKREAILK KANERLIKKN
     KENGDMLDDP NIEDGAVGNL FDDN
 
 
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