ID M3ZK48_XIPMA Unreviewed; 891 AA.
AC M3ZK48;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000002590.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000002590.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000002590.1};
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; M3ZK48; -.
DR STRING; 8083.ENSXMAP00000002590; -.
DR Ensembl; ENSXMAT00000002595.2; ENSXMAP00000002590.1; ENSXMAG00000002573.2.
DR eggNOG; KOG2281; Eukaryota.
DR GeneTree; ENSGT00940000158174; -.
DR HOGENOM; CLU_006105_1_0_1; -.
DR InParanoid; M3ZK48; -.
DR OMA; DIWVTNI; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:UP000002852}.
FT DOMAIN 34..160
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 172..598
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 691..891
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 891 AA; 101313 MW; 5B451052C1F2179E CRC64;
MHKIKRLKTD DKTEDSQESI RDALAGMTGV DELSDSTEVV EMEDVNPTQF QVEKHSWDGL
RKIIHSSRKN TGVVINKAPH DFQFVQKDEA SPHSHRIYYL GMPYASRENA LLYSDIPKKV
RKDALLVLSW KPMLDHFQAS PHHGGFSREE ELLRERKRLG VSGITAYDYH QPSGLFLFQA
NSSLYFCRDG ANNSFITSPM NPIEIKSQNS GTRMDPKICP GDPNFVGFIN NNDIWVTNTE
TGEERRLTFC HKGINNPKDD PKSAGVATFV TQEEFDRFTG YWWSPAAREE PDGGKTLQIV
YEEVDESKVE IIHVPSPALE ERKTDVYRYP RAGSSNPEIT LKIAEIRADS VGKIVSTQEK
VLPVPFNCLF PNIEYITRAG WTKDGRYAWA VMMDRRQQNL QLVLLPPALF IPAQQDEAKR
RESLEALGDS VHPFIIYRET SDIWINVHDI FHPFLQTSDD EFTFITVNES KTGYCHLYKI
TSVLQRGKYD WAKGYTHSEG DFKCPVKEEV TVTSGEWEVL ANHGAKRSCS PQIWVDEAAK
LVYFQGTKHS PLEHHLYVVS YETPGEIVRL TKPGFSHSCS VSQTFDMFIS HYSSLTTAPC
VHIYKLVGDC DPLHKEPQFW ASMMESSAYH FDAPPPEIFS FTGKSGFKLY GMLYKPNNLV
AGRKHPTVVF VYGGPQVQLV NNSYKGVKYL RLSTLACLGY VVLVIDGRGS CQRGLKFEGA
VKDKMGLVEI DDQVEGLHYI ADKYKFVDLS RVAIHGWSYG GFLSLMGLIH RPDIFKVAVA
GAPVTLWMAY DTGYTERYLD TPEKNQKGYE ACSVALHVDK LPNEPNRLLI LHGFLDENVH
FFHTNFLVSQ LIRAGKPYSL QIYPNERHSI RCPESGEHYE ISLLHFLQQN L
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