PHB2_YEAST
ID PHB2_YEAST Reviewed; 310 AA.
AC P50085; D6VV11;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Prohibitin-2;
GN Name=PHB2; OrderedLocusNames=YGR231C; ORFNames=G8561;
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=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 [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 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 [5]
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 [6]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
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).
CC -!- FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the
CC stabilization of newly synthesized mitochondrial proteins.
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 P50085; P40961: PHB1; NbExp=3; IntAct=EBI-23530, EBI-13360;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:15525670}; Single-pass type II 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 2850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Mitochondrial targeting of PHB2 is ensured by a
CC bipartite non-cleavable presequence at the N-terminus.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61181.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA97259.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X87941; CAA61181.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z73016; CAA97259.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006941; DAA08322.1; -; Genomic_DNA.
DR PIR; S57696; S57696.
DR RefSeq; NP_011747.2; NM_001181360.1.
DR AlphaFoldDB; P50085; -.
DR SMR; P50085; -.
DR BioGRID; 33483; 527.
DR ComplexPortal; CPX-1703; Prohibitin complex.
DR IntAct; P50085; 42.
DR MINT; P50085; -.
DR STRING; 4932.YGR231C; -.
DR iPTMnet; P50085; -.
DR MaxQB; P50085; -.
DR PaxDb; P50085; -.
DR PRIDE; P50085; -.
DR EnsemblFungi; YGR231C_mRNA; YGR231C; YGR231C.
DR GeneID; 853146; -.
DR KEGG; sce:YGR231C; -.
DR SGD; S000003463; PHB2.
DR VEuPathDB; FungiDB:YGR231C; -.
DR eggNOG; KOG3090; Eukaryota.
DR GeneTree; ENSGT00950000183070; -.
DR HOGENOM; CLU_047969_0_2_1; -.
DR InParanoid; P50085; -.
DR OMA; IKYTRLG; -.
DR BioCyc; YEAST:G3O-30909-MON; -.
DR PRO; PR:P50085; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P50085; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0000001; P:mitochondrion inheritance; 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; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Prohibitin-2"
FT /id="PRO_0000213888"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT COILED 212..253
FT /evidence="ECO:0000269|PubMed:15525670"
SQ SEQUENCE 310 AA; 34407 MW; 3526D9690F39B493 CRC64;
MNRSPGEFQR YAKAFQKQLS KVQQTGGRGQ VPSPRGAFAG LGGLLLLGGG ALFINNALFN
VDGGHRAIVY SRIHGVSSRI FNEGTHFIFP WLDTPIIYDV RAKPRNVASL TGTKDLQMVN
ITCRVLSRPD VVQLPTIYRT LGQDYDERVL PSIVNEVLKA VVAQFNASQL ITQREKVSRL
IRENLVRRAS KFNILLDDVS ITYMTFSPEF TNAVEAKQIA QQDAQRAAFV VDKARQEKQG
MVVRAQGEAK SAELIGEAIK KSRDYVELKR LDTARDIAKI LASSPNRVIL DNEALLLNTV
VDARIDGRGK
