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   26-MAY-2009, entry version 57.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 9;
DE            Short=PPIase;
DE            Short=Rotamase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-9;
GN   Name=cyn-9; Synonyms=cyp-9; ORFNames=T27D1.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=96276416; PubMed=8694762;
RA   Page A.P., Macniven K., Hengartner M.O.;
RT   "Cloning and biochemical characterization of the cyclophilin
RT   homologues 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   MEDLINE=98068840; PubMed=9407005; DOI=10.1089/dna.1997.16.1335;
RA   Page A.P.;
RT   "Cyclophilin and protein disulfide isomerase genes are co-transcribed
RT   in a 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   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Thought to function as a catalyst in the folding
CC       and modification of cuticle collagens.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- TISSUE SPECIFICITY: Co-expressed with pdi-1 in the syncytial
CC       hypodermis.
CC   -!- DEVELOPMENTAL STAGE: Expression significantly up-regulated in the
CC       middle of the L3 (22 hours) and L4 (26 hours) larval stages.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR   EMBL; U36581; AAC47131.1; -; mRNA.
DR   EMBL; U95074; AAB94648.1; -; Genomic_DNA.
DR   EMBL; Z37139; CAA85495.1; -; Genomic_DNA.
DR   EMBL; Z48245; CAA85495.1; JOINED; 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; -.
DR   UniGene; Cel.19631; -.
DR   HSSP; Q27450; 1A58.
DR   Ensembl; T27D1.1; Caenorhabditis elegans.
DR   GeneID; 175471; -.
DR   KEGG; cel:T27D1.1; -.
DR   NMPDR; fig|6239.3.peg.9189; -.
DR   WormBase; WBGene00000885; cyn-9.
DR   WormPep; T27D1.1; CE03745.
DR   OMA; Q09637; HWRRNAP.
DR   BRENDA; 5.2.1.8; 672.
DR   NextBio; 888308; -.
DR   ArrayExpress; Q09637; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; NAS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Isomerase; Rotamase.
FT   CHAIN         1    309       Peptidyl-prolyl cis-trans isomerase 9.
FT                                /FTId=PRO_0000064196.
FT   DOMAIN        8    173       PPIase cyclophilin-type.
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
//