Q09637 (CYP9_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase 9
Short name=PPIase 9
EC=5.2.1.8

Alternative name(s):
Cyclophilin-9
Rotamase 9

Gene names

Name:	cyn-9
Synonyms:	cyp-9
ORF Names:	T27D1.1

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens. Ref.2
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Tissue specificity	Co-expressed with pdi-1 in the syncytial hypodermis. Ref.2
Developmental stage	Expression significantly up-regulated in the middle of the L3 (22 hours) and L4 (26 hours) larval stages. Ref.2
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	extracellular matrix organization Traceable author statement Ref.2. Source: WormBase protein folding Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	intracellular Inferred from direct assay PubMed 9454556. Source: WormBase
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	Peptidyl-prolyl cis-trans isomerase 9		PRO_0000064196
Regions
	Domain	8 – 173	166	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q09637 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: F9DAAFB463E7CD46	FASTA	309	35,796
	10 20 30 40 50 60 MAAEKRVFLD ISVDENLIGR IEIRLFVEDA PKTCENFRAL CTGEVGMTPN NKARLHYKQN 70 80 90 100 110 120 EFHRIVKKFM IQGGDITEGD GRGGFSIYGR YFDDEKFKLK HSRPYLLSMA NKGPNSNSSQ 130 140 150 160 170 180 FFITTAAAPH CNGKHVVFGE VVKGQNVVDY IDNLAVDDKS KPLAKVLISN CGELVKKKKP 190 200 210 220 230 240 LKTDEELAAA LEEKNNNARD NEIPKCPKSW LYRDDDNEKK HEMRNDKRRE YRSRRSRSRS 250 260 270 280 290 300 HEKNRDYKKE NRGDSSRSQP RRDENGITVR GRGGVRFRRE RSATPEHWRR NAPTKWVHDS HKHPEEDLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans." Page A.P., Macniven K., Hengartner M.O. Biochem. J. 317:179-185(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Bristol N2.
[2]	"Cyclophilin and protein disulfide isomerase genes are co-transcribed in a functionally related manner in Caenorhabditis elegans." Page A.P. DNA Cell Biol. 16:1335-1343(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U36581 mRNA. Translation: AAC47131.1. U95074 Genomic DNA. Translation: AAB94648.1. Z48245, Z37139 Genomic DNA. Translation: CAA88291.1.
PIR	T18579.
RefSeq	NP_497745.1. NM_065344.4.
UniGene	Cel.19631.
3D structure databases
ProteinModelPortal	Q09637.
SMR	Q09637. Positions 5-175.
ModBase	Search...
Proteomic databases
PaxDb	Q09637.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	T27D1.1; T27D1.1; T27D1.1.
GeneID	175471.
KEGG	cel:CELE_T27D1.1.
UCSC	T27D1.1. c. elegans.
Organism-specific databases
CTD	175471.
WormBase	T27D1.1; CE03745; WBGene00000885; cyn-9.
Phylogenomic databases
eggNOG	COG0652.
GeneTree	ENSGT00550000074595.
HOGENOM	HOG000015947.
InParanoid	Q09637.
KO	K01802.
OMA	HCNGKHV.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	888308.

Entry information

Entry name

CYP9_CAEEL

Accession

Primary (citable) accession number: Q09637
Secondary accession number(s): A2NTF2, Q09339

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project