DPP4_HUMAN
ID DPP4_HUMAN Reviewed; 766 AA.
AC P27487; Q53TN1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Dipeptidyl peptidase 4 {ECO:0000305};
DE EC=3.4.14.5 {ECO:0000269|PubMed:10593948};
DE AltName: Full=ADABP;
DE AltName: Full=Adenosine deaminase complexing protein 2;
DE Short=ADCP-2;
DE AltName: Full=Dipeptidyl peptidase IV;
DE Short=DPP IV;
DE AltName: Full=T-cell activation antigen CD26;
DE AltName: Full=TP103;
DE AltName: CD_antigen=CD26;
DE Contains:
DE RecName: Full=Dipeptidyl peptidase 4 membrane form;
DE AltName: Full=Dipeptidyl peptidase IV membrane form;
DE Contains:
DE RecName: Full=Dipeptidyl peptidase 4 soluble form;
DE AltName: Full=Dipeptidyl peptidase IV soluble form;
GN Name=DPP4 {ECO:0000312|HGNC:HGNC:3009}; Synonyms=ADCP2, CD26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1352704; DOI=10.1016/0167-4781(92)90036-y;
RA Misumi Y., Hayashi Y., Arakawa F., Ikehara Y.;
RT "Molecular cloning and sequence analysis of human dipeptidyl peptidase IV,
RT a serine proteinase on the cell surface.";
RL Biochim. Biophys. Acta 1131:333-336(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=1347043; DOI=10.1016/s0021-9258(18)42906-7;
RA Darmoul D., Lacasa M., Baricault L., Marguet D., Sapin C., Trotot P.,
RA Barbat A.;
RT "Dipeptidyl peptidase IV (CD 26) gene expression in enterocyte-like colon
RT cancer cell lines HT-29 and Caco-2. Cloning of the complete human coding
RT sequence and changes of dipeptidyl peptidase IV mRNA levels during cell
RT differentiation.";
RL J. Biol. Chem. 267:4824-4833(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=1352530;
RA Tanaka T., Camerini D., Seed B., Torimoto Y., Dang N.H., Kameoka J.,
RA Dahlberg H.N., Schlossman S.F., Morimoto C.;
RT "Cloning and functional expression of the T cell activation antigen CD26.";
RL J. Immunol. 149:481-486(1992).
RN [4]
RP ERRATUM OF PUBMED:1352530.
RX PubMed=8094732;
RA Tanaka T.;
RL J. Immunol. 150:2090-2090(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7927537; DOI=10.1007/bf01246674;
RA Abbott C.A., Baker E., Sutherland G.R., McCaughan G.W.;
RT "Genomic organization, exact localization, and tissue expression of the
RT human CD26 (dipeptidyl peptidase IV) gene.";
RL Immunogenetics 40:331-338(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Uterus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 545-766.
RC TISSUE=Colon;
RX PubMed=1977364; DOI=10.1111/j.1469-1809.1990.tb00377.x;
RA Darmoul D., Lacasa M., Chantret I., Swallow D., Trugnan G.;
RT "Isolation of a cDNA probe for the human intestinal dipeptidylpeptidase IV
RT and assignment of the gene locus DPP4 to chromosome 2.";
RL Ann. Hum. Genet. 54:191-197(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=7487939; DOI=10.1042/bj3110835;
RA Boehm S.K., Gum J.R. Jr., Erickson R.H., Hicks J.W., Kim Y.S.;
RT "Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation
RT from a TATA-less GC-rich sequence characteristic of a housekeeping gene
RT promoter.";
RL Biochem. J. 311:835-843(1995).
RN [12]
RP PROTEIN SEQUENCE OF 1-22, AND TISSUE SPECIFICITY.
RX PubMed=1677636; DOI=10.1016/0016-5085(91)90517-o;
RA Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.;
RT "Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small
RT intestine and colon.";
RL Gastroenterology 101:618-625(1991).
RN [13]
RP PROTEIN SEQUENCE OF 29-34 AND 39-43, FUNCTION, INTERACTION WITH ADA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10951221; DOI=10.1046/j.1432-1327.2000.01634.x;
RA Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R.,
RA Haemers A., Scharpe S., De Meester I.;
RT "Molecular characterization of dipeptidyl peptidase activity in serum:
RT soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-
RT Pro dipeptides.";
RL Eur. J. Biochem. 267:5608-5613(2000).
RN [14]
RP PROTEIN SEQUENCE OF 659-669, FUNCTION, ACTIVITY REGULATION, INTERACTION
RP WITH GPC3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17549790; DOI=10.1002/pmic.200600654;
RA Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.;
RT "The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and
RT inhibits the dipeptidyl peptidase activity of CD26.";
RL Proteomics 7:2300-2310(2007).
RN [15]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=8096237; DOI=10.1084/jem.177.4.1135;
RA Morrison M.E., Vijayasaradhi S., Engelstein D., Albino A.P., Houghton A.N.;
RT "A marker for neoplastic progression of human melanocytes is a cell surface
RT ectopeptidase.";
RL J. Exp. Med. 177:1135-1143(1993).
RN [16]
RP INTERACTION WITH ADA, AND SUBCELLULAR LOCATION.
RX PubMed=8101391; DOI=10.1126/science.8101391;
RA Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.;
RT "Direct association of adenosine deaminase with a T cell activation
RT antigen, CD26.";
RL Science 261:466-469(1993).
RN [17]
RP INTERACTION WITH ADA.
RX PubMed=7907293; DOI=10.1002/eji.1830240311;
RA De Meester I., Vanham G., Kestens L., Vanhoof G., Bosmans E., Gigase P.,
RA Scharpe S.;
RT "Binding of adenosine deaminase to the lymphocyte surface via CD26.";
RL Eur. J. Immunol. 24:566-570(1994).
RN [18]
RP ASSOCIATION WITH COLLAGEN.
RX PubMed=8526932; DOI=10.1006/bbrc.1995.2782;
RA Loster K., Zeilinger K., Schuppan D., Reutter W.;
RT "The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the
RT collagen-binding site.";
RL Biochem. Biophys. Res. Commun. 217:341-348(1995).
