PET54_YEAST
ID PET54_YEAST Reviewed; 293 AA.
AC P10834; D6VV04;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein PET54;
DE AltName: Full=Petite colonies protein 54;
GN Name=PET54; OrderedLocusNames=YGR222W; ORFNames=G8527;
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 [GENOMIC DNA].
RX PubMed=2548921; DOI=10.1093/genetics/122.2.297;
RA Costanzo M.C., Seaver E.C., Fox T.D.;
RT "The PET54 gene of Saccharomyces cerevisiae: characterization of a nuclear
RT gene encoding a mitochondrial translational activator and subcellular
RT localization of its product.";
RL Genetics 122:297-305(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-16, AND SUBCELLULAR LOCATION.
RX PubMed=8389363; DOI=10.1016/s0021-9258(19)50261-7;
RA McMullin T.W., Fox T.D.;
RT "COX3 mRNA-specific translational activator proteins are associated with
RT the inner mitochondrial membrane in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:11737-11741(1993).
RN [6]
RP FUNCTION.
RX PubMed=2555177; DOI=10.1002/j.1460-2075.1989.tb08569.x;
RA Valencik M.L., Kloeckener-Gruissem B., Poyton R.O., McEwen J.E.;
RT "Disruption of the yeast nuclear PET54 gene blocks excision of
RT mitochondrial intron aI5 beta from pre-mRNA for cytochrome c oxidase
RT subunit I.";
RL EMBO J. 8:3899-3904(1989).
RN [7]
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).
CC -!- FUNCTION: Activator of specific mitochondrial mRNAs. PET54 is involved
CC in the excision of intron aI5-beta from pre-mRNA for cytochrome c
CC oxidase I (COX1) and plays a role in promoting the translation of COX3.
CC {ECO:0000269|PubMed:2555177}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:8389363}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8389363}.
CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X13427; CAA31784.1; -; Genomic_DNA.
DR EMBL; X87941; CAA61170.1; -; Genomic_DNA.
DR EMBL; Z73007; CAA97250.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08315.1; -; Genomic_DNA.
DR PIR; S05778; RGBY54.
DR RefSeq; NP_011738.3; NM_001181351.3.
DR AlphaFoldDB; P10834; -.
DR BioGRID; 33475; 68.
DR DIP; DIP-4485N; -.
DR STRING; 4932.YGR222W; -.
DR MaxQB; P10834; -.
DR PaxDb; P10834; -.
DR PRIDE; P10834; -.
DR EnsemblFungi; YGR222W_mRNA; YGR222W; YGR222W.
DR GeneID; 853137; -.
DR KEGG; sce:YGR222W; -.
DR SGD; S000003454; PET54.
DR VEuPathDB; FungiDB:YGR222W; -.
DR eggNOG; ENOG502RR5W; Eukaryota.
DR HOGENOM; CLU_1066355_0_0_1; -.
DR InParanoid; P10834; -.
DR OMA; KHCFKLY; -.
DR BioCyc; YEAST:G3O-30903-MON; -.
DR PRO; PR:P10834; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P10834; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:SGD.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:SGD.
DR GO; GO:0045182; F:translation regulator activity; IMP:SGD.
DR GO; GO:0000372; P:Group I intron splicing; IDA:SGD.
DR GO; GO:0090615; P:mitochondrial mRNA processing; IMP:SGD.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:SGD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR003954; RRM_dom_euk.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; mRNA processing; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..293
FT /note="Protein PET54"
FT /id="PRO_0000058319"
SQ SEQUENCE 293 AA; 34637 MW; D3B25F9BDFB0F341 CRC64;
MKASSKAIKL VLDHLKSTGR VLGSVESGNS ATISEKTASV NKQQQLQEKK PSVLQYRSYN
PYLVKEDFLS ILPENLYKKR GQFTNELDFQ LMKVRDPKYF QFKDQYYLFF NDYNSLTEYI
KLTKHSRINK IRVKMTPLAQ PLPTLLTKLQ RYSKNLYNAF RSSEQYFEGL NEKVDVSGEF
TTNQLRSILD SVEEIENKSV LVWNIPTKLR SHDILNYFWF YNIRSSFKIY WDDEMKRNLR
FISFENSHDA YRFKRNYHGL LAKELLTLSE KGDAADYSLE MDDSKILIEH LSE
