PHB2_DICDI
ID PHB2_DICDI Reviewed; 293 AA.
AC Q54Q31;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Prohibitin-2;
GN Name=phbB; ORFNames=DDB_G0284117;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Protein with pleiotropic attributes mediated in a cell-
CC compartment- and tissue-specific manner, which include the plasma
CC membrane-associated cell signaling functions, mitochondrial chaperone,
CC and transcriptional co-regulator of transcription factors and sex
CC steroid hormones in the nucleus. {ECO:0000250|UniProtKB:Q99623}.
CC -!- FUNCTION: In the mitochondria, together with PHB, forms large ring
CC complexes (prohibitin complexes) in the inner mitochondrial membrane
CC (IMM) and functions as chaperone protein that stabilizes mitochondrial
CC respiratory enzymes and maintains mitochondrial integrity in the IMM,
CC which is required for mitochondrial morphogenesis, neuronal survival,
CC and normal lifespan. {ECO:0000250|UniProtKB:Q99623}.
CC -!- FUNCTION: In the nucleus, serves as transcriptional co-regulator.
CC {ECO:0000250|UniProtKB:Q99623}.
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:0000250|UniProtKB:Q99623}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O35129}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P50093}; Intermembrane side
CC {ECO:0000250|UniProtKB:P50093}. Cytoplasm
CC {ECO:0000250|UniProtKB:O35129}. Nucleus {ECO:0000250|UniProtKB:O35129}.
CC Cell membrane {ECO:0000250|UniProtKB:Q99623}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR EMBL; AAFI02000063; EAL65399.1; -; Genomic_DNA.
DR RefSeq; XP_638766.1; XM_633674.1.
DR AlphaFoldDB; Q54Q31; -.
DR SMR; Q54Q31; -.
DR STRING; 44689.DDB0232062; -.
DR PaxDb; Q54Q31; -.
DR EnsemblProtists; EAL65399; EAL65399; DDB_G0284117.
DR GeneID; 8624437; -.
DR KEGG; ddi:DDB_G0284117; -.
DR dictyBase; DDB_G0284117; phbB.
DR eggNOG; KOG3090; Eukaryota.
DR HOGENOM; CLU_047969_0_2_1; -.
DR InParanoid; Q54Q31; -.
DR OMA; IKYTRLG; -.
DR PhylomeDB; Q54Q31; -.
DR PRO; PR:Q54Q31; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0035632; C:mitochondrial prohibitin complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cell membrane; Coiled coil; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleus; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..293
FT /note="Prohibitin-2"
FT /id="PRO_0000327659"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT COILED 190..235
FT /evidence="ECO:0000255"
SQ SEQUENCE 293 AA; 32845 MW; C5E43B154D8E7B6B CRC64;
MNNKKFQVNF NNIPKLPKGS FGGGFGLLAL GGVGLLALSS LVNVEGGHRA IVFNRFVGIK
NKVYNEGTHF IVPWFERAEI YDVRAKPRSI SSLTGSKDLQ MVNITIRVLS KPKVSQLPAI
YRTLGKDYDE RVLPSIVNEI LKSIVAQFNA SQLITQREQV SRLIFKRLVD RAKDFNIELD
DVSITHLNFG REYAAAIEAK QVAQQEAERA RFLVEKALQD KRSIIVKAEG EAQSAQLIND
AIKQSPYLVQ LRTLEASKEI AHILSKSPNK LYISNETLLL NGFDLNNNQQ PKK
