FKBP_CANAL
ID FKBP_CANAL Reviewed; 124 AA.
AC P28870; A0A1D8PR51; Q3MP88; Q59LZ3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=FK506-binding protein 1;
DE Short=FKBP;
DE EC=5.2.1.8 {ECO:0000305|PubMed:1563628};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rapamycin-binding protein;
GN Name=RBP1; Synonyms=RBP11; ORFNames=CaO19.11186, CaO19.3702;
GN and
GN Name=RBP2; Synonyms=RBP12; OrderedLocusNames=CAALFM_C702570CA;
GN ORFNames=CaJ7.0299, CaO19.13810, CaO19.6452;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=1563628; DOI=10.1016/0378-1119(92)90679-j;
RA Ferrara A., Cafferkey R., Vivi G.P.;
RT "Cloning and sequence analysis of a rapamycin-binding protein-encoding gene
RT (RBP1) from Candida albicans.";
RL Gene 113:125-127(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RBP2).
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RBP1 AND RBP2).
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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:0000305|PubMed:1563628};
CC -!- ACTIVITY REGULATION: Inhibited by rapamycin.
CC {ECO:0000305|PubMed:1563628}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M84759; AAA34367.1; -; Genomic_DNA.
DR EMBL; AP006852; BAE44772.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30615.1; -; Genomic_DNA.
DR PIR; JN0320; JN0320.
DR RefSeq; XP_710751.1; XM_705659.2.
DR PDB; 5HTG; X-ray; 2.40 A; A/B=3-124.
DR PDB; 5HW6; X-ray; 2.40 A; A/B=3-124.
DR PDB; 5HW7; X-ray; 2.29 A; A/B=3-124.
DR PDB; 5HW8; X-ray; 2.86 A; A/B/C/D/E/F/G/H=3-124.
DR PDB; 5I98; X-ray; 2.00 A; A/B=3-122.
DR PDB; 6TZ6; X-ray; 2.55 A; C/F=1-124.
DR PDBsum; 5HTG; -.
DR PDBsum; 5HW6; -.
DR PDBsum; 5HW7; -.
DR PDBsum; 5HW8; -.
DR PDBsum; 5I98; -.
DR PDBsum; 6TZ6; -.
DR AlphaFoldDB; P28870; -.
DR SMR; P28870; -.
DR BioGRID; 1220109; 2.
DR STRING; 237561.P28870; -.
DR PRIDE; P28870; -.
DR GeneID; 3647647; -.
DR KEGG; cal:CAALFM_C702570CA; -.
DR CGD; CAL0000188340; RBP1.
DR VEuPathDB; FungiDB:C7_02570C_A; -.
DR eggNOG; KOG0544; Eukaryota.
DR HOGENOM; CLU_013615_12_0_1; -.
DR InParanoid; P28870; -.
DR OMA; RVIAGWD; -.
DR OrthoDB; 1328688at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0005527; F:macrolide binding; IEA:EnsemblFungi.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IGI:CGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:EnsemblFungi.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:1901710; P:regulation of homoserine biosynthetic process; IEA:EnsemblFungi.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..124
FT /note="FK506-binding protein 1"
FT /id="PRO_0000075302"
FT DOMAIN 23..122
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT CONFLICT 92
FT /note="P -> G (in Ref. 1; AAA34367)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5I98"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:5I98"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5I98"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:5I98"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5I98"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:5I98"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:5I98"
FT TURN 68..73
FT /evidence="ECO:0007829|PDB:5I98"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:5I98"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5I98"
FT TURN 96..100
FT /evidence="ECO:0007829|PDB:5I98"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5I98"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:5I98"
SQ SEQUENCE 124 AA; 13267 MW; D29D481FFBF72242 CRC64;
MSEELPQIEI VQEGDNTTFA KPGDTVTIHY DGKLTNGKEF DSSRKRGKPF TCTVGVGQVI
KGWDISLTNN YGKGGANLPK ISKGTKAILT IPPNLAYGPR GIPPIIGPNE TLVFEVELLG
VNGQ
