Full text data of DPP9
DPP9
(DPRP2)
[Confidence: low (only semi-automatic identification from reviews)]
Dipeptidyl peptidase 9; DP9; 3.4.14.5 (Dipeptidyl peptidase IV-related protein 2; DPRP-2; Dipeptidyl peptidase IX; DPP IX; Dipeptidyl peptidase-like protein 9; DPLP9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dipeptidyl peptidase 9; DP9; 3.4.14.5 (Dipeptidyl peptidase IV-related protein 2; DPRP-2; Dipeptidyl peptidase IX; DPP IX; Dipeptidyl peptidase-like protein 9; DPLP9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q86TI2
ID DPP9_HUMAN Reviewed; 863 AA.
AC Q86TI2; O75273; O75868; Q1ZZB8; Q6AI37; Q6UAL0; Q6ZMT2; Q6ZNJ5;
read moreAC Q8N2J7; Q8N3F5; Q8WXD8; Q96NT8; Q9BVR3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Dipeptidyl peptidase 9;
DE Short=DP9;
DE EC=3.4.14.5;
DE AltName: Full=Dipeptidyl peptidase IV-related protein 2;
DE Short=DPRP-2;
DE AltName: Full=Dipeptidyl peptidase IX;
DE Short=DPP IX;
DE AltName: Full=Dipeptidyl peptidase-like protein 9;
DE Short=DPLP9;
GN Name=DPP9; Synonyms=DPRP2;
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 2), AND TISSUE SPECIFICITY.
RX PubMed=12459266; DOI=10.1016/S0378-1119(02)01059-4;
RA Olsen C., Wagtmann N.;
RT "Identification and characterization of human DPP9, a novel homologue
RT of dipeptidyl peptidase IV.";
RL Gene 299:185-193(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Colon;
RX PubMed=12662155; DOI=10.1042/BJ20021914;
RA Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O.;
RT "Cloning and characterization of dipeptidyl peptidase 10, a new member
RT of an emerging subgroup of serine proteases.";
RL Biochem. J. 373:179-189(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15245913; DOI=10.1016/j.bbaexp.2004.03.010;
RA Ajami K., Abbott C.A., McCaughan G.W., Gorrell M.D.;
RT "Dipeptidyl peptidase 9 has two forms, a broad tissue distribution,
RT cytoplasmic localization and DPIV-like peptidase activity.";
RL Biochim. Biophys. Acta 1679:18-28(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=16475979; DOI=10.1042/BJ20060079;
RA Bjelke J.R., Christensen J., Nielsen P.F., Branner S., Kanstrup A.B.,
RA Wagtmann N., Rasmussen H.B.;
RT "Dipeptidyl peptidases 8 and 9: specificity and molecular
RT characterization compared with dipeptidyl peptidase IV.";
RL Biochem. J. 396:391-399(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 30-649 (ISOFORMS 1/3).
RC TISSUE=Glial tumor, Ovary, Spleen, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Skin;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORMS 1/2).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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).
CC -!- FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal
CC dipeptides from proteins having a Pro or Ala residue at position
CC 2.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
CC Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
CC Zaa is neither Pro nor hydroxyproline.
CC -!- ENZYME REGULATION: Inhibited by the serine proteinase inhibitor 4-
CC (2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-
CC isopropylfuorophosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=161 uM for Ala-Pro-AMC;
CC KM=180 uM for Ala-Pro-AFC;
CC pH dependence:
CC Optimum pH is 7.5-8.5. Little activity below pH 6.5;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-7475352, EBI-7475352;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Short;
CC IsoId=Q86TI2-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q86TI2-2; Sequence=VSP_013865;
CC Note=Incomplete sequence;
CC Name=3;
CC IsoId=Q86TI2-4; Sequence=VSP_013869;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC liver, heart and muscle, and lowest levels in brain.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33801.1; Type=Erroneous gene model prediction;
CC Sequence=AAC62840.1; Type=Erroneous gene model prediction;
CC Sequence=AAH37948.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAL47179.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAO73880.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB70784.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC11362.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC85150.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=BAD18643.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=CAD39039.3; Type=Frameshift; Positions=432, 460;
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DR EMBL; AF452102; AAL47179.1; ALT_INIT; mRNA.
DR EMBL; AY172660; AAO17262.1; -; mRNA.
