PHB1_SCHPO
ID PHB1_SCHPO Reviewed; 282 AA.
AC Q9P7H3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Prohibitin-1;
GN Name=phb1; ORFNames=SPAC1782.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the
CC stabilization of newly synthesized mitochondrial proteins. Has an
CC antiproliferative activity. Regulates replicative life span (By
CC similarity). {ECO:0000250}.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Intermembrane side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR EMBL; CU329670; CAB76268.1; -; Genomic_DNA.
DR PIR; T50096; T50096.
DR RefSeq; NP_594713.1; NM_001020140.2.
DR AlphaFoldDB; Q9P7H3; -.
DR SMR; Q9P7H3; -.
DR BioGRID; 278819; 2.
DR STRING; 4896.SPAC1782.06c.1; -.
DR MaxQB; Q9P7H3; -.
DR PaxDb; Q9P7H3; -.
DR EnsemblFungi; SPAC1782.06c.1; SPAC1782.06c.1:pep; SPAC1782.06c.
DR GeneID; 2542354; -.
DR KEGG; spo:SPAC1782.06c; -.
DR PomBase; SPAC1782.06c; phb1.
DR VEuPathDB; FungiDB:SPAC1782.06c; -.
DR eggNOG; KOG3083; Eukaryota.
DR HOGENOM; CLU_047969_0_2_1; -.
DR InParanoid; Q9P7H3; -.
DR OMA; QKMQFVL; -.
DR PhylomeDB; Q9P7H3; -.
DR PRO; PR:Q9P7H3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISO:PomBase.
DR GO; GO:0000001; P:mitochondrion inheritance; ISO:PomBase.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; ISO:PomBase.
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 3: Inferred from homology;
KW Cytoplasm; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome.
FT CHAIN 1..282
FT /note="Prohibitin-1"
FT /id="PRO_0000316248"
SQ SEQUENCE 282 AA; 31054 MW; 4DBC7DEE0D693C59 CRC64;
MAVVLERVAR YAIPIGIGFT LLQSSIYDVP GGKRAVLFDR LSGVQKQVVQ EGTHFLIPWL
QKAIVYDVRT RPRNIATTTG SKDLQMVSLT LRVLHRPEVG MLPQIYQNLG LDYDERVLPS
IGNEILKSVV AQFDAAELIT QREVVSAKIR QELVQRATEF GIRLEDVSIT HMTFGKEFTK
AVERKQIAQQ EAERARFLVE QSEQERQANV IRAEGEAEAA DIVSKALDKA GGALIQIRRL
ETSKEVATAL ANKGAQVTYL PFGAGSNAQS SSGSGLLLNV NP
