Peptidyl-prolyl cis-trans isomerase 4 - Caenorhabditis elegans

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P52012 (CYP4_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase 4
Short name=PPIase 4
EC=5.2.1.8

Alternative name(s):
Cyclophilin mog-6
Cyclophilin-4
Masculinisation of germline protein 6
Rotamase 4

Gene names

Name:	cyn-4
Synonyms:	cyp-4, mog-6
ORF Names:	F59E10.2

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	523 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. Influences the hermaphrodite switch from spermatogenesis to oogenesis. Required for body-wall muscle cell development. Ref.1 Ref.5
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with mep-1.
Tissue specificity	Exclusively in the larval body-wall striated muscle cells. Ref.1
Developmental stage	Abundantly expressed in the early larval stages, lower levels at later larval and adult stages. Ref.1
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily. Contains 1 PPIase cyclophilin-type domain. Contains 1 U-box domain.

Ontologies

Keywords
Biological process	Differentiation Sexual differentiation
Molecular function	Developmental protein Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase feminization of hermaphroditic germ-line Inferred from mutant phenotype Ref.5. Source: WormBase germ cell development Inferred from mutant phenotype. Source: WormBase protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell proliferation Inferred from mutant phenotype. Source: WormBase regulation of meiosis Inferred from mutant phenotype. Source: WormBase sex differentiation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB ubiquitin-protein ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mep-1	Q21502	3	EBI-3513766,EBI-319858

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

Peptidyl-prolyl cis-trans isomerase 4

PRO_0000064193

Regions

Domain

45 – 109

U-box

Domain

278 – 433

156

PPIase cyclophilin-type

Sequences

Sequence

Length

Mass (Da)

Tools

P52012 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: 399967A6303989DE
Show »

FASTA

523

58,534

        10         20         30         40         50         60 
MGKKQHQKDK LYLTTSEWKS IGGHKDDTGT RLQRAQFKRL PINHCSLSLL PFEDPVCARS 

        70         80         90        100        110        120 
GEIFDLTAIV PYLKKHGKNP CTGKPLVAKD LIHLKFDKGE DGKFRCPVTF RTFTDHSHIL 

       130        140        150        160        170        180 
AIATSGNVYS HEAVQELNLK RNHLKDLLTD VPFTRADIID LQDPNHLEKF NMEQFLHVKL 

       190        200        210        220        230        240 
DLKTSEEIKK EKDAMKDPKF YIRRMNNACK SVLDQLDKEY VPKKSSTETD ETADEINAAH 

       250        260        270        280        290        300 
YSQGKVAAGF TSTVMAPVTS NKAAVLDNDT VRYSRVKKNA FVRLVTNFGP LNLELFAPKV 

       310        320        330        340        350        360 
PKACENFITH CSNGYYNNTK FHRLIKNFML QGGDPTGTGH GGESIWDKPF SDEFISGFSH 

       370        380        390        400        410        420 
DARGVLSMAN KGSNTNGSQF FITFRPCKYL DRKHTIFGRL VGGQDTLTTI EKLETEEGTD 

       430        440        450        460        470        480 
VPMVSVVIMR AEVFVDPFEE AEKEVQAERA EILKKTSKDA ASLANKKAKE TATKPEAVGT 

       490        500        510        520 
GVGKYMKSAA AVNKRQGKME DVPLEAAKKT KFARAGLGDF SKW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A divergent multi-domain cyclophilin is highly conserved between parasitic and free-living nematode species and is important in larval muscle development." Page A.P., Winter A.D. Mol. Biochem. Parasitol. 95:215-227(1998) [PubMed: 9803414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Bristol N2.
[2]	"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] OF 255-435. Strain: Bristol N2.
[3]	"The sex determination gene mog-6 codes for a cyclophilin that interacts with MEP-1 in C. elegans." Pugnale P., Puoti A. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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.
[5]	"More mog genes that influence the switch from spermatogenesis to oogenesis in the hermaphrodite germ line of Caenorhabditis elegans." Graham P.L., Schedl T., Kimble J. Dev. Genet. 14:471-484(1993) [PubMed: 8111975] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U36187 mRNA. Translation: AAC06337.1. AF421146 mRNA. Translation: AAL27008.1. Z36949, Z46935 Genomic DNA. Translation: CAA85417.1. Z46935, Z36949 Genomic DNA. Translation: CAA87053.1.
PIR	T23003.
RefSeq	NP_496337.1. NM_063936.5.
UniGene	Cel.18376.
3D structure databases
ProteinModelPortal	P52012.
SMR	P52012. Positions 45-75, 276-454.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52012. 1 interaction.
STRING	P52012.
Proteomic databases
PRIDE	P52012.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F59E10.2; F59E10.2; F59E10.2.
GeneID	174674.
KEGG	cel:F59E10.2.
NMPDR	fig\|6239.3.peg.7329.
UCSC	F59E10.2.1. c. elegans.
Organism-specific databases
CTD	174674.
WormBase	F59E10.2; CE01596; WBGene00000880; cyn-4.
Phylogenomic databases
eggNOG	meNOG04886.
GeneTree	EMGT00050000002627.
HOGENOM	HBG324997.
InParanoid	P52012.
OMA	TNNSHIV.
PhylomeDB	P52012.
Gene expression databases
ArrayExpress	P52012.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. IPR003613. Ubox_domain. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KO	K10598.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SMART	SM00504. Ubox. 1 hit. [Graphical view]
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	885014.

Entry information

Entry name

CYP4_CAEEL

Accession

Primary (citable) accession number: P52012
Secondary accession number(s): Q09548

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 15, 1999
Last modified:	January 25, 2012
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

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents