Full text data of DPP3
DPP3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Dipeptidyl peptidase 3; 3.4.14.4 (Dipeptidyl aminopeptidase III; Dipeptidyl arylamidase III; Dipeptidyl peptidase III; DPP III; Enkephalinase B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dipeptidyl peptidase 3; 3.4.14.4 (Dipeptidyl aminopeptidase III; Dipeptidyl arylamidase III; Dipeptidyl peptidase III; DPP III; Enkephalinase B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00020672
IPI00020672 Dipeptidyl-peptidase III Proteolysis, peptidolysis, Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00020672 Dipeptidyl-peptidase III Proteolysis, peptidolysis, Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q9NY33
ID DPP3_HUMAN Reviewed; 737 AA.
AC Q9NY33; B2RDB5; B4DLX4; F5H8L6; O95748; Q969H2; Q9BV67; Q9HAL6;
read moreDT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Dipeptidyl peptidase 3;
DE EC=3.4.14.4;
DE AltName: Full=Dipeptidyl aminopeptidase III;
DE AltName: Full=Dipeptidyl arylamidase III;
DE AltName: Full=Dipeptidyl peptidase III;
DE Short=DPP III;
DE AltName: Full=Enkephalinase B;
GN Name=DPP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HIS-145 AND
RP HIS-678.
RA Chen J.M., Fortunato M., Barrett A.J.;
RT "Cloning and sequencing of human dipeptidyl-peptidase III.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP HIS-76.
RC TISSUE=Colon, Kidney, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-723 (ISOFORM 1), CHARACTERIZATION,
RP AND VARIANT HIS-678.
RX PubMed=9425109;
RA Fukasawa K., Fukusawa K.M., Kanai M., Fujii S., Hirose J., Harada M.;
RT "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular
RT cloning and expression.";
RL Biochem. J. 329:275-282(1998).
RN [6]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC TISSUE=Erythrocyte;
RX PubMed=11209758; DOI=10.1515/BC.2000.151;
RA Abramic M., Schleuder D., Dolovcak L., Schroeder W., Strupat K.,
RA Sagi D., Peter-Katalini J., Vitale L.;
RT "Human and rat dipeptidyl peptidase III: biochemical and mass
RT spectrometric arguments for similarities and differences.";
RL Biol. Chem. 381:1233-1243(2000).
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-726 IN COMPLEX WITH OPIOID
RP PEPTIDE, FUNCTION, ENZYME REGULATION, COFACTOR, AND ZINC-BINDING
RP SITES.
RX PubMed=22493238; DOI=10.1073/pnas.1118005109;
RA Bezerra G.A., Dobrovetsky E., Viertlmayr R., Dong A., Binter A.,
RA Abramic M., Macheroux P., Dhe-Paganon S., Gruber K.;
RT "Entropy-driven binding of opioid peptides induces a large domain
RT motion in human dipeptidyl peptidase III.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6525-6530(2012).
CC -!- FUNCTION: Cleaves and degrades of the opioid peptide enkephalin.
CC Also cleaves Arg-Arg-beta-naphthylamide.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide from a
CC peptide comprising four or more residues, with broad specificity.
CC Also acts on dipeptidyl 2-naphthylamides.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- ENZYME REGULATION: Inhibited by spinorphin, an opioid peptide
CC derived from hemoglobin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.8;
CC -!- INTERACTION:
CC Q14145:KEAP1; NbExp=2; IntAct=EBI-718333, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NY33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NY33-2; Sequence=VSP_005510;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC experimental confirmation available;
CC Name=3; Synonyms=DPP3-BBS1;
CC IsoId=Q8NFJ9-2; Sequence=External;
CC Note=Based on a readthrough transcript which may produce a
CC DPP3-BBS1 fusion protein. No experimental confirmation
CC available;
CC Name=4;
CC IsoId=Q9NY33-4; Sequence=VSP_044696;
CC Note=No experimental confirmation available;
CC -!- MASS SPECTROMETRY: Mass=82500; Mass_error=60; Method=MALDI;
CC Range=1-737 (Q9NY33-1); Source=PubMed:11209758;
CC -!- SIMILARITY: Belongs to the peptidase M49 family.
