PFD5_SCHPO
ID PFD5_SCHPO Reviewed; 154 AA.
AC O94307;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable prefoldin subunit 5;
DE AltName: Full=Byr1-binding protein Bob1;
GN Name=bob1; ORFNames=SPBC215.02;
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 [GENOMIC DNA], FUNCTION, INTERACTION WITH BYR1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11683500; DOI=10.1046/j.1432-0436.2001.670402.x;
RA Henkel J., Du H., Yang P., Qyang Y., Kansra S., Ko M., Kim H., Marcus S.;
RT "Bob1, a Gim5/MM-1/Pfd5 homolog, interacts with the MAP kinase kinase byr1
RT to regulate sexual differentiation in the fission yeast,
RT Schizosaccharomyces pombe.";
RL Differentiation 67:98-106(2001).
RN [2]
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).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide chain and
CC promotes folding in an environment in which there are many competing
CC pathways for nonnative proteins (By similarity). Required for normal
CC cytoskeletal function and when bound to byr1, is involved in the
CC regulation of sexual differentiation. {ECO:0000250,
CC ECO:0000269|PubMed:11683500}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits (By similarity). Interacts with byr1. {ECO:0000250,
CC ECO:0000269|PubMed:11683500}.
CC -!- INTERACTION:
CC O94307; P10506: byr1; NbExp=2; IntAct=EBI-2042611, EBI-2042633;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11683500}.
CC Note=Localizes to the cell tips and septum forming regions.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA22116.1; -; Genomic_DNA.
DR EMBL; AY035821; AAK60340.1; -; Genomic_DNA.
DR PIR; T39892; T39892.
DR RefSeq; NP_596679.1; NM_001022602.2.
DR AlphaFoldDB; O94307; -.
DR SMR; O94307; -.
DR BioGRID; 277189; 133.
DR IntAct; O94307; 1.
DR STRING; 4896.SPBC215.02.1; -.
DR MaxQB; O94307; -.
DR PaxDb; O94307; -.
DR PRIDE; O94307; -.
DR EnsemblFungi; SPBC215.02.1; SPBC215.02.1:pep; SPBC215.02.
DR GeneID; 2540664; -.
DR KEGG; spo:SPBC215.02; -.
DR PomBase; SPBC215.02; bob1.
DR VEuPathDB; FungiDB:SPBC215.02; -.
DR eggNOG; KOG3048; Eukaryota.
DR HOGENOM; CLU_091867_0_1_1; -.
DR InParanoid; O94307; -.
DR OMA; QAKFKAC; -.
DR PhylomeDB; O94307; -.
DR PRO; PR:O94307; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016272; C:prefoldin complex; ISO:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IC:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR011599; PFD_alpha_archaea.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12674; PTHR12674; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR TIGRFAMs; TIGR00293; TIGR00293; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..154
FT /note="Probable prefoldin subunit 5"
FT /id="PRO_0000153667"
SQ SEQUENCE 154 AA; 16774 MW; 7EDDC52E8D4FFD80 CRC64;
MAEGNKAVDL TSLSLEQLSE VIKQLDSELE YLSTSYGQLG RAQLKFRECL ANVNDAVRAE
NDGKEVLVPL TSSLYVPGKL NLGNSKLLVD IGTGYYVEKS AGEATEYYKR KCEYLASSIE
NLNNAIDAKS VQIRAVQNIM QQKATATTAA TKSS
