P52009 (CYP1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase 1
Short name=PPIase 1
EC=5.2.1.8

Alternative name(s):
Cyclophilin-1
Rotamase 1

Gene names

Name:	cyn-1
Synonyms:	cyp-1
ORF Names:	Y49A3A.5

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	192 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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
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	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 192	192	Peptidyl-prolyl cis-trans isomerase 1		PRO_0000064190
Regions
	Domain	25 – 188	164	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P52009 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: C2094D91809ECE85	FASTA	192	20,711
	10 20 30 40 50 60 MKFLLRASSL AGQSLRFASQ RPKVFFDVSI GEEPAGRVTM ELFNDVVPKT AENFRALCTG 70 80 90 100 110 120 EKGVGEQGVA LHFKGSKFHR IIPEFMIQGG DFTRHNGTGG ESIYGNKFKD ENFDLKHTGP 130 140 150 160 170 180 GCLSMANAGP NTNGSQFFIC TVDTPWLDGG HVVFGQVTDG MSVVKKIEKM GSRSGAPAKT 190 VTIADCGELK SE

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: 8694762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30943 mRNA. Translation: AAC47116.1. AL033512 Genomic DNA. Translation: CAA22075.1.
PIR	T27034.
RefSeq	NP_506561.1. NM_074160.4.
UniGene	Cel.19634.
3D structure databases
ProteinModelPortal	P52009.
SMR	P52009. Positions 21-190.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y49A3A.5.1; Y49A3A.5.1; Y49A3A.5. Y49A3A.5.2; Y49A3A.5.2; Y49A3A.5.
GeneID	179936.
KEGG	cel:Y49A3A.5.
UCSC	Y49A3A.5.1. c. elegans.
Organism-specific databases
CTD	179936.
WormBase	Y49A3A.5; CE22213; WBGene00000877; cyn-1.
Phylogenomic databases
eggNOG	meNOG15253.
GeneTree	EMGT00050000000009.
HOGENOM	HBG610621.
InParanoid	P52009.
OMA	ENFTLTH.
PhylomeDB	P52009.
Gene expression databases
ArrayExpress	P52009.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K03767.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
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	907462.

Entry information

Entry name

CYP1_CAEEL

Accession

Primary (citable) accession number: P52009

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project