ID   L5MGN7_MYODS            Unreviewed;       847 AA.
AC   L5MGN7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE            EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN   ORFNames=MDA_GLEAN10011091 {ECO:0000313|EMBL:ELK37435.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK37435.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC       {ECO:0000256|ARBA:ARBA00010036}.
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DR   EMBL; KB100339; ELK37435.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5MGN7; -.
DR   MEROPS; S09.019; -.
DR   eggNOG; KOG2281; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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; 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:UP000010556}.
FT   DOMAIN          7..119
FT                   /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19520"
FT   DOMAIN          130..554
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          647..847
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   847 AA;  96800 MW;  51BEE0C55187A685 CRC64;
     MEDPATHFQV QKHSWEGLRN IIHDSRKNSG LIVNKAPHDF QFVQKTDESS PHSHRLYYLG
     MPYGSRENSL LYSEIPRKVR KEALLLLSWK QMLDHFQATP HHGVYSREEE LLRERKRLGV
     FGITSYDFHS ESGLFLFQAS NSLFHCRDGG KNGFMVSPMK PLEIKTQCSG PRMDPKICPA
     DPAFFSFINN SDLWVANIET GEEQRLTFCH RGLSNVLEDP KSAGVATFVI QEEFDRFTGY
     WWCPTASREG SEGHKTLRIL YEEVDESEVE VIHVPSPALE ERKTDSYRYP RTGSKNPKIA
     LKLAEFQTDS QGKIVSTQEK ELVQPFSMLF PKAEYIARAG WTRDGKYAWA MLLDRPQQQL
     QLVLLPPALF IPITEDEEQR EAFARAVPSN VQPYVVYEEI TSVWINVHDI FYPFPQSEGE
     DELCFIRANE SKTGFCHLYK VTTVLQPNGY DWSEPFSPGE DEFKCPVKEE IALTSGEWEV
     LARHGSKIWV NEETKLVYFQ GTKDTPLEHH LYVVSYESAS EIVRLTTPGF SHSCSMSQNF
     DMFVSHYSSV GTPPCVHVYK LTGPDDDPLH KQPQFWASMM EAASCPPDYV PPEIFDFHTR
     SDVQLYGMIY KPHAVQPGKK HPTVLFVYGG PQVQLVNNSF KGIKYLRLNT LASLGYAVVV
     IDGRGSCQRG LRFEGALKNQ MGQVEIEDQV EGLQFVAQKY GFIDLSRVAI HGWSYGGFLS
     LMGLIHKPQV FKVAIAGAPV TVWMAYDTGY TERYMDVPEN NQLGYEAGSV ALHVEKLPNE
     PNRLLILHGF LDENVHFFHT NFLVSQLIRA GKPYQLQIYP NERHSIRCPE SGEHYEVTLL
     HFLQEYL
//