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Protein

Peptidyl-prolyl cis-trans isomerase FPR2

Gene

FPR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. FKBP-13 may play a role in protein trafficking in the ER.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by both FK506 and rapamycin. Binds FK506 with 15-fold lower affinity than FKB1.

GO - Molecular functioni

  • FK506 binding Source: SGD
  • peptidyl-prolyl cis-trans isomerase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YDR519W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FPR2 (EC:5.2.1.8)
Short name:
PPIase FPR2
Alternative name(s):
FK506-binding protein 2
FKBP proline rotamase 2
FKBP-13
FKBP-15
Gene namesi
Name:FPR2
Synonyms:FKB2
Ordered Locus Names:YDR519W
ORF Names:D9719.24
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR519W.
SGDiS000002927. FPR2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 135118Peptidyl-prolyl cis-trans isomerase FPR2PRO_0000025512Add
BLAST

Proteomic databases

MaxQBiP32472.

Interactioni

Protein-protein interaction databases

BioGridi32570. 22 interactions.
IntActiP32472. 45 interactions.
MINTiMINT-2779497.

Structurei

3D structure databases

ProteinModelPortaliP32472.
SMRiP32472. Positions 39-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 13290PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00530000062784.
HOGENOMiHOG000154887.
InParanoidiP32472.
KOiK09569.
OMAiCEVQAHK.
OrthoDBiEOG77WWQ3.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32472-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFNIYLFVT FFSTILAGSL SDLEIGIIKR IPVEDCLIKA MPGDKVKVHY
60 70 80 90 100
TGSLLESGTV FDSSYSRGSP IAFELGVGRV IKGWDQGVAG MCVGEKRKLQ
110 120 130
IPSSLAYGER GVPGVIPPSA DLVFDVELVD VKSAA
Length:135
Mass (Da):14,487
Last modified:October 1, 1993 - v1
Checksum:i09CA3F1568D7E4B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90646 Genomic DNA. Translation: AAA34604.1.
M90767 Genomic DNA. Translation: AAA34605.1.
U33057 Genomic DNA. Translation: AAB64960.1.
AY558177 Genomic DNA. Translation: AAS56503.1.
BK006938 Genomic DNA. Translation: DAA12350.1.
PIRiS25337.
RefSeqiNP_010807.3. NM_001180827.3.

Genome annotation databases

EnsemblFungiiYDR519W; YDR519W; YDR519W.
GeneIDi852131.
KEGGisce:YDR519W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90646 Genomic DNA. Translation: AAA34604.1.
M90767 Genomic DNA. Translation: AAA34605.1.
U33057 Genomic DNA. Translation: AAB64960.1.
AY558177 Genomic DNA. Translation: AAS56503.1.
BK006938 Genomic DNA. Translation: DAA12350.1.
PIRiS25337.
RefSeqiNP_010807.3. NM_001180827.3.

3D structure databases

ProteinModelPortaliP32472.
SMRiP32472. Positions 39-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32570. 22 interactions.
IntActiP32472. 45 interactions.
MINTiMINT-2779497.

Proteomic databases

MaxQBiP32472.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR519W; YDR519W; YDR519W.
GeneIDi852131.
KEGGisce:YDR519W.

Organism-specific databases

EuPathDBiFungiDB:YDR519W.
SGDiS000002927. FPR2.

Phylogenomic databases

GeneTreeiENSGT00530000062784.
HOGENOMiHOG000154887.
InParanoidiP32472.
KOiK09569.
OMAiCEVQAHK.
OrthoDBiEOG77WWQ3.

Enzyme and pathway databases

BioCyciYEAST:YDR519W-MONOMER.

Miscellaneous databases

PROiP32472.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Saccharomyces cerevisiae contains a homolog of human FKBP-13, a membrane-associated FK506/rapamycin binding protein."
    Partaledis J.A., Fleming M.A., Harding M.W., Berlin V.
    Yeast 8:673-680(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Yeast FKBP-13 is a membrane-associated FK506-binding protein encoded by the nonessential gene FKB2."
    Nielsen J.B., Foor F., Siekerka J.J., Hsu M.J., Ramadan N., Morin N., Shafiee A., Dahl A., Brizuela L., Chrebet G., Bostian K.A., Parent S.A.
    Proc. Natl. Acad. Sci. U.S.A. 89:7471-7475(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-54.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFKBP2_YEAST
AccessioniPrimary (citable) accession number: P32472
Secondary accession number(s): D6VTE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.