PHB1_BOVIN
ID PHB1_BOVIN Reviewed; 272 AA.
AC Q3T165;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Prohibitin 1;
GN Name=PHB1; Synonyms=PHB;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 in the
CC nucleus (By similarity). Plays a role in adipose tissue and glucose
CC homeostasis in a sex-specific manner (By similarity). Contributes to
CC pulmonary vascular remodeling by accelerating proliferation of
CC pulmonary arterial smooth muscle cells (By similarity).
CC {ECO:0000250|UniProtKB:P35232, ECO:0000250|UniProtKB:P67778,
CC ECO:0000250|UniProtKB:P67779}.
CC -!- FUNCTION: In the mitochondria, together with PHB2, 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 (By similarity). The prohibitin complex, with
CC DNAJC19, regulates cardiolipin remodeling and the protein turnover of
CC OMA1 in a cardiolipin-binding manner (By similarity). Regulates
CC mitochondrial respiration activity playing a role in cellular aging.
CC The prohibitin complex plays a role of mitophagy receptor involved in
CC targeting mitochondria for autophagic degradation. Involved in
CC mitochondrial-mediated antiviral innate immunity, activates DDX58/RIG-
CC I-mediated signal transduction and production of IFNB1 and
CC proinflammatory cytokine IL6 (By similarity).
CC {ECO:0000250|UniProtKB:P35232, ECO:0000250|UniProtKB:P67778}.
CC -!- FUNCTION: In the nucleus, acts as a transcription coregulator, enhances
CC promoter binding by TP53, a transcription factor it activates, but
CC reduces the promoter binding by E2F1, a transcription factor it
CC represses. Interacts with STAT3 to affect IL17 secretion in T-helper
CC Th17 cells. {ECO:0000250|UniProtKB:P35232}.
CC -!- FUNCTION: In the plasma membrane, 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.
CC {ECO:0000250|UniProtKB:P67778}.
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 STOML2. Interacts
CC with MAP1LC3B (membrane-bound form LC3-II); the interaction requires
CC PHB2 and takes place upon Parkin-mediated mitochondrial damage.
CC Interacts with STAT3 (unphosphorylated or phosphorylated at 'Ser-727').
CC Interacts with CLPB (By similarity). Interacts with CD86 (via
CC cytoplasmic domain); the interactions increases after priming with CD40
CC (By similarity). {ECO:0000250|UniProtKB:P35232,
CC ECO:0000250|UniProtKB:P67778}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P35232}. Nucleus {ECO:0000250|UniProtKB:P35232}.
CC Cytoplasm {ECO:0000250|UniProtKB:P35232}. Cell membrane
CC {ECO:0000250|UniProtKB:P35232}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR EMBL; BC102094; AAI02095.1; -; mRNA.
DR RefSeq; NP_001029744.1; NM_001034572.2.
DR RefSeq; XP_005220626.1; XM_005220569.3.
DR AlphaFoldDB; Q3T165; -.
DR SMR; Q3T165; -.
DR STRING; 9913.ENSBTAP00000022759; -.
DR PaxDb; Q3T165; -.
DR PeptideAtlas; Q3T165; -.
DR PRIDE; Q3T165; -.
DR Ensembl; ENSBTAT00000022759; ENSBTAP00000022759; ENSBTAG00000017120.
DR Ensembl; ENSBTAT00000070853; ENSBTAP00000065386; ENSBTAG00000017120.
DR GeneID; 530409; -.
DR KEGG; bta:530409; -.
DR CTD; 5245; -.
DR VEuPathDB; HostDB:ENSBTAG00000017120; -.
DR VGNC; VGNC:32808; PHB1.
DR eggNOG; KOG3083; Eukaryota.
DR GeneTree; ENSGT00950000183070; -.
DR HOGENOM; CLU_047969_0_0_1; -.
DR InParanoid; Q3T165; -.
DR OMA; QKMQFVL; -.
DR OrthoDB; 1089994at2759; -.
DR TreeFam; TF300095; -.
DR Reactome; R-BTA-5673000; RAF activation.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000017120; Expressed in diaphragm and 106 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001850; F:complement component C3a binding; IEA:Ensembl.
DR GO; GO:0001851; F:complement component C3b binding; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0031871; F:proteinase activated receptor binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
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:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; IEA:Ensembl.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR GO; GO:0045917; P:positive regulation of complement activation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0039529; P:RIG-I signaling pathway; IEA:Ensembl.
DR GO; GO:0072538; P:T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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; DNA synthesis;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT CHAIN 2..272
FT /note="Prohibitin 1"
FT /id="PRO_0000223489"
FT COILED 177..211
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67778"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67778"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT MOD_RES 202
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P67778"
FT MOD_RES 249
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
SQ SEQUENCE 272 AA; 29804 MW; 915494273E342C76 CRC64;
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW
VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP
SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT
EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK
LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ
