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Dipeptidyl peptidase 8

 A0A2I3ME90_PAPAN        Unreviewed;       773 AA.
A0A2I3ME90;
28-FEB-2018, integrated into UniProtKB/TrEMBL.
28-FEB-2018, sequence version 1.
13-FEB-2019, entry version 7.
SubName: Full=Dipeptidyl peptidase 8 {ECO:0000313|Ensembl:ENSPANP00000033900};
Name=DPP8 {ECO:0000313|Ensembl:ENSPANP00000033900};
Papio anubis (Olive baboon).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000033900, ECO:0000313|Proteomes:UP000028761};
[1] {ECO:0000313|Ensembl:ENSPANP00000033900, ECO:0000313|Proteomes:UP000028761}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A.,
Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B.,
Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B.,
Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B.,
Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C.,
Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D.,
Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F.,
Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G.,
Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J.,
Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J.,
Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K.,
Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P.,
Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q.,
Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S.,
Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T.,
Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U.,
Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W.,
Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W.,
Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N.,
Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
"Whole Genome Assembly of Papio anubis.";
Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSPANP00000033900}
IDENTIFICATION.
Ensembl;
Submitted (JAN-2018) to UniProtKB.
-!- SIMILARITY: Belongs to the peptidase S9B family.
{ECO:0000256|SAAS:SAAS01094558}.
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EMBL; AHZZ02031178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AHZZ02031179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AHZZ02031180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
Ensembl; ENSPANT00000031545; ENSPANP00000033900; ENSPANG00000016711.
GeneTree; ENSGT00940000160717; -.
Proteomes; UP000028761; Chromosome 7.
ExpressionAtlas; A0A2I3ME90; baseline.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
Gene3D; 2.140.10.30; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001375; Peptidase_S9.
InterPro; IPR002469; Peptidase_S9B_N.
InterPro; IPR038554; Peptidase_S9B_N_sf.
Pfam; PF00930; DPPIV_N; 1.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000028761};
Membrane {ECO:0000256|SAM:Phobius};
Reference proteome {ECO:0000313|Proteomes:UP000028761};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 644 662 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 159 579 DPPIV_N. {ECO:0000259|Pfam:PF00930}.
DOMAIN 647 765 Peptidase_S9. {ECO:0000259|Pfam:PF00326}.
SEQUENCE 773 AA; 88924 MW; F313C1EAA1F09BB3 CRC64;
MAAAMETEQL GVEIFETADC EENIESQDQP KLEPFYVERY SWSQLKKLLA DTRKYHGYMM
AKAPHDFMFV KRNDPDGPHS DRIYYLAMSG ENRENTLFYS EIPKTINRAA VLMLSWKPLL
DLFQATLDYG MYSREEELLR ERKRIGTVGI ASYDYHQGSG TFLFQAGSGI YHVKDGGPQG
FTQQPLRPNL VETSCPNIRM DPKLCPADPD WIAFIHSNDI WISNIVTREE RRLTYVHNEL
ANMEEDARSA GVATFVLQEE FDRYSGYWWC PKAETTPSGG KILRILYEEN DESEVEIIHV
TSPMLETRRA DSFRYPKTGT ANPKVTFKMS EIMIDAEGRI MDVIDKELIQ PFEILFEGVE
YIARAGWTPE GKYAWSILLD RSQTRLQIVL ISPELFIPVE DDVMERQRLI ELVPDSVTPL
IIYEETTDIW INIHDIFHVF PQSHEEEIEF IFASECKTGF RHLYKITSIL KESKYKRSSG
GLPAPSDFKC PIKEEIAITS GEWEVLGRHG SNIQVDEVRR LVYFEGTKDS PLEHHLYVVS
YVNPGEVTRL TDRGYSHSCC ISQHCDFFIS KYSNQKNPHC VSLYKLSSSE DDLTCKTKEF
WATILDSAGI LFCPDPDVNT TGFTLYGDAS QAHDYSWKKY TTVLLAYMVA IAGAPVTLWI
FYDTGYTERY MGHPDQNEQG YYLGSVAMQA EKFPSEPNRL LLLHGFLDEN VHFAHTSILL
SFLVRAGKPY DLQIYPQERH SIRVPESGEH YELHLLHYLQ ENLGSRIAAL KVI


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Pathways :
WP470: Proteasome Degradation