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DR EMBL; AJ271216; CAB72433.1; -; mRNA.
DR EMBL; AK021449; BAB13828.1; -; mRNA.
DR EMBL; AK297199; BAG59686.1; -; mRNA.
DR EMBL; AK315478; BAG37862.1; -; mRNA.
DR EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001446; AAH01446.1; -; mRNA.
DR EMBL; BC007221; AAH07221.1; -; mRNA.
DR EMBL; BC014038; AAH14038.1; -; mRNA.
DR EMBL; BC024271; AAH24271.1; -; mRNA.
DR EMBL; AB017970; BAA75785.1; -; mRNA.
DR RefSeq; NP_001243599.1; NM_001256670.1.
DR RefSeq; NP_005691.2; NM_005700.4.
DR RefSeq; NP_569710.2; NM_130443.3.
DR UniGene; Hs.502914; -.
DR UniGene; Hs.740670; -.
DR PDB; 3FVY; X-ray; 1.90 A; A=1-726.
DR PDB; 3T6B; X-ray; 2.40 A; A/B=1-726.
DR PDB; 3T6J; X-ray; 2.98 A; A=1-726.
DR PDBsum; 3FVY; -.
DR PDBsum; 3T6B; -.
DR PDBsum; 3T6J; -.
DR ProteinModelPortal; Q9NY33; -.
DR SMR; Q9NY33; 3-726.
DR DIP; DIP-53793N; -.
DR IntAct; Q9NY33; 4.
DR BindingDB; Q9NY33; -.
DR ChEMBL; CHEMBL4520; -.
DR MEROPS; M49.001; -.
DR PhosphoSite; Q9NY33; -.
DR DMDM; 20532389; -.
DR PeptideAtlas; Q9NY33; -.
DR PRIDE; Q9NY33; -.
DR DNASU; 10072; -.
DR Ensembl; ENST00000360510; ENSP00000353701; ENSG00000254986.
DR Ensembl; ENST00000453114; ENSP00000389943; ENSG00000254986.
DR Ensembl; ENST00000530165; ENSP00000436941; ENSG00000254986.
DR Ensembl; ENST00000541961; ENSP00000440502; ENSG00000254986.
DR GeneID; 10072; -.
DR KEGG; hsa:10072; -.
DR UCSC; uc010rpe.2; human.
DR CTD; 10072; -.
DR GeneCards; GC11P066249; -.
DR HGNC; HGNC:3008; DPP3.
DR HPA; HPA035781; -.
DR MIM; 606818; gene.
DR neXtProt; NX_Q9NY33; -.
DR PharmGKB; PA27466; -.
DR HOGENOM; HOG000187784; -.
DR HOVERGEN; HBG025680; -.
DR InParanoid; Q9NY33; -.
DR KO; K01277; -.
DR ChiTaRS; DPP3; human.
DR EvolutionaryTrace; Q9NY33; -.
DR GeneWiki; DPP3; -.
DR GenomeRNAi; 10072; -.
DR NextBio; 38071; -.
DR PRO; PR:Q9NY33; -.
DR ArrayExpress; Q9NY33; -.
DR Bgee; Q9NY33; -.
DR CleanEx; HS_DPP3; -.
DR Genevestigator; Q9NY33; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR005317; Dipeptidyl-peptase3.
DR PANTHER; PTHR23422:SF3; PTHR23422:SF3; 1.
DR PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminopeptidase;
KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Polymorphism; Protease; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 737 Dipeptidyl peptidase 3.
FT /FTId=PRO_0000078238.
FT ACT_SITE 451 451 By similarity.
FT METAL 450 450 Zinc; catalytic.
FT METAL 455 455 Zinc; catalytic.
FT METAL 508 508 Zinc; catalytic.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 91 120 Missing (in isoform 4).
FT /FTId=VSP_044696.
FT VAR_SEQ 182 601 Missing (in isoform 2).
FT /FTId=VSP_005510.
FT VARIANT 76 76 R -> H (in dbSNP:rs11826683).
FT /FTId=VAR_033494.
FT VARIANT 145 145 Q -> H (in dbSNP:rs11550299).
FT /FTId=VAR_033495.
FT VARIANT 678 678 R -> H (in dbSNP:rs2305535).
FT /FTId=VAR_021850.
FT VARIANT 690 690 E -> K (in dbSNP:rs12421620).
FT /FTId=VAR_051597.
FT CONFLICT 224 224 P -> S (in Ref. 2; BAG59686).
FT CONFLICT 417 419 YAT -> TA (in Ref. 5; BAA75785).
FT CONFLICT 697 697 I -> Y (in Ref. 5; BAA75785).
FT HELIX 4 6
FT STRAND 14 16
FT HELIX 20 24
FT HELIX 28 45
FT HELIX 47 50
FT HELIX 56 69
FT HELIX 72 81
FT HELIX 86 102
FT STRAND 104 106
FT TURN 108 110
FT HELIX 120 129
FT HELIX 131 135
FT HELIX 137 152
FT HELIX 156 158
FT STRAND 159 161
FT HELIX 164 166
FT STRAND 170 172
FT HELIX 178 190
FT STRAND 198 204
FT STRAND 206 208
FT STRAND 210 217
FT STRAND 222 224
FT HELIX 231 233
FT STRAND 235 239
FT STRAND 242 250
FT HELIX 252 266
FT HELIX 272 287
FT HELIX 290 302
FT STRAND 307 316
FT STRAND 318 320
FT STRAND 321 323
FT STRAND 327 334
FT HELIX 337 348
FT HELIX 350 355
FT STRAND 357 359
FT HELIX 361 363
FT STRAND 375 384
FT STRAND 388 392
FT HELIX 396 401
FT STRAND 405 409
FT HELIX 410 413
FT HELIX 421 423
FT HELIX 429 452
FT TURN 453 456
FT STRAND 465 467
FT STRAND 469 471
FT TURN 473 475
FT TURN 479 481
FT STRAND 482 484
FT HELIX 495 498
FT TURN 500 502
FT HELIX 503 518
FT HELIX 522 528
FT HELIX 532 552
FT HELIX 553 556
FT HELIX 559 561
FT STRAND 563 565
FT HELIX 567 581
FT STRAND 586 593
FT STRAND 597 605
FT HELIX 607 609
FT TURN 610 613
FT HELIX 614 630
FT HELIX 634 644
FT TURN 651 653
FT HELIX 655 664
FT STRAND 671 673
FT STRAND 676 680
FT STRAND 683 687
FT HELIX 693 701
FT TURN 705 707
FT HELIX 708 722
FT HELIX 723 725
SQ SEQUENCE 737 AA; 82589 MW; E2BB1923C9CAFDEC CRC64;
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL QTSPEAPYIY
ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY SNMGNYKSFG DTKFVPNLPK
EKLERVILGS EAAQQHPEEV RGLWQTCGEL MFSLEPRLRH LGLGKEGITT YFSGNCTMED
AKLAQDFLDS QNLSAYNTRL FKEVDGEGKP YYEVRLASVL GSEPSLDSEV TSKLKSYEFR
GSPFQVTRGD YAPILQKVVE QLEKAKAYAA NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAVVNKAMS AKFERLVASA EQLLKELPWP
PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ TEGFKNVSLG NVLAVAYATQ
REKLTFLEED DKDLYILWKG PSFDVQVGLH ELLGHGSGKL FVQDEKGAFN FDQETVINPE
TGEQIQSWYR SGETWDSKFS TIASSYEECR AESVGLYLCL HPQVLEIFGF EGADAEDVIY
VNWLNMVRAG LLALEFYTPE AFNWRQAHMQ ARFVILRVLL EAGEGLVTIT PTTGSDGRPD
ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA PPECFLTLRD
TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF SERFPEDGPE LEEILTQLAT
ADARFWKGPS EAPSGQA
//
ID DPP3_HUMAN Reviewed; 737 AA.
