PHB2_BOVIN
ID PHB2_BOVIN Reviewed; 299 AA.
AC Q2HJ97;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Prohibitin-2;
GN Name=PHB2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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:O35129}.
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. The prohibitin complex, with DNAJC19, regulates
CC cardiolipin remodeling and the protein turnover of OMA1 in a
CC cardiolipin-binding manner.Also regulates cytochrome-c oxidase assembly
CC (COX) and mitochondrial respiration. Binding to sphingoid 1-phosphate
CC (SPP) modulates its regulator activity. Has a key role of mitophagy
CC receptor involved in targeting mitochondria for autophagic degradation.
CC Involved in mitochondrial-mediated antiviral innate immunity, activates
CC DDX58/RIG-I-mediated signal transduction and production of IFNB1 and
CC pro-inflammatory cytokine IL6. {ECO:0000250|UniProtKB:O35129}.
CC -!- FUNCTION: In the nucleus, serves as transcriptional co-regulator. Acts
CC as a mediator of transcriptional repression by nuclear hormone
CC receptors via recruitment of histone deacetylases. Functions as an
CC estrogen receptor (ER)-selective coregulator that potentiates the
CC inhibitory activities of antiestrogens and represses the activity of
CC estrogens. Competes with NCOA1 for modulation of ER transcriptional
CC activity. {ECO:0000250|UniProtKB:O35129}.
CC -!- FUNCTION: In the plasma membrane, is involved in IGFBP6-induced cell
CC migration (By similarity). Cooperates with CD86 to mediate CD86-
CC signaling in B lymphocytes that regulates the level of IgG1 produced
CC through the activation of distal signaling intermediates. Upon CD40
CC engagement, required to activate NF-kappa-B signaling pathway via
CC phospholipase C and protein kinase C activation (By similarity).
CC {ECO:0000250|UniProtKB:O35129, 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. Interacts with ESR1, HDAC1 and
CC HDAC5 (By similarity). Interacts with ZNF703. Interacts with STOML2.
CC Interacts with ARFGEF3 (By similarity). Interacts with SPHK2. Interacts
CC with COX4I1; the interaction associates PHB2 with COX (By similarity).
CC Interacts with MAP1LC3B (membrane-bound form LC3-II); the interaction
CC is direct and upon mitochondrial depolarization and proteasome-
CC dependent outer membrane rupture. Interacts with IGFBP6 (via C-terminal
CC domain). Interacts with CLPB (By similarity). Interacts with CD86 (via
CC cytoplasmic domain); the interactions increases after priming with
CC CD40. Interacts with AFG3L2. Interacts with DNAJC19 (By similarity).
CC {ECO:0000250|UniProtKB:O35129, 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 -!- DOMAIN: LC3-interaction region (LIR) is required for interaction with
CC MAP1LC3B/LC3-II and for Parkin-mediated mitophagy.
CC {ECO:0000250|UniProtKB:Q99623}.
CC -!- PTM: Phosphorylated. Tyrosine phosphorylation is indirectly stimulated
CC by IGFBP6. {ECO:0000250|UniProtKB:Q99623}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC113241; AAI13242.1; -; mRNA.
DR RefSeq; NP_001039663.1; NM_001046198.1.
DR AlphaFoldDB; Q2HJ97; -.
DR SMR; Q2HJ97; -.
DR STRING; 9913.ENSBTAP00000017442; -.
DR PaxDb; Q2HJ97; -.
DR PeptideAtlas; Q2HJ97; -.
DR PRIDE; Q2HJ97; -.
DR Ensembl; ENSBTAT00000017442; ENSBTAP00000017442; ENSBTAG00000013123.
DR GeneID; 515363; -.
DR KEGG; bta:515363; -.
DR CTD; 11331; -.
DR VEuPathDB; HostDB:ENSBTAG00000013123; -.
DR VGNC; VGNC:32809; PHB2.
DR eggNOG; KOG3090; Eukaryota.
DR GeneTree; ENSGT00950000183070; -.
DR HOGENOM; CLU_047969_0_2_1; -.
DR InParanoid; Q2HJ97; -.
DR OMA; IKYTRLG; -.
DR OrthoDB; 1089994at2759; -.
DR TreeFam; TF354230; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000013123; Expressed in digestive system secreted substance and 106 other tissues.
DR ExpressionAtlas; Q2HJ97; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098800; C:inner mitochondrial membrane protein complex; 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:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046625; F:sphingolipid binding; ISS:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1900208; P:regulation of cardiolipin metabolic process; ISS:UniProtKB.
DR GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; 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 Acetylation; Cell membrane; Coiled coil; Cytoplasm; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99623"
FT CHAIN 2..299
FT /note="Prohibitin-2"
FT /id="PRO_0000244434"
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..238
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99623"
FT MOD_RES 128
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99623"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35129"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99623"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35129"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99623"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35129"
SQ SEQUENCE 299 AA; 33357 MW; 6EEA86A48270CB68 CRC64;
MAQNLKDLAG RLPSGPRGMG TALKLLLGAG AVAYGIRESV FTVEGGHRAI FFNRIGGVQQ
DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLS RPNAMELPSM
YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD
DVAITELSFS REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAARMLGE
ALSKNPGYIK LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK
