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
//