PHB2_CHICK
ID PHB2_CHICK Reviewed; 301 AA.
AC Q5ZMN3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Prohibitin-2;
GN Name=PHB2; ORFNames=RCJMB04_1i23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(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}. 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; AJ719351; CAG31010.1; -; mRNA.
DR RefSeq; NP_001074354.1; NM_001080885.1.
DR AlphaFoldDB; Q5ZMN3; -.
DR SMR; Q5ZMN3; -.
DR BioGRID; 691830; 2.
DR STRING; 9031.ENSGALP00000023446; -.
DR PaxDb; Q5ZMN3; -.
DR GeneID; 771124; -.
DR KEGG; gga:771124; -.
DR CTD; 11331; -.
DR VEuPathDB; HostDB:geneid_771124; -.
DR eggNOG; KOG3090; Eukaryota.
DR InParanoid; Q5ZMN3; -.
DR OrthoDB; 1089994at2759; -.
DR PhylomeDB; Q5ZMN3; -.
DR PRO; PR:Q5ZMN3; -.
DR Proteomes; UP000000539; Unplaced.
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_0000328653"
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 190..237
FT /evidence="ECO:0000255"
SQ SEQUENCE 301 AA; 33337 MW; B43E2C8178F21BB4 CRC64;
MAQSLKDLAG RLPAGPRGVG TALKLLLGAG ALAYGVRESV FIVEGGQRAI FFNRIGGVQQ
DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLT RPNAAELPSM
YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD
DVAITELSFS REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QKQKIVQAEG EATAAKMLGE
ALSRNPGYIK LRKIRAAQNI SKTIAGSQNR VYLTADNLVL NLQDEGFTRG SDSLLLKQGK
K