FKBP2_YEAST
ID FKBP2_YEAST Reviewed; 135 AA.
AC P32472; D6VTE0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FPR2;
DE Short=PPIase FPR2;
DE EC=5.2.1.8 {ECO:0000269|PubMed:1380159};
DE AltName: Full=13-kDa membrane-associated FK506-binding protein {ECO:0000303|PubMed:1380159};
DE Short=FKBP-13;
DE AltName: Full=FK506-binding protein 2;
DE AltName: Full=FKBP proline rotamase 2;
DE AltName: Full=FKBP-15;
DE Flags: Precursor;
GN Name=FPR2; Synonyms=FKB2; OrderedLocusNames=YDR519W; ORFNames=D9719.24;
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].
RX PubMed=1279908; DOI=10.1002/yea.320080812;
RA Partaledis J.A., Fleming M.A., Harding M.W., Berlin V.;
RT "Saccharomyces cerevisiae contains a homolog of human FKBP-13, a membrane-
RT associated FK506/rapamycin binding protein.";
RL Yeast 8:673-680(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-54, FUNCTION,
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=1380159; DOI=10.1073/pnas.89.16.7471;
RA Nielsen J.B., Foor F., Siekerka J.J., Hsu M.J., Ramadan N., Morin N.,
RA Shafiee A., Dahl A., Brizuela L., Chrebet G., Bostian K.A., Parent S.A.;
RT "Yeast FKBP-13 is a membrane-associated FK506-binding protein encoded by
RT the nonessential gene FKB2.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7471-7475(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
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 [6]
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. FKBP-13 may play a role in protein trafficking in the
CC ER. {ECO:0000305|PubMed:1380159}.
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:1380159};
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin. Binds FK506
CC with 15-fold lower affinity than FKB1. {ECO:0000269|PubMed:1380159}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Note=Is not secreted and
CC probably localized in the endoplasmic reticulum.
CC {ECO:0000305|PubMed:1380159}.
CC -!- MISCELLANEOUS: Present with 5400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; M90646; AAA34604.1; -; Genomic_DNA.
DR EMBL; M90767; AAA34605.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64960.1; -; Genomic_DNA.
DR EMBL; AY558177; AAS56503.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12350.1; -; Genomic_DNA.
DR PIR; S25337; S25337.
DR RefSeq; NP_010807.3; NM_001180827.3.
DR AlphaFoldDB; P32472; -.
DR SMR; P32472; -.
DR BioGRID; 32570; 44.
DR IntAct; P32472; 46.
DR MINT; P32472; -.
DR STRING; 4932.YDR519W; -.
DR MaxQB; P32472; -.
DR PaxDb; P32472; -.
DR PRIDE; P32472; -.
DR EnsemblFungi; YDR519W_mRNA; YDR519W; YDR519W.
DR GeneID; 852131; -.
DR KEGG; sce:YDR519W; -.
DR SGD; S000002927; FPR2.
DR VEuPathDB; FungiDB:YDR519W; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000173147; -.
DR HOGENOM; CLU_013615_8_2_1; -.
DR InParanoid; P32472; -.
DR OMA; WAYGSRG; -.
DR BioCyc; YEAST:YDR519W-MON; -.
DR PRO; PR:P32472; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32472; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005528; F:FK506 binding; IDA:SGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PTHR45779; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Isomerase; Membrane;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:1380159"
FT CHAIN 18..135
FT /note="Peptidyl-prolyl cis-trans isomerase FPR2"
FT /id="PRO_0000025512"
FT DOMAIN 43..132
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 135 AA; 14487 MW; 09CA3F1568D7E4B4 CRC64;
MMFNIYLFVT FFSTILAGSL SDLEIGIIKR IPVEDCLIKA MPGDKVKVHY TGSLLESGTV
FDSSYSRGSP IAFELGVGRV IKGWDQGVAG MCVGEKRKLQ IPSSLAYGER GVPGVIPPSA
DLVFDVELVD VKSAA
