dpf-3 Dipeptidyl Peptidase Four (IV) family [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: dpf-3
Official Full Name: Dipeptidyl Peptidase Four (IV) family
Primary source: WormBase:WBGene00001056
Locus tag: CELE_K02F2.1
See related: AllianceGenome:WB:WBGene00001056
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 dipeptidyl-peptidase activity. Predicted to be involved in proteolysis. Human ortholog(s) of this gene implicated in primary immunodeficiency disease. Orthologous to human DPP8 (dipeptidyl peptidase 8) and DPP9 (dipeptidyl peptidase 9). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See dpf-3 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 20

Sequence:: Chromosome: I; NC_003279.8 (6838354..6843343)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protease-mediated processing of Argonaute proteins controls small RNA association.
Title: Protease-mediated processing of Argonaute proteins controls small RNA association.

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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

K02F2.1 (e-PCR)
- UniSTS:311370

K02F2.2 (e-PCR)
- UniSTS:311371

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables dipeptidyl-peptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type peptidase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Dipeptidyl Peptidase Four (IV) family

NP_491956.1

Product from WormBase gene class dpf;
Confirmed by transcript evidence

NP_491957.1

Product from WormBase gene class dpf;
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_003279.8 Reference assembly

Range

6838354..6843343

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_059555.2 → NP_491956.1 Dipeptidyl Peptidase Four (IV) family [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_491956.1

Status: REVIEWED

UniProtKB/TrEMBL

H2KZK7

Conserved Domains (4) summary

COG1506
Location:621 → 902

DAP2; Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]

pfam00326
Location:710 → 918

Peptidase_S9; Prolyl oligopeptidase family

pfam00930
Location:249 → 578

DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region

cl00137
Location:388 → 447

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
NM_059556.5 → NP_491957.1 Dipeptidyl Peptidase Four (IV) family [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_491957.1

Status: REVIEWED

UniProtKB/TrEMBL

Q965K3

Conserved Domains (4) summary

COG1506
Location:617 → 898

DAP2; Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]

pfam00326
Location:706 → 914

Peptidase_S9; Prolyl oligopeptidase family

pfam00930
Location:245 → 574

DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region

cl00137
Location:384 → 443

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...