RN [19]
RP INDUCTION.
RX PubMed=9413751; DOI=10.1016/s0171-2985(97)80084-8;
RA Cordero O.J., Salgado F.J., Vinuela J.E., Nogueira M.;
RT "Interleukin-12 enhances CD26 expression and dipeptidyl peptidase IV
RT function on human activated lymphocytes.";
RL Immunobiology 197:522-533(1997).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF GLU-205 AND GLU-206.
RX PubMed=10570924; DOI=10.1016/s0014-5793(99)01166-7;
RA Abbott C.A., McCaughan G.W., Gorrell M.D.;
RT "Two highly conserved glutamic acid residues in the predicted beta
RT propeller domain of dipeptidyl peptidase IV are required for its enzyme
RT activity.";
RL FEBS Lett. 458:278-284(1999).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10593948; DOI=10.1074/jbc.274.51.36505;
RA Park J.E., Lenter M.C., Zimmermann R.N., Garin-Chesa P., Old L.J.,
RA Rettig W.J.;
RT "Fibroblast activation protein, a dual specificity serine protease
RT expressed in reactive human tumor stromal fibroblasts.";
RL J. Biol. Chem. 274:36505-36512(1999).
RN [22]
RP ASSOCIATION WITH CANCER.
RX PubMed=11027426; DOI=10.1054/bjoc.2000.1410;
RA Cordero O.J., Ayude D., Nogueira M., Rodriguez-Berrocal F.J.,
RA de la Cadena M.P.;
RT "Preoperative serum CD26 levels: diagnostic efficiency and predictive value
RT for colorectal cancer.";
RL Br. J. Cancer 83:1139-1146(2000).
RN [23]
RP INDUCTION.
RX PubMed=10880264; DOI=10.1006/cyto.1999.0643;
RA Salgado F.J., Vela E., Martin M., Franco R., Nogueira M., Cordero O.J.;
RT "Mechanisms of CD26/dipeptidyl peptidase IV cytokine-dependent regulation
RT on human activated lymphocytes.";
RL Cytokine 12:1136-1141(2000).
RN [24]
RP FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10900005; DOI=10.1073/pnas.97.15.8439;
RA Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H.,
RA Schlossman S.F., Morimoto C.;
RT "Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor
RT II receptor contributes to T cell activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000).
RN [25]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11772392; DOI=10.1042/0264-6021:3610203;
RA Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C.,
RA Hovanessian A., Casado V., Lluis C., Franco R.;
RT "Regulation of epithelial and lymphocyte cell adhesion by adenosine
RT deaminase-CD26 interaction.";
RL Biochem. J. 361:203-209(2002).
RN [26]
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=11773049; DOI=10.1074/jbc.m109357200;
RA Alfalah M., Jacob R., Naim H.Y.;
RT "Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical
RT membrane through the concerted action of N- and O-glycans as well as
RT association with lipid microdomains.";
RL J. Biol. Chem. 277:10683-10690(2002).
RN [27]
RP INTERACTION WITH PTPRC, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12676959; DOI=10.1074/jbc.m212978200;
RA Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R.,
RA Cordero O.J., Nogueira M.;
RT "A role for interleukin-12 in the regulation of T cell plasma membrane
RT compartmentation.";
RL J. Biol. Chem. 278:24849-24857(2003).
RN [28]
RP INTERACTION WITH ADA.
RX PubMed=15016824; DOI=10.1074/jbc.m401023200;
RA Gonzalez-Gronow M., Hershfield M.S., Arredondo-Vega F.X., Pizzo S.V.;
RT "Cell surface adenosine deaminase binds and stimulates plasminogen
RT activation on 1-LN human prostate cancer cells.";
RL J. Biol. Chem. 279:20993-20998(2004).
RN [29]
RP HOMODIMERIZATION, AND MUTAGENESIS OF HIS-750.
RX PubMed=15448155; DOI=10.1074/jbc.m406185200;
RA Chien C.H., Huang L.H., Chou C.Y., Chen Y.S., Han Y.S., Chang G.G.,
RA Liang P.H., Chen X.;
RT "One site mutation disrupts dimer formation in human DPP-IV proteins.";
RL J. Biol. Chem. 279:52338-52345(2004).
RN [30]
RP FUNCTION, INTERACTION WITH ADA, AND MUTAGENESIS OF ASN-85; ASN-92; ASN-150;
RP ASN-219; ASN-229; ASN-281; ASN-321; ASN-520 AND ASN-685.
RX PubMed=14691230; DOI=10.1110/ps.03352504;
RA Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E., Sang B.C.,
RA Wijnands R.A., Webb D.R., Swanson R.V.;
RT "N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on
RT enzyme activity, homodimer formation, and adenosine deaminase binding.";
RL Protein Sci. 13:145-154(2004).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [32]
RP INDUCTION BY HYPOXIA.
RX PubMed=16670267; DOI=10.1182/blood-2006-02-001016;
RA Eltzschig H.K., Faigle M., Knapp S., Karhausen J., Ibla J., Rosenberger P.,
RA Odegard K.C., Laussen P.C., Thompson L.F., Colgan S.P.;
RT "Endothelial catabolism of extracellular adenosine during hypoxia: the role
RT of surface adenosine deaminase and CD26.";
RL Blood 108:1602-1610(2006).
RN [33]
RP FUNCTION, HETERODIMERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16651416; DOI=10.1158/0008-5472.can-05-1245;
RA Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.;
RT "The protease complex consisting of dipeptidyl peptidase IV and seprase
RT plays a role in the migration and invasion of human endothelial cells in
RT collagenous matrices.";
RL Cancer Res. 66:4652-4661(2006).
RN [34]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16254193; DOI=10.1373/clinchem.2005.057638;
RA Brandt I., Lambeir A.M., Ketelslegers J.M., Vanderheyden M., Scharpe S.,
RA De Meester I.;
RT "Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into
RT its des-SerPro form.";
RL Clin. Chem. 52:82-87(2006).
