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MRX9_YEAST
ID   MRX9_YEAST              Reviewed;         420 AA.
AC   Q07349; D6VRW5; Q05321; Q05435; Q7LHC7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=MIOREX complex component 9 {ECO:0000305|PubMed:25683707};
DE   AltName: Full=Mitochondrial organization of gene expression protein 9 {ECO:0000303|PubMed:25683707};
GN   Name=MRX9 {ECO:0000303|PubMed:25683707};
GN   OrderedLocusNames=YDL027C {ECO:0000312|SGD:S000002185}; ORFNames=D2800;
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=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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-264.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9046088;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<65::aid-yea50>3.0.co;2-t;
RA   Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
RT   "The sequence of a 36.7 kb segment on the left arm of chromosome IV from
RT   Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames
RT   (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1
RT   and 11 new ORFs.";
RL   Yeast 13:65-71(1997).
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [7]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=25683707; DOI=10.1016/j.celrep.2015.01.012;
RA   Kehrein K., Schilling R., Moller-Hergt B.V., Wurm C.A., Jakobs S.,
RA   Lamkemeyer T., Langer T., Ott M.;
RT   "Organization of mitochondrial gene expression in two distinct ribosome-
RT   containing assemblies.";
RL   Cell Rep. 10:843-853(2015).
CC   -!- FUNCTION: Component of MIOREX complexes, large expressome-like
CC       assemblies of ribosomes with factors involved in all the steps of post-
CC       transcriptional gene expression. {ECO:0000269|PubMed:25683707}.
CC   -!- SUBUNIT: Associates with the mitochondrial ribosome.
CC       {ECO:0000269|PubMed:25683707}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:16823961}. Mitochondrion membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z48432; CAA88332.1; -; Genomic_DNA.
DR   EMBL; Z74075; CAA98585.1; -; Genomic_DNA.
DR   EMBL; Z71781; CAA96462.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11825.1; -; Genomic_DNA.
DR   PIR; S67559; S67559.
DR   RefSeq; NP_010257.1; NM_001180086.1.
DR   AlphaFoldDB; Q07349; -.
DR   BioGRID; 32029; 43.
DR   IntAct; Q07349; 1.
DR   MINT; Q07349; -.
DR   STRING; 4932.YDL027C; -.
DR   MaxQB; Q07349; -.
DR   PaxDb; Q07349; -.
DR   PRIDE; Q07349; -.
DR   EnsemblFungi; YDL027C_mRNA; YDL027C; YDL027C.
DR   GeneID; 851535; -.
DR   KEGG; sce:YDL027C; -.
DR   SGD; S000002185; MRX9.
DR   VEuPathDB; FungiDB:YDL027C; -.
DR   eggNOG; ENOG502S11T; Eukaryota.
DR   HOGENOM; CLU_659145_0_0_1; -.
DR   InParanoid; Q07349; -.
DR   OMA; RTNWINT; -.
DR   BioCyc; YEAST:G3O-29453-MON; -.
DR   PRO; PR:Q07349; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q07349; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..420
FT                   /note="MIOREX complex component 9"
FT                   /id="PRO_0000202592"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   420 AA;  48312 MW;  A88F23B7F5933FAE CRC64;
     MFKVPVGLAS RTRELMNSVT LNSLNNGKGF NMYLPGILRA FPKPVPSAIT SPAIPKYRGE
     SFQFRKLSCI SSNYCSTTHQ FLSSLKSSTS RLVGKRAFHS SRRAEIKFIF SSKSPKNGNK
     PFVKVYKVSP FFIIFATASI FTFILTSTIV VIPLIFHFFF PLLIMFFFFK QFKKWQKNIF
     YKDVLTSLPK TKLKITLPTM RSLQLQPMVQ SWKEISSRMG IPNEFAKGLN VDLVKQEETR
     KQFLSFLQKR VLESFTKNEL GIRSYFLGDS VEKWIKESYD LELDIDNCRS ELRKFQTFIF
     SSVRYKLYLD SMKNLPLNPS KKLEGKKHIA DVYVIILDES FPAIMFNGGA YSKADFFKIL
     QESETSNSSK TLNTIIAIKS VNTLLSKHFV ITTNGDSGEF FSKYNISKIN DKNTEYTLKE
 
 
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