ID A0A3Q1K4S3_ANATE Unreviewed; 861 AA.
AC A0A3Q1K4S3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000026291.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000026291.2}
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; A0A3Q1K4S3; -.
DR STRING; 64144.ENSATEP00000026291; -.
DR Ensembl; ENSATET00000026714.2; ENSATEP00000026291.2; ENSATEG00000018179.2.
DR GeneTree; ENSGT00940000158174; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000265040; 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:UP000265040}.
FT DOMAIN 12..134
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 174..568
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 661..861
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 861 AA; 98231 MW; DED1147EE1E1D11D CRC64;
MTAVDGFLDS TEVVEMEDVP SQFFVEKHSW EGLRDIIHCS RKYSGMIANK APHDFQFVQK
KDENGPHSHR LYYLGMPYGS RENSLLYSEI PKKIQKEAHL VLSWKQMLDH FQATPHQGAY
SREEELLRER KRLGAFGITS YDYHAHTGLF LFQASNSLFY CQDGGNNGFI QSAPVKPVDI
KTQCSGTRMD PKICPGEPDF IAFINNNDLW IANIKTSEER RLTYCHKGLD NIKDDPKSAG
VATFVIQEEF DRFTGYWWSP SAVEDSNGGK TVYLLYEEVD ETEVEIIHVP SPALEERKAD
AYRYPRTGSK NPQATLKLSE IKTDHQGRIV RTQDKELVVP FTSLFPGTEY IARVGWTSDG
KYGWAVLLDR SQRKLQLVLL PPALFIPVTD DPVLRQESLE AVPSNTQPYI IYEETTDIWI
NVHDIFYPFI QTTDDEFTFI WINESKTGFS HLYKITSLLQ PGCYNWSEDY QHTEGDFKCA
IKEEVTLTSG EWEVLARHGS KIWVNEATKL VYFQGTKDTP LEHHLYVVSY DSPGDVVRLT
KPGFSHSCSV SQNFDFFVSH YSNVSTPPCV HVYKLISSEG DPMHVSPEFW ASMMESPGCP
GDYSPPEIFD FPGKSGFQLY GMVYKPHNLQ PGRKHPTVLF VYGGPQVQLV NNSFKGMKYL
RLNTLASLGY AVVVIDGRGS CQRGLEFEGA LKNKMGQVEI EDQVEGLQYV AEKFNFVDLS
RVAIHGWSYG GFLSLMGLIQ RPNIFKLAIA GAPVTVWMAY DTGYTERYMD VPDNNQQGYE
EGSVALHVDK LPSEPNRLLI LHGFLDENVH FFHTNFLVSQ IIRAGKPYQL QVYPNERHSI
RCPESGEHYE IMLLHFLQQY L
//
