ID A0A340WMD1_LIPVE Unreviewed; 847 AA.
AC A0A340WMD1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN Name=DPP8 {ECO:0000313|RefSeq:XP_007448175.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007448175.1};
RN [1] {ECO:0000313|RefSeq:XP_007448175.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC Pro nor hydroxyproline.; EC=3.4.14.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001257};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR RefSeq; XP_007448175.1; XM_007448113.1.
DR AlphaFoldDB; A0A340WMD1; -.
DR GeneID; 103078890; -.
DR CTD; 54878; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR045785; Dpp_8/9_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF98; DIPEPTIDYL PEPTIDASE 8; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF19520; Dpp_8_9_N; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT DOMAIN 9..162
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 176..594
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 723..839
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 847 AA; 97397 MW; DE299E7CFB9C07F2 CRC64;
MWKRSEQMKI QSGKCNMAAA METEQLGVEI FETAECEENI ESQDRPKLEP FYVERYSWSQ
LKKLLADTRK YHGYMMAKAP HDFMFVKRND PDGPHSDRIY YLAMSGENRE NTLFYSEIPK
TINRAAVLML SWKPLLDLFQ ATLDYGMYSR EEELLRERKR IGTVGIASYD YHQGSGTFLF
QAGSGIYHVK DGGPQGFTQQ PLRPNLVETS CPNIRMDPKL CPADPDWIAF IHSNDIWISN
IVTREERRLT YVHNELANME EDPRSAGVAT FVLQEEFDRY SGYWWCPEAE TTPSGSKILR
ILYEENDESE VEIIHVTSPM LETRRADSYP KPKTGTANPK VTFKMSEILI DAEGRLIDVI
DKELIQPFEI LFEGVEYIAR AGWTPEGKYS WAILLDRSQT RLQIVLISPE LFIPVEDDAM
ERQRLIESVP DSVTPLIIYE ETTDIWINIH DIFHVFPQSH EDEIEFIFAS ECKTGFRHLY
KITSILKESK YKRSSGGLPA PSDFKCPVKE EIAITSGEWE VLGRHGSNIQ VDEVRKLVYF
EGTKDSPLEH HLYVVSYVNP GEVTRLTDRG YSHSCCISRH CDFFISKYSN QKNPHCVSLY
KLSSPEDDPT CKTKEFWATI LDSAGPLPDY TPPEIFSFES TTGFTLYGML YKPHDLQPGK
KYPTVLFIYG GPQVQLVNNR FKGIKYFRLN TLASLGYVVV VIDNRGSCHR GLKFEGAFKY
KMVAIAGAPV TLWIFYDTGY TERYMGHPDQ NEQGYYLGSV AMQAEKFPSE PNRLLLLHGF
LDENVHFAHT SILLSFLVRA GKPYDLQIYP QERHSIRVPE SGEHYELHLL HYLQENLGSR
IAALKVI
//