DR EMBL; AF542510; AAO73880.2; ALT_INIT; mRNA.
DR EMBL; AY374518; AAQ83119.1; -; mRNA.
DR EMBL; DQ417928; ABD83624.1; -; mRNA.
DR EMBL; AK054656; BAB70784.1; ALT_INIT; mRNA.
DR EMBL; AK075030; BAC11362.1; ALT_INIT; mRNA.
DR EMBL; AK122654; BAG53644.1; -; mRNA.
DR EMBL; AK131100; BAC85150.1; ALT_SEQ; mRNA.
DR EMBL; AK131499; BAD18643.1; ALT_SEQ; mRNA.
DR EMBL; AC005594; AAC33801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005783; AAC62840.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471139; EAW69199.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69201.1; -; Genomic_DNA.
DR EMBL; BC000970; AAH00970.1; -; mRNA.
DR EMBL; BC037948; AAH37948.1; ALT_INIT; mRNA.
DR EMBL; AL834376; CAD39039.3; ALT_FRAME; mRNA.
DR EMBL; CR627380; CAH10477.1; -; mRNA.
DR RefSeq; NP_631898.3; NM_139159.4.
DR RefSeq; XP_005259730.1; XM_005259673.1.
DR UniGene; Hs.515081; -.
DR ProteinModelPortal; Q86TI2; -.
DR SMR; Q86TI2; 489-861.
DR MINT; MINT-4535936; -.
DR BindingDB; Q86TI2; -.
DR ChEMBL; CHEMBL4793; -.
DR MEROPS; S09.019; -.
DR PhosphoSite; Q86TI2; -.
DR DMDM; 67460390; -.
DR PaxDb; Q86TI2; -.
DR PRIDE; Q86TI2; -.
DR DNASU; 91039; -.
DR Ensembl; ENST00000262960; ENSP00000262960; ENSG00000142002.
DR Ensembl; ENST00000594671; ENSP00000472224; ENSG00000142002.
DR Ensembl; ENST00000598800; ENSP00000469603; ENSG00000142002.
DR GeneID; 91039; -.
DR KEGG; hsa:91039; -.
DR CTD; 91039; -.
DR GeneCards; GC19M004675; -.
DR H-InvDB; HIX0027578; -.
DR HGNC; HGNC:18648; DPP9.
DR HPA; HPA036059; -.
DR MIM; 608258; gene.
DR neXtProt; NX_Q86TI2; -.
DR Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR PharmGKB; PA38620; -.
DR eggNOG; COG1506; -.
DR HOVERGEN; HBG061620; -.
DR InParanoid; Q86TI2; -.
DR KO; K08656; -.
DR OMA; PLDNFCE; -.
DR OrthoDB; EOG7XWPN8; -.
DR SABIO-RK; Q86TI2; -.
DR ChiTaRS; DPP9; human.
DR GeneWiki; DPP9; -.
DR GenomeRNAi; 91039; -.
DR NextBio; 77078; -.
DR PRO; PR:Q86TI2; -.
DR ArrayExpress; Q86TI2; -.
DR Bgee; Q86TI2; -.
DR Genevestigator; Q86TI2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminopeptidase; Complete proteome;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 863 Dipeptidyl peptidase 9.
FT /FTId=PRO_0000122415.
FT ACT_SITE 730 730 Charge relay system (By similarity).
FT ACT_SITE 808 808 Charge relay system (By similarity).
FT ACT_SITE 840 840 Charge relay system (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 1 M -> MRKVKKLRLDKENTGSWRSFSLNSEGAERM (in
FT isoform 2).
FT /FTId=VSP_013865.
FT VAR_SEQ 832 858 Missing (in isoform 3).
FT /FTId=VSP_013869.
FT CONFLICT 204 204 I -> N (in Ref. 3; AAO73880/AAQ83119).
FT CONFLICT 461 461 L -> F (in Ref. 9; CAD39039).
FT CONFLICT 571 571 C -> W (in Ref. 5; BAC85150).
FT CONFLICT 709 709 L -> P (in Ref. 5; BAD18643).
FT CONFLICT 753 753 G -> C (in Ref. 5; BAB70784).
SQ SEQUENCE 863 AA; 98263 MW; 40FE0B78E26CDED5 CRC64;
MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN KAPHDFQFVQ
KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL LLLSWKQMLD HFQATPHHGV
YSREEELLRE RKRLGVFGIT SYDFHSESGL FLFQASNSLF HCRDGGKNGF MVSPMKPLEI
KTQCSGPRMD PKICPADPAF FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG
VATFVIQEEF DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT
DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE YIARAGWTRD
GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA RAVPRNVQPY VVYEEVTNVW
INVHDIFYPF PQSEGEDELC FLRANECKTG FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK
CPIKEEIALT SGEWEVLARH GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR
LTTPGFSHSC SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS
CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ LVNNSFKGIK
YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV EIEDQVEGLQ FVAEKYGFID
LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA IAGAPVTVWM AYDTGYTERY MDVPENNQHG
YEAGSVALHV EKLPNEPNRL LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH
SIRCPESGEH YEVTLLHFLQ EYL
//
ID DPP9_HUMAN Reviewed; 863 AA.
AC Q86TI2; O75273; O75868; Q1ZZB8; Q6AI37; Q6UAL0; Q6ZMT2; Q6ZNJ5;
read moreAC Q8N2J7; Q8N3F5; Q8WXD8; Q96NT8; Q9BVR3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Dipeptidyl peptidase 9;
DE Short=DP9;
DE EC=3.4.14.5;
DE AltName: Full=Dipeptidyl peptidase IV-related protein 2;
DE Short=DPRP-2;
DE AltName: Full=Dipeptidyl peptidase IX;
DE Short=DPP IX;
DE AltName: Full=Dipeptidyl peptidase-like protein 9;
DE Short=DPLP9;
GN Name=DPP9; Synonyms=DPRP2;
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 2), AND TISSUE SPECIFICITY.
RX PubMed=12459266; DOI=10.1016/S0378-1119(02)01059-4;
RA Olsen C., Wagtmann N.;
RT "Identification and characterization of human DPP9, a novel homologue
RT of dipeptidyl peptidase IV.";
RL Gene 299:185-193(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Colon;
RX PubMed=12662155; DOI=10.1042/BJ20021914;
RA Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O.;
RT "Cloning and characterization of dipeptidyl peptidase 10, a new member
RT of an emerging subgroup of serine proteases.";
RL Biochem. J. 373:179-189(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15245913; DOI=10.1016/j.bbaexp.2004.03.010;
RA Ajami K., Abbott C.A., McCaughan G.W., Gorrell M.D.;
RT "Dipeptidyl peptidase 9 has two forms, a broad tissue distribution,
RT cytoplasmic localization and DPIV-like peptidase activity.";
RL Biochim. Biophys. Acta 1679:18-28(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=16475979; DOI=10.1042/BJ20060079;
RA Bjelke J.R., Christensen J., Nielsen P.F., Branner S., Kanstrup A.B.,
RA Wagtmann N., Rasmussen H.B.;
RT "Dipeptidyl peptidases 8 and 9: specificity and molecular
RT characterization compared with dipeptidyl peptidase IV.";
RL Biochem. J. 396:391-399(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 30-649 (ISOFORMS 1/3).
RC TISSUE=Glial tumor, Ovary, Spleen, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Skin;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORMS 1/2).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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).
CC -!- FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal
CC dipeptides from proteins having a Pro or Ala residue at position
CC 2.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
CC Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
CC Zaa is neither Pro nor hydroxyproline.
CC -!- ENZYME REGULATION: Inhibited by the serine proteinase inhibitor 4-
CC (2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-
CC isopropylfuorophosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=161 uM for Ala-Pro-AMC;
CC KM=180 uM for Ala-Pro-AFC;
CC pH dependence:
CC Optimum pH is 7.5-8.5. Little activity below pH 6.5;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-7475352, EBI-7475352;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Short;
CC IsoId=Q86TI2-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q86TI2-2; Sequence=VSP_013865;
CC Note=Incomplete sequence;
CC Name=3;
CC IsoId=Q86TI2-4; Sequence=VSP_013869;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC liver, heart and muscle, and lowest levels in brain.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33801.1; Type=Erroneous gene model prediction;
CC Sequence=AAC62840.1; Type=Erroneous gene model prediction;
CC Sequence=AAH37948.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAL47179.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAO73880.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB70784.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC11362.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC85150.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=BAD18643.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=CAD39039.3; Type=Frameshift; Positions=432, 460;
CC -----------------------------------------------------------------------
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DR EMBL; AF452102; AAL47179.1; ALT_INIT; mRNA.
