ID A6MJH7_PSEAU Unreviewed; 753 AA.
AC A6MJH7;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Dipeptidyl peptidase 4 {ECO:0000256|ARBA:ARBA00014711};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE AltName: Full=Dipeptidyl peptidase IV {ECO:0000256|ARBA:ARBA00030567};
DE AltName: Full=T-cell activation antigen CD26 {ECO:0000256|ARBA:ARBA00031284};
OS Pseudechis australis (Mulga snake) (King brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX NCBI_TaxID=8670 {ECO:0000313|EMBL:ABQ63103.1};
RN [1] {ECO:0000313|EMBL:ABQ63103.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:ABQ63103.1};
RX PubMed=17608513; DOI=10.1021/pr0701613;
RA St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Diversity of toxic components from the venom of the evolutionarily
RT distinct black whip snake, Demansia vestigiata.";
RL J. Proteome Res. 6:3093-3107(2007).
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004655}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004655}. Cell junction
CC {ECO:0000256|ARBA:ARBA00004282}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004401}. Cell projection, invadopodium membrane
CC {ECO:0000256|ARBA:ARBA00004341}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004341}. Cell projection, lamellipodium
CC membrane {ECO:0000256|ARBA:ARBA00004485}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004485}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR EMBL; EF187036; ABQ63103.1; -; mRNA.
DR AlphaFoldDB; A6MJH7; -.
DR ESTHER; oxysu-a6mjh2; DPP4N_Peptidase_S9.
DR MEROPS; S09.003; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR040522; DPPIV_rep.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF128; DIPEPTIDYL PEPTIDASE 4; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF18811; DPPIV_rep; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 2: Evidence at transcript level;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..54
FT /note="Dipeptidyl peptidase 4 low complexity region"
FT /evidence="ECO:0000259|Pfam:PF18811"
FT DOMAIN 102..467
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 549..751
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 753 AA; 86495 MW; DD44865FE963F867 CRC64;
MKTVVKCLLG LLALGVIITA IVVPVVLLTR DDSDTRRKFS LEDYLNNDFQ YKSYNVRWMS
GHEYVYTNQN NVFLYNIDDG KESIILSNNT LENWNNSVAI LSPDKNFALL RYSYEKVWRH
SYTASYHIYD LNNRTIITEN PLPTTIQYIS WSPAGHKLAY VYRNNVYVKT TPNAKPVEIT
ENGAENKILN GLADWVYEEE MFGTHSALWW SPSGRFLAFA EINDTEVPLI EYSFYSEDTL
QYPKTIKIPY PKAGATNPTI RLFVVDILTL PQKNISEIVA PSSIISGDHY LSVVTWVTDE
RICLQWLRRI QNFSMLTICD YSSNVWQCPK NREHLEESKT GWVGRFQPSE PYFASDKISY
YKIISDSQGY NHIHYTDSTG NVKPITSGKW EVISIAAVTN NSLYFISNEF DGRPGGRHLY
KVDLKHDLKK TCITCDPNEE ACQYFSVSFS TDARYYKLNC YGPGLPYFTL QNSKTDKAIK
NLENNDNLKN VLKEIQMPSK RLRNITLRGQ TYWYQMILPP NFDESKKYPL LIDVYAGPCS
QKADAAFRIN WSTYLASSEG IIVASFDGRG SGFQGDKILH AIYRRLGTYE VEDQISAAKL
FSEMSFVDKD RMAIWGWSYG GYVTSMALGA GSGVFKCGIA VAPVSRWQYY DSIYTERYMG
LPEKNDNLYF YENSTVMARA ENFQMVDYLL IHGTADDNVH FQQAAQISKA LVDAQVDFQA
MWYTDKDHGI EGHAHSHIYH HMSHFIKRCF KLP
//
