ID   A0A3B3WH94_9TELE        Unreviewed;       819 AA.
AC   A0A3B3WH94;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE            EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000002082.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000002082.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- 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   AlphaFoldDB; A0A3B3WH94; -.
DR   Ensembl; ENSPMET00000013115.1; ENSPMEP00000002082.1; ENSPMEG00000003152.1.
DR   Proteomes; UP000261480; Unplaced.
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; 1.
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:SF193; DIPEPTIDYL PEPTIDASE 9; 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;
FT   DOMAIN          5..120
FT                   /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19520"
FT   DOMAIN          154..526
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          619..819
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   819 AA;  93825 MW;  412D196BE8A1F322 CRC64;
     TLMPEEKSKL FPFFVEKHSW EGLRDIIHCS RKYSGMIANK APHDFQFVQK TDENGPHSHR
     LYYLGNRENS LLYSEIPKKV RKEALLVLSW KQMLDHFQAT PHQGAYSREE ELLRERKRLG
     AFGITSYDYH YKMGLFLFQA SNSLFYCQDG GNNGFIVSTS QCSGTRMDPK ICPGHPDFIA
     FINNNDLWIA NIKTGEERRL TYCHKGLDNV KEDPRSAGVA TFVIQEEFDR FTGYWWSPSA
     AADPDGGKTL HLLYEEVDET EVEIIHVPSP ALEERKADAY RYPRTGKVGH FSSIISTQDK
     ELVVPFSTLF PRTEYMARAG WTIDGKYGWA VLLDRSQKKL QLVLLPPALF IPITEDSTLR
     QDSLEAVPSC TQPYIIYEET TDVWINVHDI FYPFIQTTED EFTFIWVNES KTGFSHLYKI
     TSLLQPDFFF FSGNFKCAIK EEVTLTSGEW EVLSRHGSKI WVNEGTKLVY FQGTRDTPLE
     HHLYVVSYES PGDVVRLTKP GFSHCCSVSQ NFDFFVSHYS NVSTPPCVHL YKLTSLEDDP
     LRVVPEFWAS LMEPPGCPGD YNPPEIFDFP GKSGFQLYGM VYKPHNLQPG RKHPTVLFVY
     GGPQVQLVNN SFKGMKYLRL NTLASLGYAV VVIDGRGSCQ RGLEFEGALK NKMGQVEIED
     QVEGLQYVAE KFNFVDLSRV AIHGWSYGGF LSLMGLIQRP NIFKLAIAGA PVTVWMAYDT
     GYTERYMDVP ENNQQGYEEG SVALHVDKLP SEPNRLLILH GFLDENVHFF HTNFLVSQII
     RAGKPYQLQV YPNERHSIRC PESGEHYEIM LLHFLQQYL
//