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PHB1_YEAST
ID   PHB1_YEAST              Reviewed;         287 AA.
AC   P40961; D6VUR4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Prohibitin-1;
GN   Name=PHB1; Synonyms=PHB; OrderedLocusNames=YGR132C;
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;
RA   Franklin D.S., Stewart D.A., Owens G.A., Danner D.B., Jazwinski S.M.;
RT   "The yeast homolog of human prohibitin determines replicative life span.";
RL   Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, AND SUBUNIT.
RX   PubMed=10835343; DOI=10.1093/emboj/19.11.2444;
RA   Nijtmans L.G.J., de Jong L., Artal-Sanz M., Coates P.J., Berden J.A.,
RA   Back J.W., Muijsers A.O., van der Spek H., Grivell L.A.;
RT   "Prohibitins act as a membrane-bound chaperone for the stabilization of
RT   mitochondrial proteins.";
RL   EMBO J. 19:2444-2451(2000).
RN   [6]
RP   SUBUNIT.
RX   PubMed=12237468; DOI=10.1110/ps.0212602;
RA   Back J.W., Artal-Sanz M., De Jong L., De Koning L.J., Nijtmans L.G.J.,
RA   De Koster C.G., Grivell L.A., Van Der Spek H., Muijsers A.O.;
RT   "A structure for the yeast prohibitin complex: structure prediction and
RT   evidence from chemical crosslinking and mass spectrometry.";
RL   Protein Sci. 11:2471-2478(2002).
RN   [7]
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   [8]
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   [9]
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   [10]
RP   SUBCELLULAR LOCATION, SINGLE PARTICLE ELECTRON MICROSCOPY, AND COILED-COIL
RP   DOMAIN.
RX   PubMed=15525670; DOI=10.1091/mbc.e04-09-0807;
RA   Tatsuta T., Model K., Langer T.;
RT   "Formation of membrane-bound ring complexes by prohibitins in
RT   mitochondria.";
RL   Mol. Biol. Cell 16:248-259(2005).
RN   [11]
RP   MUTAGENESIS OF VAL-202; VAL-213 AND 217-GLU--GLU-221.
RX   PubMed=31522117; DOI=10.1016/j.isci.2019.08.056;
RA   Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O.,
RA   Tamada T., Koshiba T.;
RT   "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes:
RT   Insight into a Role of the Coiled-Coil Region.";
RL   IScience 19:1065-1078(2019).
CC   -!- FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the
CC       stabilization of newly synthesized mitochondrial proteins. Has an
CC       antiproliferative activity. Regulates replicative life span.
CC       {ECO:0000269|PubMed:10835343}.
CC   -!- SUBUNIT: The mitochondrial prohibitin complex consists of two subunits
CC       (PHB1 and PHB2), assembled into a membrane-associated ring-shaped
CC       supercomplex of approximately 1 mDa. {ECO:0000269|PubMed:10835343,
CC       ECO:0000269|PubMed:12237468}.
CC   -!- INTERACTION:
CC       P40961; P50085: PHB2; NbExp=3; IntAct=EBI-13360, EBI-23530;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:15525670}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:15525670}; Intermembrane side
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:15525670}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Present with 9690 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: PHB1 subunits are targeted to mitochondria by an
CC       unconventional non-cleavable targeting sequence present at their N-
CC       terminus.
CC   -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR   EMBL; U16737; AAA53144.1; -; Genomic_DNA.
DR   EMBL; Z72917; CAA97145.1; -; Genomic_DNA.
DR   EMBL; AY558096; AAS56422.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08225.1; -; Genomic_DNA.
DR   PIR; S64441; S64441.
DR   RefSeq; NP_011648.3; NM_001181261.3.
DR   AlphaFoldDB; P40961; -.
DR   SMR; P40961; -.
DR   BioGRID; 33380; 216.
DR   ComplexPortal; CPX-1703; Prohibitin complex.
DR   DIP; DIP-6653N; -.
DR   IntAct; P40961; 19.
DR   MINT; P40961; -.
DR   STRING; 4932.YGR132C; -.
DR   iPTMnet; P40961; -.
DR   MaxQB; P40961; -.
DR   PaxDb; P40961; -.
DR   PRIDE; P40961; -.
DR   TopDownProteomics; P40961; -.
DR   EnsemblFungi; YGR132C_mRNA; YGR132C; YGR132C.
DR   GeneID; 853033; -.
DR   KEGG; sce:YGR132C; -.
DR   SGD; S000003364; PHB1.
DR   VEuPathDB; FungiDB:YGR132C; -.
DR   eggNOG; KOG3083; Eukaryota.
DR   GeneTree; ENSGT00950000183070; -.
DR   HOGENOM; CLU_047969_0_0_1; -.
DR   InParanoid; P40961; -.
DR   OMA; QKMQFVL; -.
DR   BioCyc; YEAST:G3O-30838-MON; -.
DR   PRO; PR:P40961; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P40961; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0035632; C:mitochondrial prohibitin complex; IPI:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:SGD.
DR   GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR   GO; GO:0070584; P:mitochondrion morphogenesis; IMP:SGD.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IDA:SGD.
DR   GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR   CDD; cd03401; SPFH_prohibitin; 1.
DR   Gene3D; 3.30.479.30; -; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; PTHR23222; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; SSF117892; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome.
FT   CHAIN           1..287
FT                   /note="Prohibitin-1"
FT                   /id="PRO_0000213883"
FT   REGION          264..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          180..224
FT                   /evidence="ECO:0000269|PubMed:15525670"
FT   MUTAGEN         202
FT                   /note="V->P: Abolishes regulation of cell growth."
FT                   /evidence="ECO:0000269|PubMed:31522117"
FT   MUTAGEN         213
FT                   /note="V->P: Abolishes regulation of cell growth."
FT                   /evidence="ECO:0000269|PubMed:31522117"
FT   MUTAGEN         217..221
FT                   /note="EGEAE->KGKAK: Abolishes regulation of cell growth."
FT                   /evidence="ECO:0000269|PubMed:31522117"
FT   CONFLICT        43
FT                   /note="R -> K (in Ref. 1; AAA53144)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="S -> G (in Ref. 1; AAA53144)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="F -> C (in Ref. 1; AAA53144)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  31427 MW;  BB9E629315364A6B CRC64;
     MSNSAKLIDV ITKVALPIGI IASGIQYSMY DVKGGSRGVI FDRINGVKQQ VVGEGTHFLV
     PWLQKAIIYD VRTKPKSIAT NTGTKDLQMV SLTLRVLHRP EVLQLPAIYQ NLGLDYDERV
     LPSIGNEVLK SIVAQFDAAE LITQREIISQ KIRKELSTRA NEFGIKLEDV SITHMTFGPE
     FTKAVEQKQI AQQDAERAKF LVEKAEQERQ ASVIRAEGEA ESAEFISKAL AKVGDGLLLI
     RRLEASKDIA QTLANSSNVV YLPSQHSGGG NSESSGSPNS LLLNIGR
 
 
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