ID   PHB2_XENTR              Reviewed;         301 AA.
AC   A9UMS3; Q28HU7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Prohibitin-2;
GN   Name=phb2; ORFNames=TGas064h09.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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}. 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ83765.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CR760726; CAJ83765.1; ALT_INIT; mRNA.
DR   EMBL; BC157771; AAI57772.1; -; mRNA.
DR   RefSeq; NP_001016551.1; NM_001016551.2.
DR   RefSeq; XP_012822064.1; XM_012966610.2.
DR   AlphaFoldDB; A9UMS3; -.
DR   SMR; A9UMS3; -.
DR   PaxDb; A9UMS3; -.
DR   Ensembl; ENSXETT00000065480; ENSXETP00000058824; ENSXETG00000023919.
DR   GeneID; 549305; -.
DR   KEGG; xtr:549305; -.
DR   CTD; 11331; -.
DR   Xenbase; XB-GENE-5844763; phb2.
DR   eggNOG; KOG3090; Eukaryota.
DR   InParanoid; A9UMS3; -.
DR   OrthoDB; 1089994at2759; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000023919; Expressed in heart and 16 other tissues.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0016363; C:nuclear matrix; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; 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   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Cytoplasm; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleus; Receptor; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..301
FT                   /note="Prohibitin-2"
FT                   /id="PRO_0000328654"
FT   REGION          19..49
FT                   /note="Necessary for transcriptional repression"
FT                   /evidence="ECO:0000250"
FT   REGION          150..174
FT                   /note="Necessary for transcriptional repression"
FT                   /evidence="ECO:0000250"
FT   COILED          191..237
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   301 AA;  33461 MW;  46E4C3AD5BF90C90 CRC64;
     MAQNLKDFAG RLPAGPRGMG TAMKLLLGAG AVAYAVKESV FTVEGGHRAI FFNRIGGVQQ
     DTILAEGLHF RFPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNITLRVLS RPLASELPFM
     YQRLGLDYDE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSIILD
     DVAITELSFS REYTAAVESK QVAQQEAQRA QFLVEKAKQD QKQKIVQAEG EAAAAKMIGD
     ALSKNPGYLK LRRIRAAQSI AKTIASSQNR VYLNADSLVL NLQDDTFTRG SDSLVAKQTK
     K