DPF2_CAEEL
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 03-AUG-2022, entry version 133.
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; -.
DR ESTHER; caeel-C27C12.7; DPP4N_Peptidase_S9.
DR MEROPS; S09.A74; -.
DR iPTMnet; Q18253; -.
DR EPD; Q18253; -.
DR PaxDb; Q18253; -.
DR PeptideAtlas; Q18253; -.
DR PRIDE; 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 CTD; 181579; -.
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; YTFPVYN; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; Q18253; -.
DR PRO; PR:Q18253; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001055; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 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