DR EMBL; AY172660; AAO17262.1; -; mRNA.
DR EMBL; AF542510; AAO73880.2; ALT_INIT; mRNA.
DR EMBL; AY374518; AAQ83119.1; -; mRNA.
DR EMBL; DQ417928; ABD83624.1; -; mRNA.
DR EMBL; AK054656; BAB70784.1; ALT_INIT; mRNA.
DR EMBL; AK075030; BAC11362.1; ALT_INIT; mRNA.
DR EMBL; AK122654; BAG53644.1; -; mRNA.
DR EMBL; AK131100; BAC85150.1; ALT_SEQ; mRNA.
DR EMBL; AK131499; BAD18643.1; ALT_SEQ; mRNA.
DR EMBL; AC005594; AAC33801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005783; AAC62840.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471139; EAW69199.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69201.1; -; Genomic_DNA.
DR EMBL; BC000970; AAH00970.1; -; mRNA.
DR EMBL; BC037948; AAH37948.1; ALT_INIT; mRNA.
DR EMBL; AL834376; CAD39039.3; ALT_FRAME; mRNA.
DR EMBL; CR627380; CAH10477.1; -; mRNA.
DR RefSeq; NP_631898.3; NM_139159.4.
DR RefSeq; XP_005259730.1; XM_005259673.1.
DR UniGene; Hs.515081; -.
DR ProteinModelPortal; Q86TI2; -.
DR SMR; Q86TI2; 489-861.
DR MINT; MINT-4535936; -.
DR BindingDB; Q86TI2; -.
DR ChEMBL; CHEMBL4793; -.
DR MEROPS; S09.019; -.
DR PhosphoSite; Q86TI2; -.
DR DMDM; 67460390; -.
DR PaxDb; Q86TI2; -.
DR PRIDE; Q86TI2; -.
DR DNASU; 91039; -.
DR Ensembl; ENST00000262960; ENSP00000262960; ENSG00000142002.
DR Ensembl; ENST00000594671; ENSP00000472224; ENSG00000142002.
DR Ensembl; ENST00000598800; ENSP00000469603; ENSG00000142002.
DR GeneID; 91039; -.
DR KEGG; hsa:91039; -.
DR CTD; 91039; -.
DR GeneCards; GC19M004675; -.
DR H-InvDB; HIX0027578; -.
DR HGNC; HGNC:18648; DPP9.
DR HPA; HPA036059; -.
DR MIM; 608258; gene.
DR neXtProt; NX_Q86TI2; -.
DR Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR PharmGKB; PA38620; -.
DR eggNOG; COG1506; -.
DR HOVERGEN; HBG061620; -.
DR InParanoid; Q86TI2; -.
DR KO; K08656; -.
DR OMA; PLDNFCE; -.
DR OrthoDB; EOG7XWPN8; -.
DR SABIO-RK; Q86TI2; -.
DR ChiTaRS; DPP9; human.
DR GeneWiki; DPP9; -.
DR GenomeRNAi; 91039; -.
DR NextBio; 77078; -.
DR PRO; PR:Q86TI2; -.
DR ArrayExpress; Q86TI2; -.
DR Bgee; Q86TI2; -.
DR Genevestigator; Q86TI2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminopeptidase; Complete proteome;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 863 Dipeptidyl peptidase 9.
FT /FTId=PRO_0000122415.
FT ACT_SITE 730 730 Charge relay system (By similarity).
FT ACT_SITE 808 808 Charge relay system (By similarity).
FT ACT_SITE 840 840 Charge relay system (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 1 M -> MRKVKKLRLDKENTGSWRSFSLNSEGAERM (in
FT isoform 2).
FT /FTId=VSP_013865.
FT VAR_SEQ 832 858 Missing (in isoform 3).
FT /FTId=VSP_013869.
FT CONFLICT 204 204 I -> N (in Ref. 3; AAO73880/AAQ83119).
FT CONFLICT 461 461 L -> F (in Ref. 9; CAD39039).
FT CONFLICT 571 571 C -> W (in Ref. 5; BAC85150).
FT CONFLICT 709 709 L -> P (in Ref. 5; BAD18643).