AC Q9NY33; B2RDB5; B4DLX4; F5H8L6; O95748; Q969H2; Q9BV67; Q9HAL6;
read moreDT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Dipeptidyl peptidase 3;
DE EC=3.4.14.4;
DE AltName: Full=Dipeptidyl aminopeptidase III;
DE AltName: Full=Dipeptidyl arylamidase III;
DE AltName: Full=Dipeptidyl peptidase III;
DE Short=DPP III;
DE AltName: Full=Enkephalinase B;
GN Name=DPP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HIS-145 AND
RP HIS-678.
RA Chen J.M., Fortunato M., Barrett A.J.;
RT "Cloning and sequencing of human dipeptidyl-peptidase III.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP HIS-76.
RC TISSUE=Colon, Kidney, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-723 (ISOFORM 1), CHARACTERIZATION,
RP AND VARIANT HIS-678.
RX PubMed=9425109;
RA Fukasawa K., Fukusawa K.M., Kanai M., Fujii S., Hirose J., Harada M.;
RT "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular
RT cloning and expression.";
RL Biochem. J. 329:275-282(1998).
RN [6]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC TISSUE=Erythrocyte;
RX PubMed=11209758; DOI=10.1515/BC.2000.151;
RA Abramic M., Schleuder D., Dolovcak L., Schroeder W., Strupat K.,
RA Sagi D., Peter-Katalini J., Vitale L.;
RT "Human and rat dipeptidyl peptidase III: biochemical and mass
RT spectrometric arguments for similarities and differences.";
RL Biol. Chem. 381:1233-1243(2000).
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-726 IN COMPLEX WITH OPIOID
RP PEPTIDE, FUNCTION, ENZYME REGULATION, COFACTOR, AND ZINC-BINDING
RP SITES.
RX PubMed=22493238; DOI=10.1073/pnas.1118005109;
RA Bezerra G.A., Dobrovetsky E., Viertlmayr R., Dong A., Binter A.,
RA Abramic M., Macheroux P., Dhe-Paganon S., Gruber K.;
RT "Entropy-driven binding of opioid peptides induces a large domain
RT motion in human dipeptidyl peptidase III.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6525-6530(2012).
CC -!- FUNCTION: Cleaves and degrades of the opioid peptide enkephalin.
CC Also cleaves Arg-Arg-beta-naphthylamide.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide from a
CC peptide comprising four or more residues, with broad specificity.
CC Also acts on dipeptidyl 2-naphthylamides.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- ENZYME REGULATION: Inhibited by spinorphin, an opioid peptide
CC derived from hemoglobin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.8;
CC -!- INTERACTION:
CC Q14145:KEAP1; NbExp=2; IntAct=EBI-718333, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NY33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NY33-2; Sequence=VSP_005510;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC experimental confirmation available;
CC Name=3; Synonyms=DPP3-BBS1;
CC IsoId=Q8NFJ9-2; Sequence=External;
CC Note=Based on a readthrough transcript which may produce a
CC DPP3-BBS1 fusion protein. No experimental confirmation
CC available;
CC Name=4;
CC IsoId=Q9NY33-4; Sequence=VSP_044696;
CC Note=No experimental confirmation available;
CC -!- MASS SPECTROMETRY: Mass=82500; Mass_error=60; Method=MALDI;
CC Range=1-737 (Q9NY33-1); Source=PubMed:11209758;
CC -!- SIMILARITY: Belongs to the peptidase M49 family.
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DR EMBL; AJ271216; CAB72433.1; -; mRNA.
DR EMBL; AK021449; BAB13828.1; -; mRNA.
DR EMBL; AK297199; BAG59686.1; -; mRNA.
DR EMBL; AK315478; BAG37862.1; -; mRNA.
DR EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001446; AAH01446.1; -; mRNA.
DR EMBL; BC007221; AAH07221.1; -; mRNA.
DR EMBL; BC014038; AAH14038.1; -; mRNA.
DR EMBL; BC024271; AAH24271.1; -; mRNA.
DR EMBL; AB017970; BAA75785.1; -; mRNA.
DR RefSeq; NP_001243599.1; NM_001256670.1.
DR RefSeq; NP_005691.2; NM_005700.4.
DR RefSeq; NP_569710.2; NM_130443.3.
DR UniGene; Hs.502914; -.
