CYP5_CAEEL
ID CYP5_CAEEL Reviewed; 204 AA.
AC P52013; O62190;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase 5;
DE Short=PPIase 5;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-5;
DE AltName: Full=Rotamase 5;
DE Flags: Precursor;
GN Name=cyn-5; Synonyms=cyp-5; ORFNames=F31C3.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8694762; DOI=10.1042/bj3170179;
RA Page A.P., Macniven K., Hengartner M.O.;
RT "Cloning and biochemical characterization of the cyclophilin homologues
RT from the free-living nematode Caenorhabditis elegans.";
RL Biochem. J. 317:179-185(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP PROTEIN SEQUENCE OF 23-27, X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF
RP 23-204, MASS SPECTROMETRY, ENZYME ACTIVITY, SUBCELLULAR LOCATION,
RP INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12215411; DOI=10.1016/s0022-2836(02)00712-x;
RA Picken N.C., Eschenlauer S., Taylor P., Page A.P., Walkinshaw M.D.;
RT "Structural and biological characterisation of the gut-associated
RT cyclophilin B isoforms from Caenorhabditis elegans.";
RL J. Mol. Biol. 322:15-25(2002).
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;
CC Evidence={ECO:0000269|PubMed:12215411};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12215411}.
CC -!- TISSUE SPECIFICITY: Embryonic, larval and adult gut cells.
CC {ECO:0000269|PubMed:12215411}.
CC -!- DEVELOPMENTAL STAGE: Throughout development, highest in embryos.
CC {ECO:0000269|PubMed:12215411}.
CC -!- INDUCTION: Inhibited by cyclosporin. {ECO:0000269|PubMed:12215411}.
CC -!- MASS SPECTROMETRY: Mass=20766; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12215411};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; U31948; AAC47126.1; -; mRNA.
DR EMBL; Z92784; CAB07192.1; -; Genomic_DNA.
DR PIR; T21587; T21587.
DR RefSeq; NP_493624.1; NM_061223.5.
DR PDB; 1H0P; X-ray; 1.75 A; A=23-204.
DR PDBsum; 1H0P; -.
DR AlphaFoldDB; P52013; -.
DR SMR; P52013; -.
DR BioGRID; 38755; 10.
DR DIP; DIP-24378N; -.
DR STRING; 6239.F31C3.1; -.
DR World-2DPAGE; 0020:P52013; -.
DR EPD; P52013; -.
DR PaxDb; P52013; -.
DR PeptideAtlas; P52013; -.
DR EnsemblMetazoa; F31C3.1.1; F31C3.1.1; WBGene00000881.
DR UCSC; F31C3.1.1; c. elegans.
DR WormBase; F31C3.1; CE17730; WBGene00000881; cyn-5.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000167766; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P52013; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P52013; -.
DR EvolutionaryTrace; P52013; -.
DR PRO; PR:P52013; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000881; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:WormBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:WormBase.
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; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Isomerase; Reference proteome; Rotamase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:12215411"
FT CHAIN 23..204
FT /note="Peptidyl-prolyl cis-trans isomerase 5"
FT /id="PRO_0000025495"
FT DOMAIN 32..189
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 4..18
FT /note="LLVVAAVLAVGALAQ -> FLLWRPCSLSELLLR (in Ref. 1;
FT AAC47126)"
FT /evidence="ECO:0000305"
FT STRAND 26..37
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:1H0P"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1H0P"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:1H0P"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1H0P"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1H0P"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1H0P"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1H0P"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:1H0P"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1H0P"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1H0P"
FT STRAND 182..197
FT /evidence="ECO:0007829|PDB:1H0P"
SQ SEQUENCE 204 AA; 21927 MW; 6216192BFE1FB493 CRC64;
MKSLLVVAAV LAVGALAQGD DAKGPKVTDK VYFDMEIGGK PIGRIVIGLF GKTVPKTATN
FIELAKKPKG EGYPGSKFHR VIADFMIQGG DFTRGDGTGG RSIYGEKFAD ENFKLKHYGA
GWLSMANAGA DTNGSQFFIT TVKTPWLDGR HVVFGKILEG MDVVRKIEQT EKLPGDRPKQ
DVIIAASGHI AVDTPFSVER EAVV
