CYP9_CAEEL
ID CYP9_CAEEL Reviewed; 309 AA.
AC Q09637; A2NTF2; Q09339;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase 9;
DE Short=PPIase 9;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-9;
DE AltName: Full=Rotamase 9;
GN Name=cyn-9; Synonyms=cyp-9; ORFNames=T27D1.1;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9407005; DOI=10.1089/dna.1997.16.1335;
RA Page A.P.;
RT "Cyclophilin and protein disulfide isomerase genes are co-transcribed in a
RT functionally related manner in Caenorhabditis elegans.";
RL DNA Cell Biol. 16:1335-1343(1997).
RN [3]
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Thought to function as a catalyst in the folding and
CC modification of cuticle collagens. {ECO:0000269|PubMed:9407005}.
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 -!- TISSUE SPECIFICITY: Co-expressed with pdi-1 in the syncytial
CC hypodermis. {ECO:0000269|PubMed:9407005}.
CC -!- DEVELOPMENTAL STAGE: Expression significantly up-regulated in the
CC middle of the L3 (22 hours) and L4 (26 hours) larval stages.
CC {ECO:0000269|PubMed:9407005}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U36581; AAC47131.1; -; mRNA.
DR EMBL; U95074; AAB94648.1; -; Genomic_DNA.
DR EMBL; Z48245; CAA88291.1; -; Genomic_DNA.
DR EMBL; Z37139; CAA88291.1; JOINED; Genomic_DNA.
DR PIR; T18579; T18579.
DR RefSeq; NP_497745.1; NM_065344.4.
DR AlphaFoldDB; Q09637; -.
DR SMR; Q09637; -.
DR BioGRID; 40711; 2.
DR STRING; 6239.T27D1.1; -.
DR EPD; Q09637; -.
DR PaxDb; Q09637; -.
DR PeptideAtlas; Q09637; -.
DR EnsemblMetazoa; T27D1.1.1; T27D1.1.1; WBGene00000885.
DR GeneID; 175471; -.
DR KEGG; cel:CELE_T27D1.1; -.
DR UCSC; T27D1.1; c. elegans.
DR CTD; 175471; -.
DR WormBase; T27D1.1; CE03745; WBGene00000885; cyn-9.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000173731; -.
DR HOGENOM; CLU_012062_33_4_1; -.
DR InParanoid; Q09637; -.
DR OMA; HCNGKHV; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q09637; -.
DR Reactome; R-CEL-8939211; ESR-mediated signaling.
DR PRO; PR:Q09637; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000885; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; 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; ISS:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; TAS:WormBase.
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; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 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 2: Evidence at transcript level;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..309
FT /note="Peptidyl-prolyl cis-trans isomerase 9"
FT /id="PRO_0000064196"
FT DOMAIN 8..173
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 217..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 35796 MW; F9DAAFB463E7CD46 CRC64;
MAAEKRVFLD ISVDENLIGR IEIRLFVEDA PKTCENFRAL CTGEVGMTPN NKARLHYKQN
EFHRIVKKFM IQGGDITEGD GRGGFSIYGR YFDDEKFKLK HSRPYLLSMA NKGPNSNSSQ
FFITTAAAPH CNGKHVVFGE VVKGQNVVDY IDNLAVDDKS KPLAKVLISN CGELVKKKKP
LKTDEELAAA LEEKNNNARD NEIPKCPKSW LYRDDDNEKK HEMRNDKRRE YRSRRSRSRS
HEKNRDYKKE NRGDSSRSQP RRDENGITVR GRGGVRFRRE RSATPEHWRR NAPTKWVHDS
HKHPEEDLV
