ID   DPF2_CAEEL              Reviewed;         829 AA.
AC   Q18253;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Dipeptidyl peptidase family member 2;
DE            EC=3.4.14.-;
GN   Name=dpf-2; ORFNames=C27C12.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   FUNCTION.
RA   Yoshina S., Gengyo-Ando K., Mitani S., Iino Y., Inoue H., Takahashi K.;
RT   "Dipeptidyl peptidase IV-like protease family is essential for control of
RT   distal tip cell migration in C. elegans.";
RL   (In) Proceedings of the 15th international C. elegans meeting, pp.402-402,
RL   Los Angeles (2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC       (By similarity). Essential for control of distal tip cell migration.
CC       {ECO:0000250, ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z69883; CAA93743.1; -; Genomic_DNA.
DR   PIR; T19514; T19514.
DR   RefSeq; NP_510461.1; NM_078060.6.
DR   AlphaFoldDB; Q18253; -.
DR   SMR; Q18253; -.
DR   STRING; 6239.C27C12.7.2; -.
DR   ESTHER; caeel-C27C12.7; DPP4N_Peptidase_S9.
DR   MEROPS; S09.A74; -.
DR   GlyCosmos; Q18253; 7 sites, No reported glycans.
DR   iPTMnet; Q18253; -.
DR   EPD; Q18253; -.
DR   PaxDb; 6239-C27C12-7; -.
DR   PeptideAtlas; Q18253; -.
DR   EnsemblMetazoa; C27C12.7.1; C27C12.7.1; WBGene00001055.
DR   GeneID; 181579; -.
DR   KEGG; cel:CELE_C27C12.7; -.
DR   UCSC; C27C12.7; c. elegans.
DR   AGR; WB:WBGene00001055; -.
DR   WormBase; C27C12.7; CE05324; WBGene00001055; dpf-2.
DR   eggNOG; KOG2100; Eukaryota.
DR   GeneTree; ENSGT00940000160454; -.
DR   HOGENOM; CLU_006105_4_0_1; -.
DR   InParanoid; Q18253; -.
DR   OMA; DKYKATT; -.
DR   OrthoDB; 2876738at2759; -.
DR   PhylomeDB; Q18253; -.
DR   Reactome; R-CEL-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   PRO; PR:Q18253; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001055; Expressed in material anatomical entity and 4 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW   Membrane; Protease; Reference proteome; Serine protease; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..829
FT                   /note="Dipeptidyl peptidase family member 2"
FT                   /id="PRO_0000248535"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..829
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        691
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        768
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        800
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        754
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        514..533
FT                   /evidence="ECO:0000250"
FT   DISULFID        711..821
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   829 AA;  94387 MW;  B3F76F6DC12E44A5 CRC64;
     MENDNYDVEE QGCSVFNGKH GYFARSCCVV FILIICVIFV FSVIFTFMQN PINLNSDNGF
     NQTSGNTSSL EATTLKPKFS SLMTTTRRFT FEQLFSGKQF LVDYYDYIWL PDGSFVQMND
     DFTIRKQMKK IPLGSSVAEP FFNNGEYVKA LSSNMKYAYG SKKVNELWRH SAEYLYHIVK
     INNKTVSTEQ WHVGPEENSL IQAFYWNPNA SSNDFVYVHN YNLYYQKDPE KPDGAIQLTV
     GGSTFNRFGL ANWLYEEEIL EASSAVWWSP SGRYVSYLRF DDREVNRIFL PKYTDDDSYV
     EYFELPYPKA GVQNNTLVTQ YIWDSENHKI VETAPPNELS AANGDYYVLT NKWITMPRNG
     SDLGEERLVT VWANRDQNHV YFSLCNEQDC VMALSFQFSI DNRQLWVSPK DVRGVFPTET
     GFLTVLPHKH DDGNIYNHVA HVELDGTGTG KITKWIGENF DVILVLGYSS KIDALTFSAY
     GDGVGEFSTY IVREAMYSNK KTTLQKVTDQ FEDCKTLGSQ SADPTGQRIV VQCEKPFDNT
     RLYLVDVVDT TKKIMLEGGT KAVIPFDVPN MKFGKLKLPS GIDGHYMMLT PANLLDGAKI
     PLLLDIYGGP DSKQVFQKTP TAHAIQIVSQ YDIAYARIDV RGTGGRGWDV KEAVYRKLGD
     AEVVDTLDMI RAFINTFGFI DEDRIAVMGW SYGGFLTSKI AIKDQGELVK CAISIAPVTD
     FKYYDSAYTE RYLGQPAENL QGYINTNVIP HARNVTNVKY LLAHGERDDN VHYQNSARWS
     EALQQNGIHF TQLVYANEAH SLSHKLFHLY GEVQRFLMND CFKSNLDLL
//