GenomeNet

Database: UniProt
Entry: A6MJI0_HOPST
LinkDB: A6MJI0_HOPST
Original site: A6MJI0_HOPST 
ID   A6MJI0_HOPST            Unreviewed;       753 AA.
AC   A6MJI0;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 45.
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   Hoplocephalus stephensii (Stephens' banded snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Hoplocephalus.
OX   NCBI_TaxID=196418 {ECO:0000313|EMBL:ABQ63106.1};
RN   [1] {ECO:0000313|EMBL:ABQ63106.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Venom gland {ECO:0000313|EMBL:ABQ63106.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF187039; ABQ63106.1; -; mRNA.
DR   AlphaFoldDB; A6MJI0; -.
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          36..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;  86405 MW;  FC23DF104128566B CRC64;
     MKTVVKCLLG LLALGVIITA IVVPVVLLTR DDSDIRRKFS LEDYLNNDFQ YKSYNVRWMS
     GHEYVYTNQN NVFLYNIDDG KETVILSNNT LENWNNSVAI LSPDKKFALL RYSYEKVWRH
     SYTASYHIYD LNNRTIITEN PLPTTIQYIS WSPAGHKLAY VYCNNVYVKT TPNAKPVEIT
     ENGAENKILN GLADWVYEEE MFGTHSALWW SPSGRFLAFA EINDTEVPLI EYSFYSEDTL
     QYPKTIKIPY PKAGATNPTI RLFVVDILAL PEKNISEIVA PSSIISGDHY LSVVTWVTDE
     RICLQWLRRI QNFSMLTICD YSSNVWQCPK NREHPEESKT GRVGRFQPSE PYFASDKISY
     YKIISDSQGY NHIHYTDSTG NVKPITSGKW EVISIAAVTN NTLYFISNEF DGRPGGRHLY
     KVDLKHDLKK TCITCDPNEE ACQYFSVSFS TDARYYKLNC YGPGMPYFTL QNSKTDKAIK
     ILENNDNLKN VLKEIQMPSK RLRNITLHGQ 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
//
DBGET integrated database retrieval system