DPP_GIAIN
ID DPP_GIAIN Reviewed; 761 AA.
AC Q95WU5; A8BCK9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Dipeptidyl-peptidase 4;
DE EC=3.4.14.-;
DE AltName: Full=Dipeptidyl-aminopeptidase;
DE AltName: Full=Dipeptidylpeptidase IV;
DE Short=DPP IV;
DE Flags: Precursor;
GN Name=DPP;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 256-266, SUBCELLULAR
RP LOCATION, INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=WB1267;
RX PubMed=12049634; DOI=10.1042/bj20020025;
RA Touz M.C., Nores M.J., Slavin I., Piacenza L., Acosta D., Carmona C.,
RA Lujan H.D.;
RT "Membrane-associated dipeptidyl peptidase IV is involved in encystation-
RT specific gene expression during Giardia differentiation.";
RL Biochem. J. 364:703-710(2002).
CC -!- FUNCTION: May be involved in metabolism of dipeptides or may affect
CC host defense mechanisms. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:12049634}.
CC Note=Associated with trophozoite membrane.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle, but
CC expression is slightly decreased during encystation.
CC {ECO:0000269|PubMed:12049634}.
CC -!- INDUCTION: Expression increased in response to the protease inhibitor
CC bestatin. {ECO:0000269|PubMed:12049634}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; AF293412; AAK97082.1; -; Genomic_DNA.
DR RefSeq; XP_001707929.1; XM_001707877.1.
DR AlphaFoldDB; Q95WU5; -.
DR ESTHER; giain-Q95WU5; Prolyl_oligopeptidase_S9.
DR MEROPS; S09.056; -.
DR GeneID; 5700838; -.
DR KEGG; gla:GL50803_006148; -.
DR VEuPathDB; GiardiaDB:DHA2_6148; -.
DR VEuPathDB; GiardiaDB:GL50581_2060; -.
DR VEuPathDB; GiardiaDB:GL50803_006148; -.
DR eggNOG; KOG2100; Eukaryota.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Membrane; Protease;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..761
FT /note="Dipeptidyl-peptidase 4"
FT /id="PRO_0000420611"
FT ACT_SITE 622
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 706
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 738
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 761 AA; 87648 MW; 620D4D34A2A114EA CRC64;
MTLSAWIILV TLAMASVLTP EDNVRLRRLT AYVANADASI VLLTYTEYEE GTNHGNSMLW
RINDPLEAEY PFDPDDISLL NAERVCPELV GVGDLQYSTH NQAFYFTAQG PDGTSQVYSY
NHKLETCTQI SFLPISVSNL KVSPKGNSVL FSAEIFVYPN NHASVDDPLN FAHDEFARIQ
ARPYKAFAYE QLYTRHWDED ILPSQYRHLF AARLERSSEY DDDYVRITVD NSIDLMPRFD
GDCPMRPFAD ASSYTFDSHG RYVAFVTQVG STAAFYTNDS IWITDLQQFL DAKKPVRDVV
LPLRCATCWN KARDQRPAFS YDGIFLYYAS MDEEQSESDL LRLRKQNVSD LFEYDCDSLF
CGPVTGEGVF NLTAGVFDRS IGQFIIPTDS TEDSIYILAE DHARTNLFRY NEESSTVTRL
TYNGTLGSLL YLRHNKIFLA TMSSYTRPTD LVMLDLTVAT EFTATRDPSD TMKDDLIKIS
YLTDLNRQRL RHIDELQEPE EFYLPSKSFP DQYVHSWYFA PANLRDSHEY PLILYVHGGP
ESPWANSWSY RWNPQLIAAR GYGVLATNFH GSSSFGEVFQ KSVRGNWYSY PLEDIMDAWS
NIYTHADKAY LSREKVCAMG ASFGATFMNY MNSHVNNVTC YVTHDGVFDT MCNALETDEL
FFPVRELGGF LLDEQVDNQQ LYEKWNPARF VENMSAPMLV IHGQKDYRIQ VYHGISLFQA
LRLRGIKTKL VYFPTQSHWV WQPQESLFWH TQVFDWLDTY L