DR UniGene; Hs.740670; -.
DR PDB; 3FVY; X-ray; 1.90 A; A=1-726.
DR PDB; 3T6B; X-ray; 2.40 A; A/B=1-726.
DR PDB; 3T6J; X-ray; 2.98 A; A=1-726.
DR PDBsum; 3FVY; -.
DR PDBsum; 3T6B; -.
DR PDBsum; 3T6J; -.
DR ProteinModelPortal; Q9NY33; -.
DR SMR; Q9NY33; 3-726.
DR DIP; DIP-53793N; -.
DR IntAct; Q9NY33; 4.
DR BindingDB; Q9NY33; -.
DR ChEMBL; CHEMBL4520; -.
DR MEROPS; M49.001; -.
DR PhosphoSite; Q9NY33; -.
DR DMDM; 20532389; -.
DR PeptideAtlas; Q9NY33; -.
DR PRIDE; Q9NY33; -.
DR DNASU; 10072; -.
DR Ensembl; ENST00000360510; ENSP00000353701; ENSG00000254986.
DR Ensembl; ENST00000453114; ENSP00000389943; ENSG00000254986.
DR Ensembl; ENST00000530165; ENSP00000436941; ENSG00000254986.
DR Ensembl; ENST00000541961; ENSP00000440502; ENSG00000254986.
DR GeneID; 10072; -.
DR KEGG; hsa:10072; -.
DR UCSC; uc010rpe.2; human.
DR CTD; 10072; -.
DR GeneCards; GC11P066249; -.
DR HGNC; HGNC:3008; DPP3.
DR HPA; HPA035781; -.
DR MIM; 606818; gene.
DR neXtProt; NX_Q9NY33; -.
DR PharmGKB; PA27466; -.
DR HOGENOM; HOG000187784; -.
DR HOVERGEN; HBG025680; -.
DR InParanoid; Q9NY33; -.
DR KO; K01277; -.
DR ChiTaRS; DPP3; human.
DR EvolutionaryTrace; Q9NY33; -.
DR GeneWiki; DPP3; -.
DR GenomeRNAi; 10072; -.
DR NextBio; 38071; -.
DR PRO; PR:Q9NY33; -.
DR ArrayExpress; Q9NY33; -.
DR Bgee; Q9NY33; -.
DR CleanEx; HS_DPP3; -.
DR Genevestigator; Q9NY33; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR005317; Dipeptidyl-peptase3.
DR PANTHER; PTHR23422:SF3; PTHR23422:SF3; 1.
DR PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminopeptidase;
KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Polymorphism; Protease; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 737 Dipeptidyl peptidase 3.
FT /FTId=PRO_0000078238.
FT ACT_SITE 451 451 By similarity.
FT METAL 450 450 Zinc; catalytic.
FT METAL 455 455 Zinc; catalytic.
FT METAL 508 508 Zinc; catalytic.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 91 120 Missing (in isoform 4).
FT /FTId=VSP_044696.
FT VAR_SEQ 182 601 Missing (in isoform 2).
FT /FTId=VSP_005510.
FT VARIANT 76 76 R -> H (in dbSNP:rs11826683).
FT /FTId=VAR_033494.
FT VARIANT 145 145 Q -> H (in dbSNP:rs11550299).
FT /FTId=VAR_033495.
FT VARIANT 678 678 R -> H (in dbSNP:rs2305535).
FT /FTId=VAR_021850.
FT VARIANT 690 690 E -> K (in dbSNP:rs12421620).
FT /FTId=VAR_051597.
FT CONFLICT 224 224 P -> S (in Ref. 2; BAG59686).
FT CONFLICT 417 419 YAT -> TA (in Ref. 5; BAA75785).
FT CONFLICT 697 697 I -> Y (in Ref. 5; BAA75785).
