PPIA_CANAL
ID PPIA_CANAL Reviewed; 162 AA.
AC P22011; A0A1D8PR38; Q3MPA6; Q5AH66;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8 {ECO:0000269|PubMed:2269432};
DE AltName: Full=Cyclophilin;
DE Short=CPH;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase;
GN Name=CYP1; OrderedLocusNames=CAALFM_C702380CA;
GN ORFNames=CaJ7.0279, CaO19.13826, CaO19.6472;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=2269432; DOI=10.1016/0378-1119(90)90252-m;
RA Koser P.L., Livi G.P., Levy M.A., Rosenberg M., Bergsma D.J.;
RT "A Candida albicans homolog of a human cyclophilin gene encodes a peptidyl-
RT prolyl cis-trans isomerase.";
RL Gene 96:189-195(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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].
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. {ECO:0000269|PubMed:2269432}.
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:2269432};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC {ECO:0000269|PubMed:2269432}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC subfamily. {ECO:0000305}.
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DR EMBL; M60628; AAA34336.1; -; Genomic_DNA.
DR EMBL; AP006852; BAE44754.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30599.1; -; Genomic_DNA.
DR PIR; JQ0888; CSCK.
DR RefSeq; XP_721313.1; XM_716220.2.
DR AlphaFoldDB; P22011; -.
DR SMR; P22011; -.
DR BioGRID; 1220072; 1.
DR STRING; 237561.P22011; -.
DR Allergome; 799; Cand a CyP.
DR COMPLUYEAST-2DPAGE; P22011; -.
DR PRIDE; P22011; -.
DR GeneID; 3636978; -.
DR KEGG; cal:CAALFM_C702380CA; -.
DR CGD; CAL0000183095; CYP1.
DR VEuPathDB; FungiDB:C7_02380C_A; -.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P22011; -.
DR OMA; SIVSMRV; -.
DR OrthoDB; 1403619at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:CGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..162
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064129"
FT DOMAIN 5..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 162 AA; 17575 MW; 3467726615CDB50D CRC64;
MSTVYFDVSA DGQKLGKITF KLYDDVVPKT AENFRALCTG EKGFGYKGSI FHRVIPQFML
QGGDFTNFNG TGGKSIYGTK FADENFVKRH DRPGLLSMAN AGPNTNGSQF FITTVPCPWL
DGKHVVFGEV TDGLDIVKKI ESFGSGSGAT SKKIVIEESG QL
