PSI1_SCHPO
ID PSI1_SCHPO Reviewed; 379 AA.
AC Q09912; Q9UU92;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Protein psi1;
DE AltName: Full=Protein psi;
GN Name=psi1; Synonyms=psi; ORFNames=SPCC830.07c;
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 [MRNA].
RX PubMed=7772606; DOI=10.1016/0167-4781(95)00063-m;
RA Park S.-K., Chon S.-K., Yoo H.-S.;
RT "A cDNA of Schizosaccharomyces pombe encoding a homologue of DnaJ-like
RT protein.";
RL Biochim. Biophys. Acta 1262:87-90(1995).
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: Required for nuclear migration during mitosis. It is required
CC for the normal initiation of translation.
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DR EMBL; L37753; AAA74732.1; -; mRNA.
DR EMBL; CU329672; CAB52880.1; -; Genomic_DNA.
DR PIR; S55900; S55900.
DR PIR; T41633; T41633.
DR RefSeq; NP_588477.1; NM_001023468.2.
DR AlphaFoldDB; Q09912; -.
DR SMR; Q09912; -.
DR BioGRID; 275576; 4.
DR STRING; 4896.SPCC830.07c.1; -.
DR MaxQB; Q09912; -.
DR PaxDb; Q09912; -.
DR EnsemblFungi; SPCC830.07c.1; SPCC830.07c.1:pep; SPCC830.07c.
DR GeneID; 2539002; -.
DR KEGG; spo:SPCC830.07c; -.
DR PomBase; SPCC830.07c; psi1.
DR VEuPathDB; FungiDB:SPCC830.07c; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q09912; -.
DR OMA; DVNFPET; -.
DR PhylomeDB; Q09912; -.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SPO-3371568; Attenuation phase.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR PRO; PR:Q09912; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; ISO:PomBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; NAS:PomBase.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Reference proteome.
FT CHAIN 1..379
FT /note="Protein psi1"
FT /id="PRO_0000071130"
FT DOMAIN 1..70
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 69..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 91
FT /note="G -> C (in Ref. 1; AAA74732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 40260 MW; B8B949A1903F9B8A CRC64;
MVADTKLYDC LEVRPEASEA ELKKAYRKLA LKYHPDKNPN GEKKFKEISL AYEVLSDPQR
RKLYDQYGIT EGNAAPPPPG AEGGPGAGFG GFPGAGPGGA RTFHFNMGGP GGAQFFSASD
PNDIFERVFG HAFAGGGGMG GGMGGMGGMD DDMDMDGGFG TRTRGGGMPG GFANMFGGGG
AGPHARRSHP SFGGSRPSQP PAQNEVITRP LNVSLEDLFT GCTKKMKISR HIIDASGQSV
KADRILEIKV KPGWKAGTKI KFAGEGDEKP DGTVQDIQFV LAEKPHPVFT RSGDDLRMQV
ELSLKEALLG FSKQISTIDG KKLKVSSSLP TQPGYEITYP GFGMPLPKNP SQRGNMIIEC
KVKFPTELTP AQKTAAEAF