FT HELIX 4 6
FT STRAND 14 16
FT HELIX 20 24
FT HELIX 28 45
FT HELIX 47 50
FT HELIX 56 69
FT HELIX 72 81
FT HELIX 86 102
FT STRAND 104 106
FT TURN 108 110
FT HELIX 120 129
FT HELIX 131 135
FT HELIX 137 152
FT HELIX 156 158
FT STRAND 159 161
FT HELIX 164 166
FT STRAND 170 172
FT HELIX 178 190
FT STRAND 198 204
FT STRAND 206 208
FT STRAND 210 217
FT STRAND 222 224
FT HELIX 231 233
FT STRAND 235 239
FT STRAND 242 250
FT HELIX 252 266
FT HELIX 272 287
FT HELIX 290 302
FT STRAND 307 316
FT STRAND 318 320
FT STRAND 321 323
FT STRAND 327 334
FT HELIX 337 348
FT HELIX 350 355
FT STRAND 357 359
FT HELIX 361 363
FT STRAND 375 384
FT STRAND 388 392
FT HELIX 396 401
FT STRAND 405 409
FT HELIX 410 413
FT HELIX 421 423
FT HELIX 429 452
FT TURN 453 456
FT STRAND 465 467
FT STRAND 469 471
FT TURN 473 475
FT TURN 479 481
FT STRAND 482 484
FT HELIX 495 498
FT TURN 500 502
FT HELIX 503 518
FT HELIX 522 528
FT HELIX 532 552
FT HELIX 553 556
FT HELIX 559 561
FT STRAND 563 565
FT HELIX 567 581
FT STRAND 586 593
FT STRAND 597 605
FT HELIX 607 609
FT TURN 610 613
FT HELIX 614 630
FT HELIX 634 644
FT TURN 651 653
FT HELIX 655 664
FT STRAND 671 673
FT STRAND 676 680
FT STRAND 683 687
FT HELIX 693 701
FT TURN 705 707
FT HELIX 708 722
FT HELIX 723 725
SQ SEQUENCE 737 AA; 82589 MW; E2BB1923C9CAFDEC CRC64;
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL QTSPEAPYIY
ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY SNMGNYKSFG DTKFVPNLPK
EKLERVILGS EAAQQHPEEV RGLWQTCGEL MFSLEPRLRH LGLGKEGITT YFSGNCTMED
AKLAQDFLDS QNLSAYNTRL FKEVDGEGKP YYEVRLASVL GSEPSLDSEV TSKLKSYEFR
GSPFQVTRGD YAPILQKVVE QLEKAKAYAA NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAVVNKAMS AKFERLVASA EQLLKELPWP
PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ TEGFKNVSLG NVLAVAYATQ
REKLTFLEED DKDLYILWKG PSFDVQVGLH ELLGHGSGKL FVQDEKGAFN FDQETVINPE
TGEQIQSWYR SGETWDSKFS TIASSYEECR AESVGLYLCL HPQVLEIFGF EGADAEDVIY
VNWLNMVRAG LLALEFYTPE AFNWRQAHMQ ARFVILRVLL EAGEGLVTIT PTTGSDGRPD
ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA PPECFLTLRD
TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF SERFPEDGPE LEEILTQLAT
ADARFWKGPS EAPSGQA
//
MIM
606818
*RECORD*
*FIELD* NO
606818
*FIELD* TI
*606818 DIPEPTIDYL PEPTIDASE III; DPP3
*FIELD* TX
DESCRIPTION
DPP3 (EC 3.4.14.4) is one of the dipeptidyl aminopeptidases that remove
read moreN-terminal dipeptides from physiologically active peptides such as
angiotensin (see 106150) or enkephalin (131330).
CLONING
Fukasawa et al. (1999) isolated a partial DPP3 cDNA clone from a
placenta cDNA library, using antibody to the purified protein as probe.
By mass spectrometry, Abramic et al. (2000) determined that the
molecular mass of full-length DPP3 is 82.5 kD; by SDS-PAGE, the apparent
molecular mass is 81.2 kD.
GENE FUNCTION
By mutation and enzyme analysis of the rat recombinant DPP3 protein,
Fukasawa et al. (1999) found that DPP3 shows zinc-dependent
metalloprotease activity and contains a conserved HELLGH motif with
similarity to the zincin HExxH consensus motif. Abramic et al. (2000)
noted that whereas the enzymes purified from rat and human erythrocytes
show the same molecular mass, pI, and enzyme substrates, they differ
significantly in their temperature stability, pH optima, kinetic
parameters, and sensitivity to divalent cations, sulfhydryl reagents,
and microbial protease inhibitors.
