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RL4P_YEAST
ID   RL4P_YEAST              Reviewed;         286 AA.
AC   P51998; D6VZE9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=54S ribosomal protein YmL6, mitochondrial;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL4m {ECO:0000303|PubMed:24675956};
DE   Flags: Precursor;
GN   Name=YML6; OrderedLocusNames=YML025C;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   PROTEIN SEQUENCE OF 27-53, AND SUBUNIT.
RC   STRAIN=07173;
RX   PubMed=2060626; DOI=10.1016/0014-5793(91)80759-v;
RA   Grohmann L., Graack H.-R., Kruft V., Choli T., Goldschmidt-Reisin S.,
RA   Kitakawa M.;
RT   "Extended N-terminal sequencing of proteins of the large ribosomal subunit
RT   from yeast mitochondria.";
RL   FEBS Lett. 284:51-56(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 110-121; 147-156; 241-249 AND 279-286, AND SUBUNIT.
RC   STRAIN=07173;
RX   PubMed=9151978; DOI=10.1111/j.1432-1033.1997.t01-2-00449.x;
RA   Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S., Herfurth E.,
RA   Wittmann-Liebold B., Nishimura T., Isono K.;
RT   "Identification and characterization of the genes for mitochondrial
RT   ribosomal proteins of Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 245:449-456(1997).
RN   [5]
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   [6]
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   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25609543; DOI=10.1038/ncomms7019;
RA   Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT   "Organization of the mitochondrial translation machinery studied in situ by
RT   cryoelectron tomography.";
RL   Nat. Commun. 6:6019-6019(2015).
RN   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND SUBUNIT.
RX   PubMed=24675956; DOI=10.1126/science.1249410;
RA   Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F.,
RA   Murshudov G., Scheres S.H., Ramakrishnan V.;
RT   "Structure of the yeast mitochondrial large ribosomal subunit.";
RL   Science 343:1485-1489(2014).
CC   -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC       dedicated translation machinery responsible for the synthesis of
CC       mitochondrial genome-encoded proteins, including at least some of the
CC       essential transmembrane subunits of the mitochondrial respiratory
CC       chain. The mitoribosomes are attached to the mitochondrial inner
CC       membrane and translation products are cotranslationally integrated into
CC       the membrane. {ECO:0000305|PubMed:24675956,
CC       ECO:0000305|PubMed:25609543}.
CC   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
CC       and a large (54S) subunit. The 37S small subunit contains a 15S
CC       ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
CC       subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
CC       {ECO:0000269|PubMed:2060626, ECO:0000269|PubMed:24675956,
CC       ECO:0000269|PubMed:9151978}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the
CC       mitochondrial inner membrane and spatially aligned with the membrane
CC       insertion machinery through two distinct membrane contact sites, formed
CC       by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein
CC       MBA1. {ECO:0000269|PubMed:25609543}.
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000305}.
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DR   EMBL; Z46659; CAA86630.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09873.1; -; Genomic_DNA.
DR   PIR; S50887; S50887.
DR   RefSeq; NP_013687.1; NM_001182383.1.
DR   PDB; 3J6B; EM; 3.20 A; D=1-286.
DR   PDB; 5MRC; EM; 3.25 A; D=29-280.
DR   PDB; 5MRE; EM; 3.75 A; D=29-280.
DR   PDB; 5MRF; EM; 4.97 A; D=29-280.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P51998; -.
DR   SMR; P51998; -.
DR   BioGRID; 35144; 74.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-6670N; -.
DR   IntAct; P51998; 41.
DR   MINT; P51998; -.
DR   STRING; 4932.YML025C; -.
DR   MaxQB; P51998; -.
DR   PaxDb; P51998; -.
DR   PRIDE; P51998; -.
DR   EnsemblFungi; YML025C_mRNA; YML025C; YML025C.
DR   GeneID; 854983; -.
DR   KEGG; sce:YML025C; -.
DR   SGD; S000004487; YML6.
DR   VEuPathDB; FungiDB:YML025C; -.
DR   eggNOG; KOG1624; Eukaryota.
DR   GeneTree; ENSGT00390000014512; -.
DR   HOGENOM; CLU_041575_4_2_1; -.
DR   InParanoid; P51998; -.
DR   OMA; KTRYDVH; -.
DR   BioCyc; YEAST:G3O-32627-MON; -.
DR   PRO; PR:P51998; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P51998; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR   Gene3D; 3.40.1370.10; -; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR013005; Ribosomal_uL4/L1e.
DR   PANTHER; PTHR10746; PTHR10746; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2060626"
FT   CHAIN           27..286
FT                   /note="54S ribosomal protein YmL6, mitochondrial"
FT                   /id="PRO_0000030541"
FT   REGION          85..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        30
FT                   /note="N -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="A -> I (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="E -> P (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="S -> K (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="L -> F (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="E -> C (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  31970 MW;  50528B571B0411F2 CRC64;
     MTIKRNLVKT LQSIRYQATT ATAHAESTLN PLPNAAIPPK YALVTVRSFP SLEPLTFVPV
     PTSTVAAPLR RDILWRAVVY ENDNRRVGAS NPPGRSENGF SRRKLMPQKG SGRARVGDAN
     SPTRHNGGRA LARTAPNDYT TELPSKVYSM AFNNALSHQY KSGKLFVIGG EKVDLISPTP
     ELDLNRLDLV NTNTVEGKEI FEGEVIFRKF LEEFQLKGKR LLFITDKTRE GLIKSSDPYK
     QKVDVIQKEL VEVNDILRAQ AVFIELEALE YLAMAHQKEI LHSVSN
 
 
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