ID A0A3Q1FN19_9TELE Unreviewed; 892 AA.
AC A0A3Q1FN19;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000018548.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000018548.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR AlphaFoldDB; A0A3Q1FN19; -.
DR STRING; 80966.ENSAPOP00000018548; -.
DR Ensembl; ENSAPOT00000028165.1; ENSAPOP00000018548.1; ENSAPOG00000021934.1.
DR GeneTree; ENSGT00940000158174; -.
DR InParanoid; A0A3Q1FN19; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000257200; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 34..160
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 172..599
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 691..892
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 892 AA; 101592 MW; 476AF830FC37C066 CRC64;
MHRVKRLKIE DKTEDRQESI REALAGMTGV DELSDSTEVV EMDDVNLTQF QVEKHSWDGL
RKIIHNSRKS AGVVINKAPH DFQFIQKDET SPHSHRIYYL GMPYASRENA LLYSDIPKKI
RKDALLVLTW KPMLDHFQAS PHHGGFSREE ELLRERKRLG VSGITSYDHH RPSGLFLFQA
NSSLYYCRDG GNNSFITSPV NPVEIKSQNS GTRMDPKICP GNPNFIGFIN NNDIWVTSIE
TGEEKRLTFC HKGINNPKED TKSAGVATFV TQEEFDRFTG YWWCPAAREE PDGGKTLQIL
YEEVDESEVE IIHVPSPALE ERKTDVYRYP RAGSKNPDIT LKIAEIRTDD LGKIVSTQEK
ELPVSFSSLF PNAEYITRAG WTKDGRYAWV VMMDRRQQNL QLVLLPPALF IPAHQDETRR
RESLEALGDA VHPFIIYQET SDIWINVHDI FHPFIQTSDD EITFITVNES KTGFCHLYKI
TSVLQRGSYH WADGYTHSED DFKCPVKEEV TVTSGEWEVL ANHGAKRSSS PQIWVDEATK
LVYFQGTKDS PLEHHLYVVS YDSPGEIVRL TKPGFSHSCS VSQTFDMFIS HYSSLTCPPC
VHIYKLNGSD SDPLHKEPHF WASMMEASGF PFDSTPPEIF SFTGKSGFEL YGMLYKPQKL
VPGRKHPTVV FVYGGPQVQL VNNSYKGVKY LRLSTLAGLG YVVLVIDGRG SCQRGLKFEG
AVKDKMGQVE IEDQVEGLHY VAEKYKFVDL NRVAIHGWSY GGFLSLMGLV HKPDIFKVAI
AGAPVTLWMA YDTGYTERYL DTPEKNQKGY EACSVALHVD KLPNEPNRLL ILHGFLDENV
HFFHTNFLVS QLIRAGKPYS LQVYPNERHS IRCPESGEHY EITLLHFLQQ NL
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