MAPPING
Fukasawa et al. (2000) mapped the DPP3 gene to chromosome 11q12-q13.1 by
FISH.
*FIELD* RF
1. Abramic, M.; Schleuder, D.; Dolovcak, L.; Schroder, W.; Strupat,
K.; Sagi, D.; Peter-Katalini, J.; Vitale, L.: Human and rat dipeptidyl
peptidase III: biochemical and mass spectrometric arguments for similarities
and differences. Biol. Chem. 381: 1233-1243, 2000.
2. Fukasawa, K.; Fukasawa, K. M.; Iwamoto, H.; Hirose, J.; Harada,
M.: The HELLGH motif of rat liver dipeptidyl peptidase III is involved
in zinc coordination and the catalytic activity of the enzyme. Biochemistry 38:
8299-8303, 1999.
3. Fukasawa, K. M.; Fukasawa, K.; Harada, M.: Assignment of the dipeptidyl
peptidase III gene (DPP3) to human chromosome 11 band q12-q13.1 by
in situ hybridization. Cytogenet. Cell Genet. 88: 99-100, 2000.
*FIELD* CD
Patricia A. Hartz: 4/3/2002
*FIELD* ED
wwang: 10/14/2008
carol: 4/4/2002
carol: 4/3/2002
*RECORD*
*FIELD* NO
606818
*FIELD* TI
*606818 DIPEPTIDYL PEPTIDASE III; DPP3
*FIELD* TX
DESCRIPTION
DPP3 (EC 3.4.14.4) is one of the dipeptidyl aminopeptidases that remove
read moreN-terminal dipeptides from physiologically active peptides such as
angiotensin (see 106150) or enkephalin (131330).
CLONING
Fukasawa et al. (1999) isolated a partial DPP3 cDNA clone from a
placenta cDNA library, using antibody to the purified protein as probe.
By mass spectrometry, Abramic et al. (2000) determined that the
molecular mass of full-length DPP3 is 82.5 kD; by SDS-PAGE, the apparent
molecular mass is 81.2 kD.
GENE FUNCTION
By mutation and enzyme analysis of the rat recombinant DPP3 protein,
Fukasawa et al. (1999) found that DPP3 shows zinc-dependent
metalloprotease activity and contains a conserved HELLGH motif with
similarity to the zincin HExxH consensus motif. Abramic et al. (2000)
noted that whereas the enzymes purified from rat and human erythrocytes
show the same molecular mass, pI, and enzyme substrates, they differ
significantly in their temperature stability, pH optima, kinetic
parameters, and sensitivity to divalent cations, sulfhydryl reagents,
and microbial protease inhibitors.
MAPPING
Fukasawa et al. (2000) mapped the DPP3 gene to chromosome 11q12-q13.1 by
FISH.
*FIELD* RF
1. Abramic, M.; Schleuder, D.; Dolovcak, L.; Schroder, W.; Strupat,
K.; Sagi, D.; Peter-Katalini, J.; Vitale, L.: Human and rat dipeptidyl
peptidase III: biochemical and mass spectrometric arguments for similarities
and differences. Biol. Chem. 381: 1233-1243, 2000.
2. Fukasawa, K.; Fukasawa, K. M.; Iwamoto, H.; Hirose, J.; Harada,
M.: The HELLGH motif of rat liver dipeptidyl peptidase III is involved
in zinc coordination and the catalytic activity of the enzyme. Biochemistry 38:
8299-8303, 1999.
3. Fukasawa, K. M.; Fukasawa, K.; Harada, M.: Assignment of the dipeptidyl
peptidase III gene (DPP3) to human chromosome 11 band q12-q13.1 by
in situ hybridization. Cytogenet. Cell Genet. 88: 99-100, 2000.
*FIELD* CD
Patricia A. Hartz: 4/3/2002
*FIELD* ED
wwang: 10/14/2008
carol: 4/4/2002
carol: 4/3/2002