DPF6_CAEEL
ID DPF6_CAEEL Reviewed; 740 AA.
AC P34422; Q8MQ47; Q8MQ48; Q8MQ49;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Dipeptidyl peptidase family member 6;
DE EC=3.4.14.-;
GN Name=dpf-6; ORFNames=F44B9.1;
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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).
CC -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC (By similarity). Essential for control of distal tip cell migration.
CC {ECO:0000250}.
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=3;
CC Name=a;
CC IsoId=P34422-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34422-2; Sequence=VSP_007095, VSP_007096;
CC Name=c;
CC IsoId=P34422-3; Sequence=VSP_007097, VSP_007098;
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
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DR EMBL; FO080400; CCD63439.1; -; Genomic_DNA.
DR EMBL; FO080400; CCD63440.1; -; Genomic_DNA.
DR EMBL; FO080400; CCD63441.1; -; Genomic_DNA.
DR PIR; S44807; S44807.
DR RefSeq; NP_741240.1; NM_171203.4. [P34422-1]
DR RefSeq; NP_741241.1; NM_171204.3.
DR RefSeq; NP_741242.1; NM_171205.4. [P34422-2]
DR AlphaFoldDB; P34422; -.
DR SMR; P34422; -.
DR BioGRID; 41338; 1.
DR STRING; 6239.F44B9.1a; -.
DR ESTHER; caeel-f44b9.1; Prolyl_oligopeptidase_S9.
DR MEROPS; S09.A77; -.
DR EPD; P34422; -.
DR PaxDb; P34422; -.
DR PeptideAtlas; P34422; -.
DR PRIDE; P34422; -.
DR EnsemblMetazoa; F44B9.1a.1; F44B9.1a.1; WBGene00001059. [P34422-1]
DR EnsemblMetazoa; F44B9.1b.1; F44B9.1b.1; WBGene00001059. [P34422-2]
DR EnsemblMetazoa; F44B9.1c.1; F44B9.1c.1; WBGene00001059. [P34422-3]
DR GeneID; 176132; -.
DR KEGG; cel:CELE_F44B9.1; -.
DR UCSC; F44B9.1b; c. elegans. [P34422-1]
DR CTD; 176132; -.
DR WormBase; F44B9.1a; CE30989; WBGene00001059; dpf-6. [P34422-1]
DR WormBase; F44B9.1b; CE30990; WBGene00001059; dpf-6. [P34422-2]
DR WormBase; F44B9.1c; CE30991; WBGene00001059; dpf-6. [P34422-3]
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; P34422; -.
DR OMA; TIPPYWE; -.
DR OrthoDB; 893792at2759; -.
DR PhylomeDB; P34422; -.
DR PRO; PR:P34422; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001059; Expressed in pharyngeal muscle cell (C elegans) and 3 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: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 Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
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..740
FT /note="Dipeptidyl peptidase family member 6"
FT /id="PRO_0000122435"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..740
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 516
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 604
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 636
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 535..658
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007095"
FT VAR_SEQ 230..234
FT /note="KAITM -> MYNFR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007096"
FT VAR_SEQ 573
FT /note="D -> E (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_007097"
FT VAR_SEQ 574..740
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_007098"
SQ SEQUENCE 740 AA; 83500 MW; F04FCB0E7E93128A CRC64;
MLFLPILILN LLIITHAIDI IPREVLFQDP KYSSVSLSPD AKQVGYVAPD ENGIRNVFTR
CSSCSYSRQV TFETEHPILN YVWTAIPDVI LFTQDNHGDE NTRIYKKNIS ATAIAADKTQ
RVVISEKPMV KAMILSNNLI SETVLIGMND ENPALHNIYA FNCQTDELKL VLQNRRFSIF
FFDNDLNVRL ASEEGPDGEM IYYRPRSNEG ARTTEQNTWV EYLRIQHDDK AITMPITFDK
SNNFMYWIMG DGSDLGNLVV FPFEDPQQKE ILYTAQRAQI GNVLIHPTDK TLLAVTEVYH
KPELFVANET FMEDLQYLVN MKPSGSMNIV SMSIDMSTWL VTYSSSDEPY DIYLYRRWNK
KAELFMSTRP ELKKYTLNKQ IGFDFRARDE MTIQAYLSLP PQAPLLKSSQ VPDGDRPYAN
LGMIPAVPQK MIVLVHGGPK ARDHYGFSPM NAWLTNRGYS VLQVNFRGST GFGKRLTNAG
NGEWGRKMHF DILDAVEFAV SKGIANRSEV AVMGGSYGGY ETLVALTFTP QTFACGVDIV
GPSNLISLVQ AIPPYWLGFR KDLIKMVGAD ISDEEGRQSL QSRSPLFFAD RVTKPIMIIQ
GANDPRVKQA ESDQFVAALE KKHIPVTYLL YPDEGHGVRK PQNSMEQHGH IETFLQQCLG
GETQPFQPGQ YNSSAIIKKI GIEGAAIARQ NLQIAQNQFA QQLPRGPVAP SIFYRPPVRA
QRVMLAPNQN VMNRIFPVQG