RN [35]
RP FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION,
RP INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-750.
RX PubMed=17287217; DOI=10.1074/jbc.m609157200;
RA Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N.,
RA Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.;
RT "Caveolin-1 triggers T-cell activation via CD26 in association with
RT CARMA1.";
RL J. Biol. Chem. 282:10117-10131(2007).
RN [36]
RP FUNCTION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=18708048; DOI=10.1016/j.yexcr.2008.07.024;
RA Shin J.W., Jurisic G., Detmar M.;
RT "Lymphatic-specific expression of dipeptidyl peptidase IV and its dual role
RT in lymphatic endothelial function.";
RL Exp. Cell Res. 314:3048-3056(2008).
RN [37]
RP REVIEW.
RX PubMed=19557413; DOI=10.1007/s00262-009-0728-1;
RA Cordero O.J., Salgado F.J., Nogueira M.;
RT "On the origin of serum CD26 and its altered concentration in cancer
RT patients.";
RL Cancer Immunol. Immunother. 58:1723-1747(2009).
RN [38]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-92; ASN-150; ASN-520 AND
RP ASN-685.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [39]
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., Buerckstuemmer T.,
RA 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 [40]
RP INTERACTION WITH HUMAN CORONAVIRUS-EMC SPIKE PROTEIN.
RX PubMed=23486063; DOI=10.1038/nature12005;
RA Raj V.S., Mou H., Smits S.L., Dekkers D.H., Muller M.A., Dijkman R.,
RA Muth D., Demmers J.A., Zaki A., Fouchier R.A., Thiel V., Drosten C.,
RA Rottier P.J., Osterhaus A.D., Bosch B.J., Haagmans B.L.;
RT "Dipeptidyl peptidase 4 is a functional receptor for the emerging human
RT coronavirus-EMC.";
RL Nature 495:251-254(2013).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-766 IN COMPLEX WITH INHIBITOR,
RP AND HOMODIMERIZATION.
RX PubMed=12832764; DOI=10.1107/s0907444903010059;
RA Oefner C., D'Arcy A., Mac Sweeney A., Pierau S., Gardiner R., Dale G.E.;
RT "High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and
RT its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-
RT cyano-(S)-pyrrolidine.";
RL Acta Crystallogr. D 59:1206-1212(2003).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION,
RP GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, AND
RP DISULFIDE BONDS.
RX PubMed=12646248; DOI=10.1016/s0006-291x(03)00258-4;
RA Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H.,
RA Sugiyama S., Inaka K., Yamamoto A., Shimizu R.;
RT "The structure and function of human dipeptidyl peptidase IV, possessing a
RT unique eight-bladed beta-propeller fold.";
RL Biochem. Biophys. Res. Commun. 302:849-854(2003).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION,
RP GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321 AND
RP ASN-520, AND DISULFIDE BONDS.
RX PubMed=12483204; DOI=10.1038/nsb882;
RA Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.;
RT "Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a
RT substrate analog.";
RL Nat. Struct. Biol. 10:19-25(2003).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION,
RP GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, AND DISULFIDE BONDS.
RX PubMed=12906826; DOI=10.1016/s0969-2126(03)00160-6;
RA Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.;
RT "Structural basis of proline-specific exopeptidase activity as observed in
RT human dipeptidyl peptidase-IV.";
RL Structure 11:947-959(2003).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 39-766, AND GLYCOSYLATION AT
RP ASN-85; ASN-92; ASN-150; ASN-219; ASN-229 AND ASN-520.
RX PubMed=20684603; DOI=10.1021/jm100634a;
RA Meng W., Brigance R.P., Chao H.J., Fura A., Harrity T., Marcinkeviciene J.,
RA O'Connor S.P., Tamura J.K., Xie D., Zhang Y., Klei H.E., Kish K.,
RA Weigelt C.A., Turdi H., Wang A., Zahler R., Kirby M.S., Hamann L.G.;
RT "Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-
RT a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4
RT (DPP4) inhibitors.";
RL J. Med. Chem. 53:5620-5628(2010).
RN [47] {ECO:0007744|PDB:4L72}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 39-766 IN COMPLEX WITH MERS-COV
RP SPIKE GLYCOPROTEIN, GLYCOSYLATION AT ASN-85; ASN-92; ASN-150; ASN-219;
RP ASN-229; ASN-281; ASN-321 AND ASN-520, INTERACTION WITH MERS-COV SPIKE
RP GLYCOPROTEIN (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=23835475; DOI=10.1038/cr.2013.92;
RA Wang N., Shi X., Jiang L., Zhang S., Wang D., Tong P., Guo D., Fu L.,
RA Cui Y., Liu X., Arledge K.C., Chen Y.H., Zhang L., Wang X.;
RT "Structure of MERS-CoV spike receptor-binding domain complexed with human
RT receptor DPP4.";
RL Cell Res. 23:986-993(2013).
RN [48]
RP VARIANT ILE-266.
RX PubMed=32867305; DOI=10.3390/genes11091010;
RA Latini A., Agolini E., Novelli A., Borgiani P., Giannini R., Gravina P.,
RA Smarrazzo A., Dauri M., Andreoni M., Rogliani P., Bernardini S.,
RA Helmer-Citterich M., Biancolella M., Novelli G.;
RT "COVID-19 and Genetic Variants of Protein Involved in the SARS-CoV-2 Entry
RT into the Host Cells.";
RL Genes (Basel) 11:0-0(2020).
