PHB1_MESAU
ID PHB1_MESAU Reviewed; 87 AA.
AC P86220;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Prohibitin 1;
DE Flags: Fragments;
GN Name=PHB1; Synonyms=PHB {ECO:0000250|UniProtKB:P35232};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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:0000255}.
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DR AlphaFoldDB; P86220; -.
DR SMR; P86220; -.
DR PRIDE; P86220; -.
DR Proteomes; UP000189706; 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; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
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:0072538; P:T-helper 17 type immune response; ISS:UniProtKB.
DR InterPro; IPR000163; Prohibitin.
DR PANTHER; PTHR23222; PTHR23222; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; DNA synthesis; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN <1..>87
FT /note="Prohibitin 1"
FT /id="PRO_0000394751"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67778"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT NON_CONS 34..35
FT /evidence="ECO:0000305"
FT NON_CONS 44..45
FT /evidence="ECO:0000305"
FT NON_CONS 53..54
FT /evidence="ECO:0000305"
FT NON_CONS 73..74
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 87
SQ SEQUENCE 87 AA; 10043 MW; F38C46EF7385ABBD CRC64;
DLQNVNITLR ILFRPVASQL PRIYTSIGED YDERFDAGEL ITQRQVSDDL TEREFTEAVE
AKQVAQQEAE RARKLEAAED IAYQLSR
