ID   A0A2K6B5V2_MACNE        Unreviewed;       832 AA.
AC   A0A2K6B5V2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE            EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN   Name=DPP9 {ECO:0000313|Ensembl:ENSMNEP00000006788.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000006788.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000006788.1}
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}.
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DR   AlphaFoldDB; A0A2K6B5V2; -.
DR   STRING; 9545.ENSMNEP00000006788; -.
DR   Ensembl; ENSMNET00000030917.1; ENSMNEP00000006788.1; ENSMNEG00000027918.1.
DR   GeneTree; ENSGT00940000158174; -.
DR   OMA; VTHMTPQ; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000027918; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR   GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0070269; P:pyroptosis; IEA:Ensembl.
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:SF109; 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; 2.
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:UP000233120}.
FT   DOMAIN          51..164
FT                   /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19520"
FT   DOMAIN          175..391
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          399..539
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          632..832
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          16..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  94714 MW;  F2C691AB5E24A19A CRC64;
     MRKVKKLRLD KENTGSWRSF SLNSEGAERM ATTGTPTADR GDAAATDDPA ARFQVQKHSW
     DGLRSIIHGS RKYSGLIVNK APHDFQFVQK TDESGPHSHR LYYLGMPYGS RENSLLYSEI
     PKKVRKEALL LLSWKQMLDH FQATPHHGVY SREEELLRER KRLGVFGITS YDFHSESGLF
     LFQASNSLFH CRDGGKNGFM VSPMKPLEIK TQCSGPRMDP KICPADPAFF SFINNSDLWV
     ANIETGEERR LTFCHQGLSN VLDDPKSAGV ATFVIQEEFD RFTGYWWCPT ASWEGSEGLK
     TLRILYEEVD ESEVEVIHVP SPALEERKTD SYRYPRTGSK NPKIALKLAE FQTDSQGKIV
     STQEKELVQP FSSLFPKVEY IARAGWTRDG KVHDIFYPFP QSEGEDELCF LRANECKTGF
     CHLYKVTAVL KSQGYDWSEP FSPREDEFKC PIKEEIALTS GEWEVLARHG SKIWVNEETK
     LVYFQGTKDT PLEHHLYVVS YEAAGEIVRL TTPGFSHSCS MSQNFDMFVS HYSSVSTPPC
     VHVYKLSGPD DDPLHKQPRF WASMMEAASC PPDYVPPEIF HFHTRSDVRL YGMIYKPHAL
     QPGKKHPTVL FVYGGPQVQL VNNSFKGIKY LRLNTLASLG YAVVVIDGRG SCQRGLRFEG
     ALKNQMGQVE IEDQVEGLQF VAEKYGFIDL SRVAIHGWSY GGFLSLMGLI HKPQVFKVAI
     AGAPVTVWMA YDTGYTERYM DVPENNQHGY EAGSVALHVE KLPNEPNRLL ILHGFLDENV
     HFFHTNFLVS QLIRAGKPYQ LQIYPNERHS IRCPESGEHY EVTLLHFLQE YL
//