CC -!- FUNCTION: Cell surface glycoprotein receptor involved in the
CC costimulatory signal essential for T-cell receptor (TCR)-mediated T-
CC cell activation (PubMed:10951221, PubMed:10900005, PubMed:11772392,
CC PubMed:17287217). Acts as a positive regulator of T-cell coactivation,
CC by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10951221,
CC PubMed:10900005, PubMed:11772392, PubMed:14691230). Its binding to CAV1
CC and CARD11 induces T-cell proliferation and NF-kappa-B activation in a
CC T-cell receptor/CD3-dependent manner (PubMed:17287217). Its interaction
CC with ADA also regulates lymphocyte-epithelial cell adhesion
CC (PubMed:11772392). In association with FAP is involved in the
CC pericellular proteolysis of the extracellular matrix (ECM), the
CC migration and invasion of endothelial cells into the ECM
CC (PubMed:16651416, PubMed:10593948). May be involved in the promotion of
CC lymphatic endothelial cells adhesion, migration and tube formation
CC (PubMed:18708048). When overexpressed, enhanced cell proliferation, a
CC process inhibited by GPC3 (PubMed:17549790). Acts also as a serine
CC exopeptidase with a dipeptidyl peptidase activity that regulates
CC various physiological processes by cleaving peptides in the
CC circulation, including many chemokines, mitogenic growth factors,
CC neuropeptides and peptide hormones such as brain natriuretic peptide 32
CC (PubMed:16254193, PubMed:10570924). Removes N-terminal dipeptides
CC sequentially from polypeptides having unsubstituted N-termini provided
CC that the penultimate residue is proline (PubMed:10593948).
CC {ECO:0000269|PubMed:10570924, ECO:0000269|PubMed:10593948,
CC ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221,
CC ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:14691230,
CC ECO:0000269|PubMed:16254193, ECO:0000269|PubMed:16651416,
CC ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790,
CC ECO:0000269|PubMed:18708048}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for human
CC coronavirus MERS-CoV-2. {ECO:0000269|PubMed:23835475}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10084, ECO:0000269|PubMed:10593948};
CC -!- ACTIVITY REGULATION: Inhibited by GPC3 and diprotin A.
CC {ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.
CC -!- SUBUNIT: Monomer. Homodimer (PubMed:12832764, PubMed:15448155,
CC PubMed:17287217, PubMed:12646248, PubMed:12483204, PubMed:12906826).
CC Heterodimer with Seprase (FAP) (PubMed:16651416). Requires
CC homodimerization for optimal dipeptidyl peptidase activity and T-cell
CC costimulation. Found in a membrane raft complex, at least composed of
CC BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Associates with
CC collagen (PubMed:8526932). Interacts with PTPRC; the interaction is
CC enhanced in an interleukin-12-dependent manner in activated lymphocytes
CC (PubMed:12676959). Interacts (via extracellular domain) with ADA; does
CC not inhibit its dipeptidyl peptidase activity (PubMed:15016824,
CC PubMed:10951221, PubMed:14691230, PubMed:7907293, PubMed:8101391).
CC Interacts with CAV1 (via the N-terminus); the interaction is direct
CC (PubMed:17287217). Interacts (via cytoplasmic tail) with CARD11 (via
CC PDZ domain); its homodimerization is necessary for interaction with
CC CARD11 (PubMed:17287217). Interacts with IGF2R; the interaction is
CC direct (PubMed:10900005). Interacts with GPC3 (PubMed:17549790).
CC Interacts with human coronavirus-EMC spike protein and acts as a
CC receptor for this virus (PubMed:23486063).
CC {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221,
CC ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248,
CC ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:12832764,
CC ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:14691230,
CC ECO:0000269|PubMed:15016824, ECO:0000269|PubMed:15448155,
CC ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217,
CC ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:23486063,
CC ECO:0000269|PubMed:7907293, ECO:0000269|PubMed:8101391,
CC ECO:0000269|PubMed:8526932}.
CC -!- SUBUNIT: (Microbial infection) Interacts with MERS coronavirus/MERS-CoV
CC spike protein. {ECO:0000269|PubMed:23835475}.
CC -!- INTERACTION:
CC P27487; P51671: CCL11; NbExp=2; IntAct=EBI-2871277, EBI-727357;
CC P27487; P02778: CXCL10; NbExp=2; IntAct=EBI-2871277, EBI-7815386;
CC P27487; O14625: CXCL11; NbExp=2; IntAct=EBI-2871277, EBI-2871971;
CC P27487; P19875: CXCL2; NbExp=2; IntAct=EBI-2871277, EBI-2114901;
CC P27487; Q07325: CXCL9; NbExp=2; IntAct=EBI-2871277, EBI-3911467;
CC P27487; P27487: DPP4; NbExp=12; IntAct=EBI-2871277, EBI-2871277;
CC P27487; P01275: GCG; NbExp=4; IntAct=EBI-2871277, EBI-7629173;
CC P27487; Q14416: GRM2; NbExp=2; IntAct=EBI-2871277, EBI-10232876;
CC P27487; P01282: VIP; NbExp=2; IntAct=EBI-2871277, EBI-751454;
CC P27487; P56658: ADA; Xeno; NbExp=5; IntAct=EBI-2871277, EBI-7475530;
CC P27487; A0A2R4KP93: S; Xeno; NbExp=2; IntAct=EBI-2871277, EBI-25589622;
CC P27487; K0BRG7: S; Xeno; NbExp=5; IntAct=EBI-2871277, EBI-16040613;
CC P27487; K9N5Q8: S; Xeno; NbExp=7; IntAct=EBI-2871277, EBI-25474996;
CC P27487; R9UQ53: S; Xeno; NbExp=3; IntAct=EBI-2871277, EBI-25645424;
CC -!- SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted
CC {ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:16254193}.
CC Note=Detected in the serum and the seminal fluid.
CC {ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:16254193}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10900005,
CC ECO:0000269|PubMed:11772392, ECO:0000305|PubMed:8101391}; Single-pass
CC type II membrane protein. Apical cell membrane
CC {ECO:0000269|PubMed:11773049}; Single-pass type II membrane protein.
CC Cell projection, invadopodium membrane {ECO:0000269|PubMed:16651416};
CC Single-pass type II membrane protein. Cell projection, lamellipodium
CC membrane {ECO:0000269|PubMed:16651416}; Single-pass type II membrane
CC protein. Cell junction {ECO:0000269|PubMed:11772392}. Membrane raft
CC {ECO:0000269|PubMed:17287217}. Note=Translocated to the apical membrane
CC through the concerted action of N- and O-Glycans and its association
CC with lipid microdomains containing cholesterol and sphingolipids
CC (PubMed:11773049). Redistributed to membrane rafts in T-cell in an
CC interleukin-12-dependent activation (PubMed:12676959). Its interaction
CC with CAV1 is necessary for its translocation to membrane rafts
CC (PubMed:17287217). Colocalized with PTPRC in membrane rafts
CC (PubMed:12676959). Colocalized with FAP in invadopodia and lamellipodia
CC of migratory activated endothelial cells in collagenous matrix.
CC Colocalized with FAP on endothelial cells of capillary-like
CC microvessels but not large vessels within invasive breast ductal
CC carcinoma (PubMed:16651416). Colocalized with ADA at the cell junction
CC in lymphocyte-epithelial cell adhesion (PubMed:11772392). Colocalized
CC with IGF2R in internalized cytoplasmic vesicles adjacent to the cell
CC surface (PubMed:10900005). {ECO:0000269|PubMed:10900005,
CC ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:11773049,
CC ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:16651416,
CC ECO:0000269|PubMed:17287217}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in lymphatic vessels but not
CC in blood vessels in the skin, small intestine, esophagus, ovary, breast
CC and prostate glands. Not detected in lymphatic vessels in the lung,
CC kidney, uterus, liver and stomach (at protein level). Expressed in the
CC poorly differentiated crypt cells of the small intestine as well as in
CC the mature villous cells. Expressed at very low levels in the colon.
CC {ECO:0000269|PubMed:1677636, ECO:0000269|PubMed:18708048}.
CC -!- INDUCTION: Up-regulated by IL12/interleukin-12 on activated T-cells.
CC IL12-activated cells expressed enhanced levels of DPP4 but not mRNAs.
CC Down-regulated by TNF. Up-regulated in migratory endothelial cells and
CC in the invasive endothelial cells in tumors. Induced by hypoxia
CC (PubMed:16670267). {ECO:0000269|PubMed:10880264,
CC ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:16651416,
CC ECO:0000269|PubMed:16670267, ECO:0000269|PubMed:9413751}.
CC -!- DOMAIN: The extracellular cysteine-rich region is necessary for
CC association with collagen, dimer formation and optimal dipeptidyl
CC peptidase activity.
CC -!- PTM: The soluble form (Dipeptidyl peptidase 4 soluble form also named
CC SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane
CC form also named MDPP) by proteolytic processing.
CC -!- PTM: N- and O-Glycosylated. {ECO:0000269|PubMed:10900005,
CC ECO:0000269|PubMed:11773049, ECO:0000269|PubMed:12483204,
CC ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:20684603}.
CC -!- PTM: Phosphorylated. Mannose 6-phosphate residues in the carbohydrate
CC moiety are necessary for interaction with IGF2R in activated T-cells.
CC Mannose 6-phosphorylation is induced during T-cell activation.
CC {ECO:0000269|PubMed:10900005}.
CC -!- MISCELLANEOUS: Level of plasma concentrations of the soluble form
CC (SDPP) can be managed as a colon carcinoma diagnostic and prognostic
CC marker.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Dipeptidyl peptidase-4 entry;
CC URL="https://en.wikipedia.org/wiki/Dipeptidyl_peptidase-4";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DPP4ID40360ch2q24.html";
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DR EMBL; X60708; CAA43118.1; -; mRNA.
DR EMBL; M80536; AAA52308.1; -; mRNA.
DR EMBL; M74777; AAA51943.1; -; mRNA.
DR EMBL; U13735; AAB60646.1; -; Genomic_DNA.
DR EMBL; U13710; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13711; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13712; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13713; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13714; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13715; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13716; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13717; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13718; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13719; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13720; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13721; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13722; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13723; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13724; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13725; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13726; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13727; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13728; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13729; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13730; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13731; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13732; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13733; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; U13734; AAB60646.1; JOINED; Genomic_DNA.
DR EMBL; AB451339; BAG70153.1; -; mRNA.
DR EMBL; AB451488; BAG70302.1; -; mRNA.
DR EMBL; AC008063; AAX93179.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11361.1; -; Genomic_DNA.
DR EMBL; BC013329; AAH13329.2; -; mRNA.
DR EMBL; BC065265; AAH65265.1; -; mRNA.
DR EMBL; S79876; AAB35614.1; -; Genomic_DNA.
DR CCDS; CCDS2216.1; -.
DR PIR; S24313; CDHU26.
DR RefSeq; NP_001926.2; NM_001935.3.
DR PDB; 1J2E; X-ray; 2.60 A; A/B=33-766.
DR PDB; 1N1M; X-ray; 2.50 A; A/B=39-766.
DR PDB; 1NU6; X-ray; 2.10 A; A/B=39-766.
DR PDB; 1NU8; X-ray; 2.50 A; A/B=39-766.
DR PDB; 1PFQ; X-ray; 1.90 A; A/B=36-766.
DR PDB; 1R9M; X-ray; 2.10 A; A/B/C/D=39-766.
DR PDB; 1R9N; X-ray; 2.30 A; A/B/C/D=39-766.
DR PDB; 1RWQ; X-ray; 2.20 A; A/B=39-766.
DR PDB; 1TK3; X-ray; 2.00 A; A/B=39-766.
DR PDB; 1TKR; X-ray; 2.70 A; A/B=39-766.
DR PDB; 1U8E; X-ray; 2.20 A; A/B=39-766.
DR PDB; 1W1I; X-ray; 3.03 A; A/B/C/D=39-766.
DR PDB; 1WCY; X-ray; 2.20 A; A/B=33-766.
DR PDB; 1X70; X-ray; 2.10 A; A/B=39-766.
DR PDB; 2AJL; X-ray; 2.50 A; I/J=39-766.
DR PDB; 2BGN; X-ray; 3.15 A; A/B/C/D=39-766.
DR PDB; 2BGR; X-ray; 2.00 A; A/B=29-766.
DR PDB; 2BUB; X-ray; 2.66 A; A/B=39-766.
DR PDB; 2FJP; X-ray; 2.40 A; A/B=39-766.
DR PDB; 2G5P; X-ray; 2.40 A; A/B=39-764.
DR PDB; 2G5T; X-ray; 2.30 A; A/B=39-764.
DR PDB; 2G63; X-ray; 2.00 A; A/B/C/D=39-764.
DR PDB; 2HHA; X-ray; 2.35 A; A/B=40-766.
DR PDB; 2I03; X-ray; 2.40 A; A/B/C/D=39-764.
DR PDB; 2I78; X-ray; 2.50 A; A/B/C/D=39-764.
DR PDB; 2IIT; X-ray; 2.35 A; A/B=39-766.
DR PDB; 2IIV; X-ray; 2.15 A; A/B=39-766.
DR PDB; 2JID; X-ray; 2.80 A; A/B=31-766.
DR PDB; 2OAG; X-ray; 2.30 A; A/B/C/D=39-764.
DR PDB; 2OGZ; X-ray; 2.10 A; A/B=39-766.
DR PDB; 2OLE; X-ray; 2.40 A; A/B=39-766.
DR PDB; 2ONC; X-ray; 2.55 A; A/B/C/D=41-766.
DR PDB; 2OPH; X-ray; 2.40 A; A/B=39-766.
DR PDB; 2OQI; X-ray; 2.80 A; A/B/C/D=39-766.
DR PDB; 2OQV; X-ray; 2.80 A; A/B=39-764.
DR PDB; 2P8S; X-ray; 2.20 A; A/B=40-766.
DR PDB; 2QJR; X-ray; 2.20 A; A/B=31-766.
DR PDB; 2QKY; X-ray; 3.10 A; A/B/C/D=40-766.
DR PDB; 2QOE; X-ray; 2.30 A; A/B=39-766.
DR PDB; 2QT9; X-ray; 2.10 A; A/B=1-766.
DR PDB; 2QTB; X-ray; 2.25 A; A/B=1-766.
DR PDB; 2RGU; X-ray; 2.60 A; A/B=39-766.
DR PDB; 2RIP; X-ray; 2.90 A; A=38-766.
DR PDB; 3BJM; X-ray; 2.35 A; A/B=39-766.
DR PDB; 3C43; X-ray; 2.30 A; A/B=39-766.
DR PDB; 3C45; X-ray; 2.05 A; A/B=39-766.
DR PDB; 3CCB; X-ray; 2.49 A; A/B/C/D=39-766.
DR PDB; 3CCC; X-ray; 2.71 A; A/B/C/D=39-766.
DR PDB; 3D4L; X-ray; 2.00 A; A/B=39-766.
DR PDB; 3EIO; X-ray; 2.00 A; A/B=39-766.
DR PDB; 3F8S; X-ray; 2.43 A; A/B=31-766.
DR PDB; 3G0B; X-ray; 2.25 A; A/B/C/D=39-766.
DR PDB; 3G0C; X-ray; 2.69 A; A/B/C/D=39-766.
DR PDB; 3G0D; X-ray; 2.39 A; A/B/C/D=39-766.
DR PDB; 3G0G; X-ray; 2.45 A; A/B/C/D=39-766.
DR PDB; 3H0C; X-ray; 2.66 A; A/B=39-766.
DR PDB; 3HAB; X-ray; 2.10 A; A/B=39-766.
DR PDB; 3HAC; X-ray; 2.00 A; A/B=39-766.
DR PDB; 3KWF; X-ray; 2.40 A; A/B=39-766.
DR PDB; 3KWJ; X-ray; 2.80 A; A/B=39-766.
DR PDB; 3NOX; X-ray; 2.34 A; A/B=39-766.
DR PDB; 3O95; X-ray; 2.85 A; A/B/C/D=39-766.
DR PDB; 3O9V; X-ray; 2.75 A; A/B/C/D=39-766.
DR PDB; 3OC0; X-ray; 2.70 A; A/B=39-766.
DR PDB; 3OPM; X-ray; 2.72 A; A/B/C/D=39-766.
DR PDB; 3Q0T; X-ray; 2.40 A; A/B=39-766.
DR PDB; 3Q8W; X-ray; 3.64 A; A/B=39-764.
DR PDB; 3QBJ; X-ray; 2.21 A; A/B=31-766.
DR PDB; 3SWW; X-ray; 2.00 A; A/B=39-766.
DR PDB; 3SX4; X-ray; 2.60 A; A/B=39-766.
DR PDB; 3VJK; X-ray; 2.49 A; A/B=33-766.
DR PDB; 3VJL; X-ray; 2.39 A; A/B=33-766.
DR PDB; 3VJM; X-ray; 2.10 A; A/B=33-766.
DR PDB; 3W2T; X-ray; 2.36 A; A/B=33-766.
DR PDB; 3WQH; X-ray; 2.85 A; A/B=39-766.
DR PDB; 4A5S; X-ray; 1.62 A; A/B=39-766.
DR PDB; 4DSA; X-ray; 3.25 A; A/B=39-766.
DR PDB; 4DSZ; X-ray; 3.20 A; A/B=39-766.
DR PDB; 4DTC; X-ray; 3.00 A; A/B=39-766.
DR PDB; 4G1F; X-ray; 2.90 A; A/B/C/D=39-766.
DR PDB; 4J3J; X-ray; 3.20 A; A/B=39-766.
DR PDB; 4JH0; X-ray; 2.35 A; A/B=39-766.
DR PDB; 4KR0; X-ray; 2.70 A; A=39-766.
DR PDB; 4L72; X-ray; 3.00 A; A=39-766.
DR PDB; 4LKO; X-ray; 2.43 A; A/B=39-766.
DR PDB; 4N8D; X-ray; 1.65 A; A/B=39-766.
DR PDB; 4N8E; X-ray; 2.30 A; A/B=39-766.
DR PDB; 4PNZ; X-ray; 1.90 A; A/B=39-766.
DR PDB; 4PV7; X-ray; 3.24 A; A/B=39-766.
DR PDB; 4QZV; X-ray; 2.59 A; A/C=39-766.
DR PDB; 5I7U; X-ray; 1.95 A; A/B=39-766.
DR PDB; 5ISM; X-ray; 2.00 A; A/B=39-766.
DR PDB; 5J3J; X-ray; 2.75 A; A/B=40-766.
DR PDB; 5KBY; X-ray; 2.24 A; A/B/C/D=39-766.
DR PDB; 5T4B; X-ray; 1.76 A; A/B=40-766.
DR PDB; 5T4E; X-ray; 1.77 A; A/B=40-766.
DR PDB; 5T4F; X-ray; 1.90 A; A/B=40-766.
DR PDB; 5T4H; X-ray; 2.61 A; A/B=40-766.
DR PDB; 5Y7H; X-ray; 3.00 A; A/B=39-766.
DR PDB; 5Y7J; X-ray; 2.52 A; A/B/C/D=39-766.
DR PDB; 5Y7K; X-ray; 2.51 A; A/B/C/D=39-766.
DR PDB; 5ZID; X-ray; 3.00 A; A/B=40-766.
DR PDB; 6B1E; X-ray; 1.77 A; A/B=39-766.
DR PDB; 6B1O; X-ray; 1.91 A; A/B=39-766.
DR PDBsum; 1J2E; -.
DR PDBsum; 1N1M; -.
DR PDBsum; 1NU6; -.
DR PDBsum; 1NU8; -.
DR PDBsum; 1PFQ; -.
DR PDBsum; 1R9M; -.
DR PDBsum; 1R9N; -.
DR PDBsum; 1RWQ; -.
DR PDBsum; 1TK3; -.
DR PDBsum; 1TKR; -.
DR PDBsum; 1U8E; -.
DR PDBsum; 1W1I; -.
DR PDBsum; 1WCY; -.
DR PDBsum; 1X70; -.
DR PDBsum; 2AJL; -.
DR PDBsum; 2BGN; -.
DR PDBsum; 2BGR; -.
DR PDBsum; 2BUB; -.
DR PDBsum; 2FJP; -.
DR PDBsum; 2G5P; -.
DR PDBsum; 2G5T; -.
DR PDBsum; 2G63; -.
DR PDBsum; 2HHA; -.
DR PDBsum; 2I03; -.
DR PDBsum; 2I78; -.
DR PDBsum; 2IIT; -.
DR PDBsum; 2IIV; -.
DR PDBsum; 2JID; -.
DR PDBsum; 2OAG; -.
DR PDBsum; 2OGZ; -.
DR PDBsum; 2OLE; -.
DR PDBsum; 2ONC; -.
DR PDBsum; 2OPH; -.
DR PDBsum; 2OQI; -.
DR PDBsum; 2OQV; -.
DR PDBsum; 2P8S; -.
DR PDBsum; 2QJR; -.
DR PDBsum; 2QKY; -.
DR PDBsum; 2QOE; -.
DR PDBsum; 2QT9; -.
DR PDBsum; 2QTB; -.
DR PDBsum; 2RGU; -.
DR PDBsum; 2RIP; -.
DR PDBsum; 3BJM; -.
DR PDBsum; 3C43; -.
DR PDBsum; 3C45; -.
DR PDBsum; 3CCB; -.
DR PDBsum; 3CCC; -.
DR PDBsum; 3D4L; -.
DR PDBsum; 3EIO; -.
DR PDBsum; 3F8S; -.
DR PDBsum; 3G0B; -.
DR PDBsum; 3G0C; -.
DR PDBsum; 3G0D; -.
DR PDBsum; 3G0G; -.
DR PDBsum; 3H0C; -.
DR PDBsum; 3HAB; -.
DR PDBsum; 3HAC; -.
DR PDBsum; 3KWF; -.
DR PDBsum; 3KWJ; -.
DR PDBsum; 3NOX; -.
DR PDBsum; 3O95; -.
DR PDBsum; 3O9V; -.
DR PDBsum; 3OC0; -.
DR PDBsum; 3OPM; -.
DR PDBsum; 3Q0T; -.
DR PDBsum; 3Q8W; -.
DR PDBsum; 3QBJ; -.
DR PDBsum; 3SWW; -.
DR PDBsum; 3SX4; -.
DR PDBsum; 3VJK; -.
DR PDBsum; 3VJL; -.
DR PDBsum; 3VJM; -.
DR PDBsum; 3W2T; -.
DR PDBsum; 3WQH; -.
DR PDBsum; 4A5S; -.
DR PDBsum; 4DSA; -.
DR PDBsum; 4DSZ; -.
DR PDBsum; 4DTC; -.
DR PDBsum; 4G1F; -.
DR PDBsum; 4J3J; -.
DR PDBsum; 4JH0; -.
DR PDBsum; 4KR0; -.
DR PDBsum; 4L72; -.
DR PDBsum; 4LKO; -.
DR PDBsum; 4N8D; -.
DR PDBsum; 4N8E; -.
DR PDBsum; 4PNZ; -.
DR PDBsum; 4PV7; -.
DR PDBsum; 4QZV; -.
DR PDBsum; 5I7U; -.
DR PDBsum; 5ISM; -.
DR PDBsum; 5J3J; -.
DR PDBsum; 5KBY; -.
DR PDBsum; 5T4B; -.
DR PDBsum; 5T4E; -.
DR PDBsum; 5T4F; -.
DR PDBsum; 5T4H; -.
DR PDBsum; 5Y7H; -.
DR PDBsum; 5Y7J; -.
DR PDBsum; 5Y7K; -.
DR PDBsum; 5ZID; -.
DR PDBsum; 6B1E; -.
DR PDBsum; 6B1O; -.
DR AlphaFoldDB; P27487; -.
DR SMR; P27487; -.
