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Database: UniProt
Entry: H2NX38_PONAB
LinkDB: H2NX38_PONAB
Original site: H2NX38_PONAB 
ID   H2NX38_PONAB            Unreviewed;       811 AA.
AC   H2NX38;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 52.
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:ENSPPYP00000010557.2};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000010557.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000010557.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPPYP00000010557.2}
RP   IDENTIFICATION.
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; H2NX38; -.
DR   Ensembl; ENSPPYT00000010971.2; ENSPPYP00000010557.2; ENSPPYG00000009415.3.
DR   eggNOG; KOG2281; Eukaryota.
DR   GeneTree; ENSGT00940000158174; -.
DR   HOGENOM; CLU_006105_1_0_1; -.
DR   InParanoid; H2NX38; -.
DR   TreeFam; TF313309; -.
DR   Proteomes; UP000001595; Chromosome 19.
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:UP000001595}.
FT   DOMAIN          51..164
FT                   /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19520"
FT   DOMAIN          175..599
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          692..777
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   REGION          778..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  91864 MW;  7F4A8F73C616A8C0 CRC64;
     MRKVKKLRLD KENTGSWRSF SLNSEGAERM ATTGTPTADR GDTAATDDPA 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 KYAWAMFLDR PQQWLQLVLL PPALFIPSTE
     NEEQRLASAR AVPRNVQPYV VYEEVTNVWI NVHDIFYPFP QSEGDDELCF LRANECKTGF
     CHLYKVTAVL KSQGYDWSEP FSPGEDEFKC 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 HKPQVFKQPH
     GAEPPSSLPA TADRRMASGC TKPRQQLSVG G
//
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