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Protein

Dipeptidyl peptidase family member 2

Gene

dpf-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Removes N-terminal dipeptides sequentially from polypeptides (By similarity). Essential for control of distal tip cell migration.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei691 – 6911Charge relay systemBy similarity
Active sitei768 – 7681Charge relay systemBy similarity
Active sitei800 – 8001Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Protein family/group databases

ESTHERicaeel-C27C12.7. DPP4N_Peptidase_S9.
MEROPSiS09.A74.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase family member 2 (EC:3.4.14.-)
Gene namesi
Name:dpf-2
ORF Names:C27C12.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiC27C12.7; CE05324; WBGene00001055; dpf-2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2727CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei28 – 4821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini49 – 829781ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 829829Dipeptidyl peptidase family member 2PRO_0000248535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)2 Publications
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi514 ↔ 533By similarity
Disulfide bondi711 ↔ 821By similarity
Glycosylationi754 – 7541N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ18253.
PRIDEiQ18253.

Interactioni

Protein-protein interaction databases

STRINGi6239.C27C12.7.

Structurei

3D structure databases

ProteinModelPortaliQ18253.
SMRiQ18253. Positions 168-823.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000018328.
InParanoidiQ18253.
OMAiCAISIAP.
OrthoDBiEOG71CFKC.
PhylomeDBiQ18253.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR031245. FAP/Dpf2.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PANTHERiPTHR11731:SF111. PTHR11731:SF111. 1 hit.
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q18253-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENDNYDVEE QGCSVFNGKH GYFARSCCVV FILIICVIFV FSVIFTFMQN
60 70 80 90 100
PINLNSDNGF NQTSGNTSSL EATTLKPKFS SLMTTTRRFT FEQLFSGKQF
110 120 130 140 150
LVDYYDYIWL PDGSFVQMND DFTIRKQMKK IPLGSSVAEP FFNNGEYVKA
160 170 180 190 200
LSSNMKYAYG SKKVNELWRH SAEYLYHIVK INNKTVSTEQ WHVGPEENSL
210 220 230 240 250
IQAFYWNPNA SSNDFVYVHN YNLYYQKDPE KPDGAIQLTV GGSTFNRFGL
260 270 280 290 300
ANWLYEEEIL EASSAVWWSP SGRYVSYLRF DDREVNRIFL PKYTDDDSYV
310 320 330 340 350
EYFELPYPKA GVQNNTLVTQ YIWDSENHKI VETAPPNELS AANGDYYVLT
360 370 380 390 400
NKWITMPRNG SDLGEERLVT VWANRDQNHV YFSLCNEQDC VMALSFQFSI
410 420 430 440 450
DNRQLWVSPK DVRGVFPTET GFLTVLPHKH DDGNIYNHVA HVELDGTGTG
460 470 480 490 500
KITKWIGENF DVILVLGYSS KIDALTFSAY GDGVGEFSTY IVREAMYSNK
510 520 530 540 550
KTTLQKVTDQ FEDCKTLGSQ SADPTGQRIV VQCEKPFDNT RLYLVDVVDT
560 570 580 590 600
TKKIMLEGGT KAVIPFDVPN MKFGKLKLPS GIDGHYMMLT PANLLDGAKI
610 620 630 640 650
PLLLDIYGGP DSKQVFQKTP TAHAIQIVSQ YDIAYARIDV RGTGGRGWDV
660 670 680 690 700
KEAVYRKLGD AEVVDTLDMI RAFINTFGFI DEDRIAVMGW SYGGFLTSKI
710 720 730 740 750
AIKDQGELVK CAISIAPVTD FKYYDSAYTE RYLGQPAENL QGYINTNVIP
760 770 780 790 800
HARNVTNVKY LLAHGERDDN VHYQNSARWS EALQQNGIHF TQLVYANEAH
810 820
SLSHKLFHLY GEVQRFLMND CFKSNLDLL
Length:829
Mass (Da):94,387
Last modified:November 1, 1996 - v1
Checksum:iB3F76F6DC12E44A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69883 Genomic DNA. Translation: CAA93743.1.
PIRiT19514.
RefSeqiNP_510461.1. NM_078060.6.
UniGeneiCel.5433.

Genome annotation databases

EnsemblMetazoaiC27C12.7; C27C12.7; WBGene00001055.
GeneIDi181579.
KEGGicel:CELE_C27C12.7.
UCSCiC27C12.7. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69883 Genomic DNA. Translation: CAA93743.1.
PIRiT19514.
RefSeqiNP_510461.1. NM_078060.6.
UniGeneiCel.5433.

3D structure databases

ProteinModelPortaliQ18253.
SMRiQ18253. Positions 168-823.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.C27C12.7.

Protein family/group databases

ESTHERicaeel-C27C12.7. DPP4N_Peptidase_S9.
MEROPSiS09.A74.

Proteomic databases

PaxDbiQ18253.
PRIDEiQ18253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC27C12.7; C27C12.7; WBGene00001055.
GeneIDi181579.
KEGGicel:CELE_C27C12.7.
UCSCiC27C12.7. c. elegans.

Organism-specific databases

CTDi181579.
WormBaseiC27C12.7; CE05324; WBGene00001055; dpf-2.

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000018328.
InParanoidiQ18253.
OMAiCAISIAP.
OrthoDBiEOG71CFKC.
PhylomeDBiQ18253.

Miscellaneous databases

NextBioi914522.
PROiQ18253.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR031245. FAP/Dpf2.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PANTHERiPTHR11731:SF111. PTHR11731:SF111. 1 hit.
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
    Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
    Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  3. "Dipeptidyl peptidase IV-like protease family is essential for control of distal tip cell migration in C. elegans."
    Yoshina S., Gengyo-Ando K., Mitani S., Iino Y., Inoue H., Takahashi K.
    (In) Proceedings of the 15th international C. elegans meeting, pp.402-402, Los Angeles (2005)
    Cited for: FUNCTION.
  4. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.

Entry informationi

Entry nameiDPF2_CAEEL
AccessioniPrimary (citable) accession number: Q18253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.