CYPH_CATRO
ID CYPH_CATRO Reviewed; 172 AA.
AC Q39613; I3QBM4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000255|RuleBase:RU363019, ECO:0000303|PubMed:24939849};
DE Short=PPIase {ECO:0000255|RuleBase:RU363019, ECO:0000303|PubMed:24939849};
DE EC=5.2.1.8 {ECO:0000255|RuleBase:RU363019, ECO:0000269|PubMed:24939849};
DE AltName: Full=Cyclophilin {ECO:0000303|PubMed:24939849, ECO:0000303|Ref.1};
DE Short=Cyp {ECO:0000303|PubMed:24939849};
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase;
DE AltName: Allergen=Cat r 1 {ECO:0000303|PubMed:24939849};
GN Name=PCKR1;
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Clastre M., Maaroufi H., Andreu F., Chenieux J.-C., Rideau M., Hamdi S.;
RT "Isolation of a full-length cDNA encoding a cytosolic cyclophilin from
RT Periwinkle (Catharanthus roseus).";
RL (er) Plant Gene Register PGR95-100(1995).
RN [2] {ECO:0000312|EMBL:AFI56997.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-14, STRUCTURE BY NMR,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PTM, ALLERGEN, MUTAGENESIS OF 48-ARG--HIS-54, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=24939849; DOI=10.1074/jbc.m114.559971;
RA Ghosh D., Mueller G.A., Schramm G., Edwards L.L., Petersen A., London R.E.,
RA Haas H., Gupta Bhattacharya S.;
RT "Primary identification, biochemical characterization, and immunologic
RT properties of the allergenic pollen cyclophilin cat R 1.";
RL J. Biol. Chem. 289:21374-21385(2014).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (By similarity).
CC It catalyzes the cis-trans isomerization of proline imidic peptide
CC bonds in oligopeptides (PubMed:24939849).
CC {ECO:0000250|UniProtKB:Q8LDP4, ECO:0000269|PubMed:24939849}.
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;
CC Evidence={ECO:0000269|PubMed:24939849};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24939849}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen. {ECO:0000269|PubMed:24939849}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:24939849}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 100% of
CC 15 patients tested allergic to periwinkle C.roseus pollen. Causes
CC release of beta-hexosaminidase from rat basophil leukemia (RBL) cells.
CC {ECO:0000269|PubMed:24939849}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; X85185; CAA59468.1; -; mRNA.
DR EMBL; JF973325; AFI56997.1; -; mRNA.
DR PIR; T10056; T10056.
DR PDB; 2MC9; NMR; -; A=1-172.
DR PDBsum; 2MC9; -.
DR AlphaFoldDB; Q39613; -.
DR BMRB; Q39613; -.
DR SMR; Q39613; -.
DR Allergome; 2900; Cat r 1.
DR Allergome; 3181; Cat r 1.0101.
DR PRIDE; Q39613; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0061083; P:regulation of protein refolding; ISS:UniProtKB.
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 3D-structure; Allergen; Chaperone; Cytoplasm; Direct protein sequencing;
KW Isomerase; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:24939849"
FT CHAIN 2..172
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064143"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MUTAGEN 48..54
FT /note="Missing: No effect in binding to IgE."
FT /evidence="ECO:0000269|PubMed:24939849"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2MC9"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:2MC9"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2MC9"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2MC9"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:2MC9"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2MC9"
SQ SEQUENCE 172 AA; 18285 MW; EA6EC51886A50A81 CRC64;
MPNPRVFFDM SVGGQPAGRI VMELFADTTP RTAENFRALC TGEKGTGRSG KPLHYKDSSF
HRVIPGFMCQ GGDFTAGNGT GGESIYGAKF ADENFIKKHT GPGILSMANA GPNTNGSQFF
ICTAKTEWLD GKHVVFGQVV EGMDVVKAIE KVGSSSGRTA KKVVVEDCGQ LS
