P52015 (CYP7_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase 7
Short name=PPIase 7
EC=5.2.1.8

Alternative name(s):
Cyclophilin-7
Rotamase 7

Gene names

Name:	cyn-7
Synonyms:	cyp-7
ORF Names:	Y75B12B.2

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase 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 – 171	171	Peptidyl-prolyl cis-trans isomerase 7		PRO_0000064194
Regions
	Domain	7 – 170	164	PPIase cyclophilin-type
Experimental info
	Sequence conflict	12	1	I → T in AAC47125. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P52015 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: D5BD5E32A32942A7	FASTA	171	18,401
	10 20 30 40 50 60 MSRPRVFFDI TIAGKPTGRI VMELYNDIVP KTAENFRALC TGEKGVGKSG KPLHFKGSKF 70 80 90 100 110 120 HRIIPEFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT GPGVLSMANA GPNTNGSQFF 130 140 150 160 170 LCTVKTAWLD GKHVVFGRVV EGLDIVSKVE GNGSSSGTPK SECLIADCGQ L

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.
[3]	"Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing." Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R. Electrophoresis 18:557-562(1997) [PubMed: 9150941] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-13. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U27559 mRNA. Translation: AAC47125.1. AL032663 Genomic DNA. Translation: CAA21760.1.
PIR	T27371.
RefSeq	NP_506749.1. NM_074348.6.
UniGene	Cel.6641.
3D structure databases
ProteinModelPortal	P52015.
SMR	P52015. Positions 1-171.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24704N.
MINT	MINT-1105763.
STRING	P52015.
2D gel databases
Siena-2DPAGE	P52015.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y75B12B.2.1; Y75B12B.2.1; Y75B12B.2. Y75B12B.2.2; Y75B12B.2.2; Y75B12B.2.
GeneID	180027.
KEGG	cel:Y75B12B.2.
UCSC	Y75B12B.2.1. c. elegans.
Organism-specific databases
CTD	180027.
WormBase	Y75B12B.2; CE20371; WBGene00000883; cyn-7.
Phylogenomic databases
eggNOG	meNOG15253.
GeneTree	EMGT00050000000009.
HOGENOM	HBG610621.
InParanoid	P52015.
OMA	YFDMTID.
PhylomeDB	P52015.
Gene expression databases
ArrayExpress	P52015.
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	K01802.
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	907800.

Entry information

Entry name

CYP7_CAEEL

Accession

Primary (citable) accession number: P52015

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project