DPF1_CAEEL
ID DPF1_CAEEL Reviewed; 799 AA.
AC Q7JKY3; O18119;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Dipeptidyl peptidase family member 1;
DE EC=3.4.14.-;
GN Name=dpf-1; ORFNames=T23F1.7;
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], AND ALTERNATIVE SPLICING.
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 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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-512, 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.2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q7JKY3-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q7JKY3-2; Sequence=VSP_020298;
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
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DR EMBL; Z81129; CAB03411.1; -; Genomic_DNA.
DR EMBL; Z81129; CAB03412.1; -; Genomic_DNA.
DR PIR; T25173; T25173.
DR PIR; T25174; T25174.
DR RefSeq; NP_506850.1; NM_074449.3. [Q7JKY3-1]
DR RefSeq; NP_506851.1; NM_074450.4. [Q7JKY3-2]
DR AlphaFoldDB; Q7JKY3; -.
DR SMR; Q7JKY3; -.
DR STRING; 6239.T23F1.7b; -.
DR ESTHER; caeel-T23F1.7; DPP4N_Peptidase_S9.
DR MEROPS; S09.A76; -.
DR iPTMnet; Q7JKY3; -.
DR EPD; Q7JKY3; -.
DR PaxDb; Q7JKY3; -.
DR EnsemblMetazoa; T23F1.7a.1; T23F1.7a.1; WBGene00001054. [Q7JKY3-2]
DR EnsemblMetazoa; T23F1.7b.1; T23F1.7b.1; WBGene00001054. [Q7JKY3-1]
DR GeneID; 180042; -.
DR KEGG; cel:CELE_T23F1.7; -.
DR UCSC; T23F1.7a; c. elegans. [Q7JKY3-1]
DR CTD; 180042; -.
DR WormBase; T23F1.7a; CE21195; WBGene00001054; dpf-1. [Q7JKY3-2]
DR WormBase; T23F1.7b; CE21196; WBGene00001054; dpf-1. [Q7JKY3-1]
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000161291; -.
DR InParanoid; Q7JKY3; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; Q7JKY3; -.
DR PRO; PR:Q7JKY3; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001054; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q7JKY3; baseline and differential.
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 Alternative splicing; Aminopeptidase; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..799
FT /note="Dipeptidyl peptidase family member 1"
FT /id="PRO_0000248534"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..799
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 669
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 742
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 774
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 474..477
FT /evidence="ECO:0000250"
FT DISULFID 482..500
FT /evidence="ECO:0000250"
FT DISULFID 689..794
FT /evidence="ECO:0000250"
FT VAR_SEQ 151..170
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020298"
SQ SEQUENCE 799 AA; 91365 MW; 421180047516E8BE CRC64;
MTAEADLLEG YDEELGGNES QKRDCKGITT AIVVVLLILV MIFAALVFFT PLFAAKSFGS
WRLNVSDLRS LRYPYAEFAF TDNNAVVMQS WEGVEIVEDG VSRLIFGREN GAEITPSADR
KYFAMMDHAP NPGMNPQNET FHLKIVNNNE RLNPLLPFEV EELFRELSDS RITYDIGLRK
EESVIQAFKW NGKFNDFVFV ESNKIYYQSS PEEEGLTRVS NGGEHTVDGL FDWIYEEEIF
GRKDAMWWST KGDQLAYASY DNHLTKNVSL KTYHRLEPYP IDTNFHYPKT FAKVLPTYTL
SIWNKKTEQS RQLDVQLKDS LSYHYLLAVK WLEINGTEQL VSVWTNRYQN EVALTICDWD
TAICRLEFEY KYASKRWVTH DDFHSITSFE DTLFFLLPHD KRDNAFQQVA SLRLSHGQLR
TPKFLNLGEY DVTSINGINK ETRTIFFHAA APKPSHRSLF SYSLADESRN SAYCISCSIK
NCTWAQAQMD DQMKTAIVSC KGPAAPHTAI VNLTRMDSDK KTEHANLLYD KTYQNRVEEA
GLPVIIKETI KISDDFDALI KLSIPKDIYN RDKHQAIPLI VHVYGGPNDQ NTKEATQIGI
EEVVASASQA AILRIDGRGS GGRGWKYRSA IYGQLGTVEV EDQIKAIKVV LRLYRHLLDA
RRVAVFGWSY GGFMTLSMVN EAPEQFFKCA VSVAPVTNFA YYDATYTERY MGDAPLESYS
DVTKKLDNFK STRLLLMHGL LDDNVHFQNS AILIDELQNR GVDFDLMVYP NQAHSLSSRT
SHVVGKMTHF LRQCFYTDK
