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BOL2_YEAST
ID   BOL2_YEAST              Reviewed;         120 AA.
AC   P53082; D6VVB5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=BolA-like protein 2;
DE   AltName: Full=Altered inheritance rate of mitochondria protein 15;
DE   AltName: Full=Fe repressor of activation 2;
GN   Name=BOL2; Synonyms=AIM15, FRA2; OrderedLocusNames=YGL220W;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
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   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FRA1; GRX3 AND GRX4.
RX   PubMed=18281282; DOI=10.1074/jbc.m801160200;
RA   Kumanovics A., Chen O.S., Li L., Bagley D., Adkins E.M., Lin H.,
RA   Dingra N.N., Outten C.E., Keller G., Winge D., Ward D.M., Kaplan J.;
RT   "Identification of FRA1 and FRA2 as genes involved in regulating the yeast
RT   iron regulon in response to decreased mitochondrial iron-sulfur cluster
RT   synthesis.";
RL   J. Biol. Chem. 283:10276-10286(2008).
RN   [8]
RP   FUNCTION.
RX   PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA   Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA   Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA   Troyanskaya O.G., Caudy A.A.;
RT   "Computationally driven, quantitative experiments discover genes required
RT   for mitochondrial biogenesis.";
RL   PLoS Genet. 5:E1000407-E1000407(2009).
CC   -!- FUNCTION: Involved in the regulation of the iron regulon in response to
CC       decreased mitochondrial iron-sulfur cluster synthesis. May be involved
CC       in mitochondrial organization and biogenesis.
CC       {ECO:0000269|PubMed:18281282, ECO:0000269|PubMed:19300474}.
CC   -!- SUBUNIT: Interacts with FRA1, GRX3 and GRX4.
CC       {ECO:0000269|PubMed:18281282}.
CC   -!- INTERACTION:
CC       P53082; Q03835: GRX3; NbExp=2; IntAct=EBI-24159, EBI-22178;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- MISCELLANEOUS: Present with 2050 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the BolA/IbaG family. {ECO:0000305}.
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DR   EMBL; Z72742; CAA96936.1; -; Genomic_DNA.
DR   EMBL; AY558390; AAS56716.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07899.1; -; Genomic_DNA.
DR   PIR; S64242; S64242.
DR   RefSeq; NP_011295.1; NM_001181085.1.
DR   PDB; 5Y4B; NMR; -; A=36-120.
DR   PDBsum; 5Y4B; -.
DR   AlphaFoldDB; P53082; -.
DR   SMR; P53082; -.
DR   BioGRID; 33039; 55.
DR   ComplexPortal; CPX-6864; BOL2-GRX3 iron-sulfur cluster assembly complex.
DR   ComplexPortal; CPX-6865; BOL2-GRX4 iron-sulfur cluster assembly complex.
DR   DIP; DIP-2048N; -.
DR   IntAct; P53082; 7.
DR   MINT; P53082; -.
DR   STRING; 4932.YGL220W; -.
DR   MaxQB; P53082; -.
DR   PaxDb; P53082; -.
DR   PRIDE; P53082; -.
DR   EnsemblFungi; YGL220W_mRNA; YGL220W; YGL220W.
DR   GeneID; 852652; -.
DR   KEGG; sce:YGL220W; -.
DR   SGD; S000003188; BOL2.
DR   VEuPathDB; FungiDB:YGL220W; -.
DR   eggNOG; KOG3348; Eukaryota.
DR   GeneTree; ENSGT00510000047760; -.
DR   HOGENOM; CLU_109462_4_0_1; -.
DR   InParanoid; P53082; -.
DR   OMA; VHAFSQK; -.
DR   BioCyc; YEAST:G3O-30694-MON; -.
DR   PRO; PR:P53082; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53082; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:SGD.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR   GO; GO:0034396; P:negative regulation of transcription from RNA polymerase II promoter in response to iron; IMP:SGD.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IEA:InterPro.
DR   InterPro; IPR045115; BOL2.
DR   InterPro; IPR002634; BolA.
DR   InterPro; IPR036065; BolA-like_sf.
DR   PANTHER; PTHR12735; PTHR12735; 1.
DR   Pfam; PF01722; BolA; 1.
DR   PIRSF; PIRSF003113; BolA; 1.
DR   SUPFAM; SSF82657; SSF82657; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..120
FT                   /note="BolA-like protein 2"
FT                   /id="PRO_0000201232"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   STRAND          55..60
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   HELIX           84..94
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   HELIX           96..101
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:5Y4B"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:5Y4B"
SQ   SEQUENCE   120 AA;  14102 MW;  9111F95A839235A8 CRC64;
     MTGERIEKVK INDEFAKSHF LTTQWRETKR QRHYKMPVTE QGLRERIESA IPQVYHIIVT
     DLSYGCGQSF DIVVVSDFFQ GKSKLMRSRA VNKAVKEELQ EIHAFSCKCY TEEEWSKIVV
 
 
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