Related Genes :
[DPP8 DPRP1 MSTP097 MSTP135 MSTP141] Dipeptidyl peptidase 8 (DP8) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 1) (DPRP-1) (Dipeptidyl peptidase VIII) (DPP VIII) (Prolyl dipeptidase DPP8)
[DPP4 ADCP2 CD26] Dipeptidyl peptidase 4 (EC 3.4.14.5) (ADABP) (Adenosine deaminase complexing protein 2) (ADCP-2) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]
[CTSC CPPI] Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]
[Dpp4 Cd26] Dipeptidyl peptidase 4 (EC 3.4.14.5) (Bile canaliculus domain-specific membrane glycoprotein) (Dipeptidyl peptidase IV) (DPP IV) (GP110 glycoprotein) (T-cell activation antigen CD26) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form); Dipeptidyl peptidase 4 60 kDa soluble form (Dipeptidyl peptidase IV 60 kDa soluble form)]
[DPP4 CD26] Dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]
[Ctsc] Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]
[Ctsc] Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]
[Dpp4 Cd26] Dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (Thymocyte-activating molecule) (THAM) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]
[DPP4 CD26] Dipeptidyl peptidase 4 (EC 3.4.14.5) (Activation molecule 3) (ACT3) (Adenosine deaminase complexing protein) (ADCP-I) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (WC10) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]
[DPP4 CD26] Dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]
[DPP9 DPRP2] Dipeptidyl peptidase 9 (DP9) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 2) (DPRP-2) (Dipeptidyl peptidase IX) (DPP IX) (Dipeptidyl peptidase-like protein 9) (DPLP9)
[DPP10 DPRP3 KIAA1492] Inactive dipeptidyl peptidase 10 (Dipeptidyl peptidase IV-related protein 3) (DPRP-3) (Dipeptidyl peptidase X) (DPP X) (Dipeptidyl peptidase-like protein 2) (DPL2)
[DPP3] Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III) (Enkephalinase B)
[DPP6] Dipeptidyl aminopeptidase-like protein 6 (DPPX) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI)
[DPP7 DPP2 QPP] Dipeptidyl peptidase 2 (EC 3.4.14.2) (Dipeptidyl aminopeptidase II) (Dipeptidyl peptidase 7) (Dipeptidyl peptidase II) (DPP II) (Quiescent cell proline dipeptidase)
[Dpp6] Dipeptidyl aminopeptidase-like protein 6 (DPPX) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI)
[Dpp6 Dpp-6] Dipeptidyl aminopeptidase-like protein 6 (DPPX) (Dipeptidyl aminopeptidase-related protein) (Dipeptidyl peptidase 6) (Dipeptidyl peptidase IV-like protein) (Dipeptidyl peptidase VI) (DPP VI)
[Dpp3] Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III) (Enkephalinase B)
[Dpp7 Dpp2] Dipeptidyl peptidase 2 (EC 3.4.14.2) (Dipeptidyl aminopeptidase II) (Dipeptidyl peptidase 7) (Dipeptidyl peptidase II) (DPP II) (Quiescent cell proline dipeptidase)
[DppIII CG7415] Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III)
[dpp11 PGN_0607] Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11)
[CTSC] Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain 1 (Dipeptidyl peptidase I heavy chain 1); Dipeptidyl peptidase 1 heavy chain 2 (Dipeptidyl peptidase I heavy chain 2); Dipeptidyl peptidase 1 heavy chain 3 (Dipeptidyl peptidase I heavy chain 3); Dipeptidyl peptidase 1 heavy chain 4 (Dipeptidyl peptidase I heavy chain 4); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)] (Fragment)
[FAP] Prolyl endopeptidase FAP (EC 3.4.21.26) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) (Z-Pro-prolinal insensitive peptidase) (ZIP) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]
[FAP] Prolyl endopeptidase FAP (EC 3.4.21.26) (170 kDa melanoma membrane-bound gelatinase) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]
[CTSC] Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]
[Dpp7 Dpp2 Qpp] Dipeptidyl peptidase 2 (EC 3.4.14.2) (Dipeptidyl aminopeptidase II) (Dipeptidyl peptidase 7) (Dipeptidyl peptidase II) (DPP II) (Quiescent cell proline dipeptidase)
[dpp11 PeDPP11] Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11)
[Fap] Prolyl endopeptidase FAP (EC 3.4.21.26) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]
[Dpp10] Inactive dipeptidyl peptidase 10 (Dipeptidyl peptidase X) (DPP X)
[dpp7 dpp-7 PGN_1479] Dipeptidyl-peptidase 7 (DPP-7) (DPP7) (EC 3.4.14.-)

Bibliography :
[30897780] Correction: Kim, Young-Gun; Jeon, Ja Young; Kim, Hae Jin; Kim, Dae Jung; Lee, Kwan-Woo; Moon, So Young; Han, Seung Jin. Risk of Dementia in Older Patients with Type 2 Diabetes on Dipeptidyl-Peptidase IV Inhibitors versus Sulfonylureas: A Real-World Population-Based Cohort Study. 2019, , 28.
[30888218] Homocysteine-induced inverse expression of tissue factor and DPP4 in endothelial cells is related to NADPH oxidase activity.
[30886577] The Relationship Between Plasma DPP4 Activity to BDNF Ratio and Mild Cognitive Impairment in Elderly Population With Normal Glucose Tolerance.
[30885955] The SGLT2 Inhibitor Dapagliflozin Reduces Liver Fat but Does Not Affect Tissue Insulin Sensitivity: A Randomized, Double-Blind, Placebo Controlled Study With 8-Week Treatment in Type 2 Diabetes Patients.
[30880253] A dipeptidyl peptidase-IV inhibitor improves diastolic dysfunction in Dahl salt-sensitive rats.
[30850916] Effects of Teneligliptin on the Progressive Left Ventricular Diastolic Dysfunction in Patients with Type 2 Diabetes Mellitus in Open-Label, Marker-Stratified Randomized, Parallel-Group Comparison, Standard Treatment-Controlled Multicenter Trial (TOPLEVEL Study): Rationale and Study Design.
[30833929] Diabetes and Aging: From Treatment Goals to Pharmacologic Therapy.
[30828846] Randomised clinical trial: the DPP-4 inhibitor, vildagliptin, inhibits gastric accommodation and increases glucagon-like peptide-1 plasma levels in healthy volunteers.
[30826768] Treatment patterns, persistence and adherence rates in patients with type 2 diabetes mellitus in Japan: a claims-based cohort study.
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