FT CONFLICT 753 753 G -> C (in Ref. 5; BAB70784).
SQ SEQUENCE 863 AA; 98263 MW; 40FE0B78E26CDED5 CRC64;
MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN KAPHDFQFVQ
KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL LLLSWKQMLD HFQATPHHGV
YSREEELLRE RKRLGVFGIT SYDFHSESGL FLFQASNSLF HCRDGGKNGF MVSPMKPLEI
KTQCSGPRMD PKICPADPAF FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG
VATFVIQEEF DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT
DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE YIARAGWTRD
GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA RAVPRNVQPY VVYEEVTNVW
INVHDIFYPF PQSEGEDELC FLRANECKTG FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK
CPIKEEIALT SGEWEVLARH GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR
LTTPGFSHSC SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS
CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ LVNNSFKGIK
YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV EIEDQVEGLQ FVAEKYGFID
LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA IAGAPVTVWM AYDTGYTERY MDVPENNQHG
YEAGSVALHV EKLPNEPNRL LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH
SIRCPESGEH YEVTLLHFLQ EYL
//
MIM
608258
*RECORD*
*FIELD* NO
608258
*FIELD* TI
*608258 DIPEPTIDYL PEPTIDASE IX; DPP9
;;DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2; DPRP2
read more*FIELD* TX
CLONING
By searching an EST database for sequences similar to the catalytic
domain of DPP4 (102720), followed by PCR and 5-prime RACE of skeletal
muscle and chronic myelogenous leukemia (K-562) cell line cDNA
libraries, Olsen and Wagtmann (2002) cloned DPP9. The deduced 863-amino
acid protein has a calculated molecular mass of about 98 kD. An
alternatively spliced transcript cloned from the K-562 cell line cDNA
library lacks exon 2 in the 5-prime untranslated region and encodes the
same deduced protein. Use of an alternate start codon would result in a
DPP9 protein with 29 more amino acids. DPP9 contains an active-site
serine protease motif (GWSYG) and 2 N-glycosylation sites. The order and
spacing of the serine, aspartic acid, and histidine residues that form
the catalytic triad in DPP9 are conserved with DPP4. DPP9 lacks an
N-terminal signal sequence and transmembrane domain. It shares 58% amino
acid identity with DPP8 (606879) and 92% identity with mouse Dpp9.
Northern blot analysis detected ubiquitous expression of a 4.4-kb
transcript. Highest expression was in skeletal muscle, heart, and liver,
and lowest expression was in brain. Western blot analysis detected
expression of DPP9 in all cell lines examined, including a
T-lymphoblastoid cell line that does not express DPP4. In vitro
translation resulted in a soluble protein with an apparent molecular
mass of 98 kD by SDS-PAGE.
By PCR, Qi et al. (2003) cloned DPP9 from a colon cDNA library. DPP9
shares 19% amino acid identity with DPP4, with the greatest similarity
in the C-terminal sequences. It shares 20% amino acid identity with
DPP10 (608209). Northern blot analysis revealed ubiquitous expression of
a 4.5-kb transcript, with highest expression in liver and muscle.
Transcripts of 5.0 and 1.4 kb were also found in liver. Western blot
analysis detected recombinant DPP9 expressed as a cytosolic protein of
100 kD.
GENE FUNCTION
By biochemical analysis using several synthetic peptides, Qi et al.
(2003) determined that DPP9 and DPP8 showed prolyl oligopeptidase
activity similar to that displayed by DPP4. Maximum activity was
measured between pH 7.5 and 8.5. Activity was inhibited by broad serine
protease inhibitors, but not by aprotinin, which is specific for
trypsin-like serine proteases.
GENE STRUCTURE
Olsen and Wagtmann (2002) determined that the DPP9 gene contains 22
exons and spans 48.7 kb. The promoter region has features typical for
promoters of housekeeping genes, namely a high GC content, multiple
sites for initiation of transcription, and lack of a TATAA box.
MAPPING
By genomic sequence analysis, Olsen and Wagtmann (2002) mapped the DPP9
gene to chromosome 19p13.3. They mapped the mouse Dpp9 gene to a region
of mouse chromosome 17 that shows homology of synteny with human
chromosome 19p13.3.
