Reviewed, UniProtKB/Swiss-Prot P52012 (CYP4_CAEEL)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase 4
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-4
    Cyclophilin mog-6
    Masculinisation of germline protein 6

Gene names

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

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. 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
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from electronic annotation. Source: InterPro 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...

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	65	U-box
	Domain	278 – 433	156	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	P52012-1 [UniParc]. Last modified July 15, 1999. Version 3. Checksum: 399967A6303989DE	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

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
EMBLGenBankDDBJ	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.
UniGene	Cel.18376
3D structure databases
HSSP	HSSP built from PDB template 1A58 based on UniProtKB Q27450.
ModBase	Search...
Genome annotation databases
Ensembl	F59E10.2.1; F59E10.2.1; F59E10.2; Caenorhabditis elegans. [Genome view] F59E10.2.2; F59E10.2.2; F59E10.2; Caenorhabditis elegans. [Genome view]
GeneID	174674.
KEGG	cel:F59E10.2.
NMPDR	fig|6239.3.peg.7329.
UCSC	F59E10.2.1. c. elegans.
Organism-specific databases
CTD	174674.
WormBase	WBGene00000880. cyn-4.
WormPep	F59E10.2. CE01596. [WorfDB]
Phylogenomic databases
OMA	GGESFWG.
Enzyme and pathway databases
BRENDA	5.2.1.8. 672.
Gene expression databases
ArrayExpress	P52012.
Family and domain databases
InterPro	IPR002130. PPIase_cyclophilin. IPR003613. Ubox_domain. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SMART	SM00504. Ubox. 1 hit. [Graphical view]
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 3, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project