FKBP4_SCHPO
ID FKBP4_SCHPO Reviewed; 361 AA.
AC O74191; Q9UTU5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=FK506-binding protein 39 kDa;
DE EC=5.2.1.8 {ECO:0000269|PubMed:10544281};
DE AltName: Full=Histone proline isomerase {ECO:0000303|PubMed:14981505};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=fkbp39 {ECO:0000303|PubMed:10544281};
GN ORFNames=SPBC1347.02 {ECO:0000312|PomBase:SPBC1347.02};
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].
RC STRAIN=JY741;
RX PubMed=10544281; DOI=10.1093/oxfordjournals.jbchem.a022530;
RA Himukai R., Kuzuhara T., Horikoshi M.;
RT "Relationship between the subcellular localization and structures of
RT catalytic domains of FKBP-type PPIases.";
RL J. Biochem. 126:879-888(1999).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-145.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14981505; DOI=10.1038/nsmb733;
RA Kuzuhara T., Horikoshi M.;
RT "A nuclear FK506-binding protein is a histone chaperone regulating rDNA
RT silencing.";
RL Nat. Struct. Mol. Biol. 11:275-283(2004).
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-213 AND SER-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: PPIase that acts as a histone chaperone (PubMed:14981505).
CC Histone proline isomerase that increases the rate of cis-trans
CC isomerization at prolines on the histone H3 N-terminal tail. Proline
CC isomerization influences H3 methylation thereby regulating gene
CC expression (By similarity). {ECO:0000250|UniProtKB:Q06205,
CC ECO:0000269|PubMed:14981505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:10544281};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10544281,
CC ECO:0000269|PubMed:14981505}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF017990; AAC29477.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB37433.1; -; Genomic_DNA.
DR EMBL; AB027991; BAA87295.1; -; Genomic_DNA.
DR PIR; JC7159; T43536.
DR RefSeq; NP_596694.1; NM_001022618.2.
DR AlphaFoldDB; O74191; -.
DR SMR; O74191; -.
DR BioGRID; 276362; 164.
DR STRING; 4896.SPBC1347.02.1; -.
DR iPTMnet; O74191; -.
DR MaxQB; O74191; -.
DR PaxDb; O74191; -.
DR PRIDE; O74191; -.
DR EnsemblFungi; SPBC1347.02.1; SPBC1347.02.1:pep; SPBC1347.02.
DR GeneID; 2539812; -.
DR KEGG; spo:SPBC1347.02; -.
DR PomBase; SPBC1347.02; fkbp39.
DR VEuPathDB; FungiDB:SPBC1347.02; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_3_1_1; -.
DR InParanoid; O74191; -.
DR OMA; CQEELIG; -.
DR PhylomeDB; O74191; -.
DR PRO; PR:O74191; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005527; F:macrolide binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; EXP:PomBase.
DR GO; GO:0006334; P:nucleosome assembly; ISO:PomBase.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR023566; PPIase_Fpr3/Fpr4-like.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Chaperone; Isomerase; Nucleus; Phosphoprotein; Reference proteome;
KW Rotamase.
FT CHAIN 1..361
FT /note="FK506-binding protein 39 kDa"
FT /id="PRO_0000075315"
FT DOMAIN 275..361
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 122..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 361 AA; 39302 MW; FA44DF1D12622A82 CRC64;
MSLPIAVYSL SVKGKDVPAV EESTDASIHL TMASIDAGEK SNKPTTLLVK VRPRIPVEDE
DDEELDEQMQ ELLEESQREF VLCTLKPGSL YQQPLNLTIT PGDEVFFSAS GDATIHLSGN
FLVDEEDEEE EESDEDYDLS PTEEDLVETV SGDEESEEES ESEDNSASEE DELDSAPAKK
AQVKKKRTKD ESEQEEAASP KKNNTKKQKV EGTPVKEKKV AFAEKLEQGP TGPAAKKEKQ
QASSNAPSSP KTRTLKGGVV VTDVKTGSGA SATNGKKVEM RYIGKLENGK VFDKNTKGKP
FAFILGRGEV IRGWDVGVAG MQEGGERKIT IPAPMAYGNQ SIPGIPKNST LVFEVKLVRV
H