*FIELD* RF
1. Olsen, C.; Wagtmann, N.: Identification and characterization of
human DPP9, a novel homologue of dipeptidyl peptidase IV. Gene 299:
185-193, 2002.
2. Qi, S. Y.; Riviere, P. J.; Trojnar, J.; Junien, J.-L.; Akinsanya,
K. O.: Cloning and characterization of dipeptidyl peptidase 10, a
new member of an emerging subgroup of serine proteases. Biochem.
J. 373: 179-189, 2003.
*FIELD* CD
Patricia A. Hartz: 11/13/2003
*FIELD* ED
mgross: 11/13/2003
*RECORD*
*FIELD* NO
608258
*FIELD* TI
*608258 DIPEPTIDYL PEPTIDASE IX; DPP9
;;DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2; DPRP2
read more*FIELD* TX
CLONING
By searching an EST database for sequences similar to the catalytic
domain of DPP4 (102720), followed by PCR and 5-prime RACE of skeletal
muscle and chronic myelogenous leukemia (K-562) cell line cDNA
libraries, Olsen and Wagtmann (2002) cloned DPP9. The deduced 863-amino
acid protein has a calculated molecular mass of about 98 kD. An
alternatively spliced transcript cloned from the K-562 cell line cDNA
library lacks exon 2 in the 5-prime untranslated region and encodes the
same deduced protein. Use of an alternate start codon would result in a
DPP9 protein with 29 more amino acids. DPP9 contains an active-site
serine protease motif (GWSYG) and 2 N-glycosylation sites. The order and
spacing of the serine, aspartic acid, and histidine residues that form
the catalytic triad in DPP9 are conserved with DPP4. DPP9 lacks an
N-terminal signal sequence and transmembrane domain. It shares 58% amino
acid identity with DPP8 (606879) and 92% identity with mouse Dpp9.
Northern blot analysis detected ubiquitous expression of a 4.4-kb
transcript. Highest expression was in skeletal muscle, heart, and liver,
and lowest expression was in brain. Western blot analysis detected
expression of DPP9 in all cell lines examined, including a
T-lymphoblastoid cell line that does not express DPP4. In vitro
translation resulted in a soluble protein with an apparent molecular
mass of 98 kD by SDS-PAGE.
By PCR, Qi et al. (2003) cloned DPP9 from a colon cDNA library. DPP9
shares 19% amino acid identity with DPP4, with the greatest similarity
in the C-terminal sequences. It shares 20% amino acid identity with
DPP10 (608209). Northern blot analysis revealed ubiquitous expression of
a 4.5-kb transcript, with highest expression in liver and muscle.
Transcripts of 5.0 and 1.4 kb were also found in liver. Western blot
analysis detected recombinant DPP9 expressed as a cytosolic protein of
100 kD.
GENE FUNCTION
By biochemical analysis using several synthetic peptides, Qi et al.
(2003) determined that DPP9 and DPP8 showed prolyl oligopeptidase
activity similar to that displayed by DPP4. Maximum activity was
measured between pH 7.5 and 8.5. Activity was inhibited by broad serine
protease inhibitors, but not by aprotinin, which is specific for
trypsin-like serine proteases.
GENE STRUCTURE
Olsen and Wagtmann (2002) determined that the DPP9 gene contains 22
exons and spans 48.7 kb. The promoter region has features typical for
promoters of housekeeping genes, namely a high GC content, multiple
sites for initiation of transcription, and lack of a TATAA box.
MAPPING
By genomic sequence analysis, Olsen and Wagtmann (2002) mapped the DPP9
gene to chromosome 19p13.3. They mapped the mouse Dpp9 gene to a region
of mouse chromosome 17 that shows homology of synteny with human
chromosome 19p13.3.
*FIELD* RF
1. Olsen, C.; Wagtmann, N.: Identification and characterization of
human DPP9, a novel homologue of dipeptidyl peptidase IV. Gene 299:
185-193, 2002.
2. Qi, S. Y.; Riviere, P. J.; Trojnar, J.; Junien, J.-L.; Akinsanya,
K. O.: Cloning and characterization of dipeptidyl peptidase 10, a
new member of an emerging subgroup of serine proteases. Biochem.
J. 373: 179-189, 2003.
*FIELD* CD
Patricia A. Hartz: 11/13/2003
*FIELD* ED
mgross: 11/13/2003