FKBP3_YEAST
ID FKBP3_YEAST Reviewed; 411 AA.
AC P38911; D6W0K9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000303|PubMed:7925954};
DE Short=PPIase {ECO:0000303|PubMed:7925954};
DE EC=5.2.1.8 {ECO:0000269|PubMed:7525596, ECO:0000269|PubMed:7925954, ECO:0000269|PubMed:8051210};
DE AltName: Full=FK506-binding nuclear protein;
DE AltName: Full=FKBP-70 {ECO:0000303|PubMed:7925954};
DE AltName: Full=Nucleolar proline isomerase {ECO:0000303|PubMed:8051210};
DE AltName: Full=Proline rotamase {ECO:0000305};
GN Name=FPR3 {ECO:0000303|PubMed:7525596};
GN Synonyms=NPI46 {ECO:0000303|PubMed:8051210}; OrderedLocusNames=YML074C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7925954; DOI=10.1016/0014-5793(94)00927-9;
RA Manning-Krieg U.C., Henriquez R., Cammas F., Graff P., Gaveriaux S.,
RA Movva N.R.;
RT "Purification of FKBP-70, a novel immunophilin from Saccharomyces
RT cerevisiae, and cloning of its structural gene, FPR3.";
RL FEBS Lett. 352:98-103(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8051210; DOI=10.1083/jcb.126.4.853;
RA Shan X., Xue Z., Melese T.;
RT "Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in
RT the nucleolus.";
RL J. Cell Biol. 126:853-862(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=YNN 214;
RX PubMed=7525596; DOI=10.1083/jcb.127.3.623;
RA Benton B.M., Zang J.-H., Thorner J.;
RT "A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the
RT yeast Saccharomyces cerevisiae is a proline rotamase localized to the
RT nucleolus.";
RL J. Cell Biol. 127:623-639(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP PHOSPHORYLATION AT TYR-184 AND SER-186.
RX PubMed=9148902; DOI=10.1074/jbc.272.20.12961;
RA Wilson L.K., Dhillon N., Thorner J., Martin G.S.;
RT "Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar
RT immunophilin Fpr3.";
RL J. Biol. Chem. 272:12961-12967(1997).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP INTERACTION WITH NOP53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15686447; DOI=10.1042/bj20041297;
RA Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T.,
RA Wozniak R.W., Aitchison J.D.;
RT "Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein.";
RL Biochem. J. 388:819-826(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-81, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-81 AND THR-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Proline isomerase that belongs to an abundant class of
CC enzymes that catalyze the cis-trans isomerization of X-Pro peptide
CC bonds and can accelerate the refolding of proline-containing
CC polypeptides (PubMed:7925954, PubMed:8051210, PubMed:7525596).
CC Specifically binds nuclear localization sequences (PubMed:7925954). May
CC be involved in the assembly or folding of ribosomal proteins
CC (PubMed:8051210). {ECO:0000269|PubMed:7525596,
CC ECO:0000269|PubMed:7925954, ECO:0000269|PubMed:8051210}.
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; Evidence={ECO:0000269|PubMed:7525596,
CC ECO:0000269|PubMed:7925954, ECO:0000269|PubMed:8051210};
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Interacts with NOP53. {ECO:0000269|PubMed:15686447}.
CC -!- INTERACTION:
CC P38911; Q06205: FPR4; NbExp=4; IntAct=EBI-6951, EBI-6956;
CC P38911; P43586: LOC1; NbExp=3; IntAct=EBI-6951, EBI-22906;
CC P38911; Q12080: NOP53; NbExp=3; IntAct=EBI-6951, EBI-29395;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8051210}.
CC -!- PTM: Phosphorylated at tyrosine and dephosphorylated by the
CC phosphotyrosine-specific phosphoprotein phosphatase PTP1.
CC {ECO:0000269|PubMed:9148902}.
CC -!- MISCELLANEOUS: Present with 9490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC {ECO:0000305}.
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DR EMBL; L34569; AAB04165.1; -; Genomic_DNA.
DR EMBL; X79379; CAA55924.1; -; Genomic_DNA.
DR EMBL; S73876; AAB31995.1; -; Genomic_DNA.
DR EMBL; Z46373; CAA86504.1; -; Genomic_DNA.
DR EMBL; AY693136; AAT93155.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09823.1; -; Genomic_DNA.
DR PIR; S48647; S48647.
DR RefSeq; NP_013637.1; NM_001182433.1.
DR AlphaFoldDB; P38911; -.
DR SMR; P38911; -.
DR BioGRID; 35067; 139.
DR DIP; DIP-6578N; -.
DR IntAct; P38911; 71.
DR MINT; P38911; -.
DR STRING; 4932.YML074C; -.
DR iPTMnet; P38911; -.
DR MaxQB; P38911; -.
DR PaxDb; P38911; -.
DR PRIDE; P38911; -.
DR EnsemblFungi; YML074C_mRNA; YML074C; YML074C.
DR GeneID; 854901; -.
DR KEGG; sce:YML074C; -.
DR SGD; S000004539; FPR3.
DR VEuPathDB; FungiDB:YML074C; -.
DR eggNOG; KOG0552; Eukaryota.
DR GeneTree; ENSGT00940000176659; -.
DR HOGENOM; CLU_022297_3_1_1; -.
DR InParanoid; P38911; -.
DR OMA; CPPHMAY; -.
DR BioCyc; YEAST:YML074C-MON; -.
DR PRO; PR:P38911; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38911; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005527; F:macrolide binding; IDA:SGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IDA:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:SGD.
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 Acetylation; Isomerase; Nucleus; Phosphoprotein; Reference proteome;
KW Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..411
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000075313"
FT DOMAIN 324..411
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 54..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..271
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 65..84
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 184
FT /note="Phosphotyrosine; by CK2"
FT /evidence="ECO:0000269|PubMed:9148902"
FT MOD_RES 186
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9148902"
FT CONFLICT 122
FT /note="L -> P (in Ref. 1; AAB04165)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> EEE (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="L -> F (in Ref. 1; AAB04165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46553 MW; A01D24DE0078FE11 CRC64;
MSDLLPLATY SLNVEPYTPV PAIDVTMPIT VRITMAALNP EAIDEENKPS TLRIIKRNPD
FEDDDFLGGD FDEDEIDEES SEEEEEEKTQ KKKKSKGKKA ESESEDDEED DDEDDEFQES
VLLTLSPEAQ YQQSLDLTIT PEEEVQFIVT GSYAISLSGN YVKHPFDTPM GVEGEDEDED
ADIYDSEDYD LTPDEDEIIG DDMDDLDDEE EEEVRIEEVQ EEDEEDNDGE EEQEEEEEEE
QKEEVKPEPK KSKKEKKRKH EEKEEEKKAK KVKKVEFKKD LEEGPTKPKS KKEQDKHKPK
SKVLEGGIVI EDRTIGDGPQ AKRGARVGMR YIGKLKNGKV FDKNTSGKPF AFKLGRGEVI
KGWDIGVAGM SVGGERRIII PAPYAYGKQA LPGIPANSEL TFDVKLVSMK N
