cyn-4 Peptidyl-prolyl cis-trans isomerase 4 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: cyn-4
Official Full Name: Peptidyl-prolyl cis-trans isomerase 4
Primary source: WormBase:WBGene00000880
Locus tag: CELE_F59E10.2
See related: AllianceGenome:WB:WBGene00000880
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable ubiquitin protein ligase activity. Involved in feminization of hermaphroditic germ-line. Predicted to be located in nucleus. Predicted to be part of catalytic step 2 spliceosome. Is expressed in body wall musculature; germ line; intestine; pharynx; and uterus. Orthologous to human PPIL2 (peptidylprolyl isomerase like 2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See cyn-4 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 5

Sequence:: Chromosome: II; NC_003280.10 (10870779..10872611, complement)

Chromosome II - NC_003280.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003280.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

MOG-6 has a function distinct from that of prevailing cyclophilins and that its binding to MEP-1 is essential for germline sex determination.
Title: Roles of the C. elegans cyclophilin-like protein MOG-6 in MEP-1 binding and germline fates.

Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

F59E10.2 (e-PCR)
- UniSTS:321536

F59E10.3 (e-PCR)
- UniSTS:320996

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables peptidyl-prolyl cis-trans isomerase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin-protein transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in cell differentiation	IEA Inferred from Electronic Annotation more info
involved_in feminization of hermaphroditic germ-line	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein peptidyl-prolyl isomerization	IEA Inferred from Electronic Annotation more info
involved_in protein ubiquitination	IEA Inferred from Electronic Annotation more info
involved_in sex differentiation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of catalytic step 2 spliceosome	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Peptidyl-prolyl cis-trans isomerase 4

NP_496337.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003280.10 Reference assembly

Range

10870779..10872611 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_063936.7 → NP_496337.1 Peptidyl-prolyl cis-trans isomerase 4 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_496337.1

Status: REVIEWED

UniProtKB/Swiss-Prot

P52012, Q09548

Conserved Domains (2) summary

smart00504
Location:45 → 96

Ubox; Modified RING finger domain

cd01923
Location:281 → 440

cyclophilin_RING; cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal ...