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Database: UniProt
Entry: M7C0I9_CHEMY
LinkDB: M7C0I9_CHEMY
Original site: M7C0I9_CHEMY 
ID   M7C0I9_CHEMY            Unreviewed;       987 AA.
AC   M7C0I9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE            EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN   ORFNames=UY3_01055 {ECO:0000313|EMBL:EMP41660.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP41660.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(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   -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC       {ECO:0000256|ARBA:ARBA00010036}.
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DR   EMBL; KB486406; EMP41660.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7C0I9; -.
DR   STRING; 8469.M7C0I9; -.
DR   eggNOG; KOG2281; Eukaryota.
DR   Proteomes; UP000031443; 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; 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; 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:UP000031443}.
FT   DOMAIN          1..146
FT                   /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19520"
FT   DOMAIN          159..434
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          591..762
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   987 AA;  111826 MW;  78865EBB8C01BF8E CRC64;
     MAAAMETEQL GLEIFGTSES EEHAEAEEQP TLEPFYVERY SWSQLKKLLT DTRKYHGYMV
     AKAPHDFTFV KKNDPEGPHS DRIYYLAMSG ENRENTLFYS EIPKTINKAE VLMLSWKPLL
     DLFQASLDYG MYSREEELLR ERKRIGTVGI ASYDYHRESG TFLFQAGSGI YHVKDGGPHG
     FTQQPLKPNL VETSCPNIRM DPKLCPADPN WIAFIHSNDI WISNILTREE RRLTFVHNEL
     ANLEEDPRSA GVATFVLQEE FDRYTGYWWC PNAEPTVTGG KILRILYEEN DESEVEIIHV
     TSPMLETRRT DSFRYPKTGT ANPKVTFKMS EITVDAEGRI AAVMDKELVQ PFEILFEGIE
     YIARAGWTPE GKYAWSILLD RSQTRLQIVL ISPALFIAVE DDAMERQKLI DAVPDSVTPL
     TIYEETTDIW INIHVDEAKK LVYFEGTKDS PLEHHLYVVS YKNPGEVKRL TDRSYSHACS
     ISQDCDMFIS KFSNQKNPHC VSLYRLTGSE DDVAHRKKEF WATILDSAGP LPDYVPPEIF
     SFESSSGFTL YGMMYKPHHL QPGKKYPTVL FIYGGPQVQL VNNRFKGIKY FRLNTLASLG
     YVVVVIDNRG SCHRGLKFEG AFKYKMGQIE IDDQVEGLQY LASQYDFIDL DRVGIHGWSY
     GGYLSLMALM QRSDLFRVAI AGAPVTLWIF YDTGYTERYM GHPDHNEQGY YLGSVAMQAE
     KFPSEPHRLL LLHGFLDENV HFAHTSILLS FLVRAGKPYD LQPQMACISP LSTNSSDPLS
     DWCDNWSVTD RQHEQQLKLM PYRQMARSQA QCGIWPQDIS FYPGLANVHD LLCKTDTANS
     FVTNPCPSRS FLAVSVLHIV AARSLNTSMT TELGSPCSKN TPTTSARAVA LLPALAPERS
     RQRYQFDTND VHDVTPDLQS STLSKALFAL DSGTCGFRDL PGLILTVNAS SPSRWTLTAV
     TVFAASNDQS THQPARLAKD TATEMIL
//
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