ID A0A2Y9DHK8_TRIMA Unreviewed; 726 AA.
AC A0A2Y9DHK8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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};
GN Name=LOC101341317 {ECO:0000313|RefSeq:XP_004374728.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004374728.1};
RN [1] {ECO:0000313|RefSeq:XP_004374728.1}
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 -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR RefSeq; XP_004374728.1; XM_004374671.3.
DR AlphaFoldDB; A0A2Y9DHK8; -.
DR STRING; 127582.A0A2Y9DHK8; -.
DR GeneID; 101341317; -.
DR KEGG; tmu:101341317; -.
DR InParanoid; A0A2Y9DHK8; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000248480; 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; 2.
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; 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:UP000248480}.
FT DOMAIN 9..162
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 176..336
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 357..422
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 515..718
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 726 AA; 83258 MW; CDC0161E4104A06E CRC64;
MWKRSGQMKI QSGKCNMAAA METEQLGVEI FETAECEENI ESQDQPKLEP FYVERYSWSQ
LKKLLADTRK YHGYMMAKAP HDFMFVKRSD PDGPHSDRIY YLAMSGENRE NTLFYSEIPK
TINKAAVLML SWKPLLDLFQ ATLDYGMYSR EEELLRERKR IGTVGIASYD YHQGSGTFLF
QAGSGIYHVK DGGPQGFTQQ PLRPNLVETS CPNIRMDPKL CPADPDWIAF IHSSDIWVSN
IVTREERRLT YVHNELANME EDPRSAGVAT FVLQEEFDRY SGYWWCPTAE LAPSGGKILR
ILYEENDESE VEIIHVTSPM LETRRADAFR YPKTGTVPIG IHTHAGTDFL LLVFWQIQVD
EVRKLVYFEG TKDSPLEHHL YVVSYANPGE VTRLTDRGYS HSCCISGHCD FFISKYSNQK
NPHCVSLYKL SNTEDDPTCR TKEFWATILD SAGPLPDYTP PEIFSFESTT GFTLYGMLYK
PHDLQPGKKY PTVLFIYGGP QVQLVNNRFK GVKYFRLNTL ASLGYVVVVI DNRGSCHRGL
KFEGAFKYKM GQIEIDDQVE GLQYLASQYD FIDLERVGIH GWSYGGYLSL MALMQRSDIF
RVAIAGAPVT LWIFYDTGYT ERYMGHPDQN EQGYYLGSVA MQAEKFPSEP NRLLLLHGFL
DENVHFAHTS ILLSFLVRAG KPYDLQIYPQ ERHSIRVPES GEHYELHLLH YLQENLGSRM
AALKVI
//
