PHB1_CHICK
ID PHB1_CHICK Reviewed; 272 AA.
AC P84173;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Prohibitin 1;
GN Name=PHB1; Synonyms=PHB {ECO:0000250|UniProtKB:P67779};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=White Leghorn Hisex; TISSUE=Trunk;
RA Boardman P.E., Bonfield J.K., Brown W.R.A., Carder C., Chalk S.E.,
RA Croning M.D.R., Davies R.M., Francis M.D., Grafham D.V., Hubbard S.J.,
RA Humphray S.J., Hunt P.J., Maddison M., McLaren S.R., Niblett D.,
RA Overton I.M., Rogers J., Scott C.E., Taylor R.G., Tickle C., Wilson S.A.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX PubMed=16287166; DOI=10.1002/pmic.200402056;
RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA Schneider J., Palomar M.A., Linares R.;
RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT development.";
RL Proteomics 5:4946-4957(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 in the
CC nucleus. {ECO:0000250|UniProtKB:P35232}.
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. {ECO:0000250|UniProtKB:P35232}.
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. {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. {ECO:0000250|UniProtKB:P35232}.
CC -!- INTERACTION:
CC P84173; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-1636878, EBI-1635766;
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 -!- MASS SPECTROMETRY: Mass=29804; Mass_error=2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287166};
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000255}.
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DR EMBL; CR387706; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P84173; -.
DR SMR; P84173; -.
DR IntAct; P84173; 1.
DR STRING; 9031.ENSGALP00000001750; -.
DR PaxDb; P84173; -.
DR VEuPathDB; HostDB:geneid_419980; -.
DR eggNOG; KOG3083; Eukaryota.
DR HOGENOM; CLU_047969_0_0_1; -.
DR InParanoid; P84173; -.
DR PhylomeDB; P84173; -.
DR PRO; PR:P84173; -.
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; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; DNA synthesis; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleus; Reference proteome.
FT CHAIN 1..272
FT /note="Prohibitin 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000223490"
FT COILED 177..211
FT /evidence="ECO:0000255"
SQ SEQUENCE 272 AA; 29896 MW; 3FCD502A96EC3633 CRC64;
MAAKVFESIG KFGLGLAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDTVV GEGTHFLIPW
VQKPIIFDCR SRPRNIPVIT GSKDLQNVNI TLRILFRPVT AQLPRIFTSI GEDYDERVLP
SITTEILKSV VARFDAGELI TQRELVSRQV SEDLTERAAT FGLILDDVSL THLTFGKEFT
EAVEMKQVAQ QEAERARFIV EKAEQQKKAA VISAEGDSKA AELIANSLAT AGDGLIELRK
LEAAEDIAYQ LSRSRNITYL PSGQSVLLQL PQ