DR BioGRID; 108137; 439.
DR ComplexPortal; CPX-5768; MERS-CoV Spike - human DPP4 receptor complex.
DR ComplexPortal; CPX-5769; MERS-CoV Spike - human DPP4 receptor complex.
DR CORUM; P27487; -.
DR DIP; DIP-351N; -.
DR IntAct; P27487; 29.
DR MINT; P27487; -.
DR STRING; 9606.ENSP00000353731; -.
DR BindingDB; P27487; -.
DR ChEMBL; CHEMBL284; -.
DR DrugBank; DB07356; (1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-ETHYNYLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINE.
DR DrugBank; DB06880; (1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-PROP-1-YN-1-YLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINE.
DR DrugBank; DB07072; (1S,2R,5S)-5-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-2-(2,4,5-TRIFLUOROPHENYL)CYCLOHEXANAMINE.
DR DrugBank; DB07465; (1S,3S,5S)-2-{(2S)-2-amino-2-[(1R,3S,5R,7S)-3-hydroxytricyclo[3.3.1.1~3,7~]dec-1-yl]acetyl}-2-azabicyclo[3.1.0]hexane-3-carbonitrile.
DR DrugBank; DB08051; (2R)-4-(2-BENZOYL-1,2-DIAZEPAN-1-YL)-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINE.
DR DrugBank; DB07081; (2R)-4-[(8R)-8-METHYL-2-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[1,5-A]PYRAZIN-7(8H)-YL]-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINE.
DR DrugBank; DB07482; (2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE.
DR DrugBank; DB07193; (2R,3R)-7-(methylsulfonyl)-3-(2,4,5-trifluorophenyl)-1,2,3,4-tetrahydropyrido[1,2-a]benzimidazol-2-amine.
DR DrugBank; DB03253; (2s)-Pyrrolidin-2-Ylmethylamine.
DR DrugBank; DB07092; (2S,3S)-3-AMINO-4-(3,3-DIFLUOROPYRROLIDIN-1-YL)-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-6-YLCYCLOHEXYL)BUTANAMIDE.
DR DrugBank; DB07135; (2S,3S)-3-AMINO-4-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-N,N-DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-5-YLCYCLOHEXYL)BUTANAMIDE.
DR DrugBank; DB06994; (2S,3S)-3-{3-[2-chloro-4-(methylsulfonyl)phenyl]-1,2,4-oxadiazol-5-yl}-1-cyclopentylidene-4-cyclopropyl-1-fluorobutan-2-amine.
DR DrugBank; DB07067; (2S,3S)-3-{3-[4-(METHYLSULFONYL)PHENYL]-1,2,4-OXADIAZOL-5-YL}-1-OXO-1-PYRROLIDIN-1-YLBUTAN-2-AMINE.
DR DrugBank; DB06993; (2S,3S)-4-cyclopropyl-3-{(3R,5R)-3-[2-fluoro-4-(methylsulfonyl)phenyl]-1,2,4-oxadiazolidin-5-yl}-1-[(3S)-3-fluoropyrrolidin-1-yl]-1-oxobutan-2-amine.
DR DrugBank; DB07154; (3R)-4-[(3R)-3-AMINO-4-(2,4,5-TRIFLUOROPHENYL)BUTANOYL]-3-METHYL-1,4-DIAZEPAN-2-ONE.
DR DrugBank; DB08164; (3R,4R)-1-{6-[3-(METHYLSULFONYL)PHENYL]PYRIMIDIN-4-YL}-4-(2,4,5-TRIFLUOROPHENYL)PIPERIDIN-3-AMINE.
DR DrugBank; DB07015; (3R,4R)-4-(pyrrolidin-1-ylcarbonyl)-1-(quinoxalin-2-ylcarbonyl)pyrrolidin-3-amine.
DR DrugBank; DB07851; (3R,4S)-1-(3,4-DIMETHOXYPHENYL)-3-(3-METHYLPHENYL)PIPERIDIN-4-AMINE.
DR DrugBank; DB08445; (3R,4S)-1-[6-(6-METHOXYPYRIDIN-3-YL)PYRIMIDIN-4-YL]-4-(2,4,5-TRIFLUOROPHENYL)PYRROLIDIN-3-AMINE.
DR DrugBank; DB07666; (3R,4S)-1-{6-[3-(METHYLSULFONYL)PHENYL]PYRIMIDIN-4-YL}-4-(2,4,5-TRIFLUOROPHENYL)PYRROLIDIN-3-AMINE.
DR DrugBank; DB07830; (4R,5R)-5-AMINO-1-[2-(1,3-BENZODIOXOL-5-YL)ETHYL]-4-(2,4,5-TRIFLUOROPHENYL)PIPERIDIN-2-ONE.
DR DrugBank; DB07021; (7R,8R)-8-(2,4,5-trifluorophenyl)-6,7,8,9-tetrahydroimidazo[1,2-a:4,5-c']dipyridin-7-amine.
DR DrugBank; DB04578; (S)-2-[(R)-3-amino-4-(2-fluorophenyl)butyryl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide.
DR DrugBank; DB04577; 1-(1-phenylcyclopentyl)methylamine.
DR DrugBank; DB08024; 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE.
DR DrugBank; DB07412; 1-biphenyl-2-ylmethanamine.
DR DrugBank; DB08588; 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-3(4H)-YL}METHYL)BENZONITRILE.
DR DrugBank; DB08743; 2-({8-[(3R)-3-AMINOPIPERIDIN-1-YL]-1,3-DIMETHYL-2,6-DIOXO-1,2,3,6-TETRAHYDRO-7H-PURIN-7-YL}METHYL)BENZONITRILE.
DR DrugBank; DB01884; 2-Amino-3-Methyl-1-Pyrrolidin-1-Yl-Butan-1-One.
DR DrugBank; DB07181; 4'-[(1R)-1-amino-2-(2,5-difluorophenyl)ethyl]biphenyl-3-carboxamide.
DR DrugBank; DB07271; 4-[(3R)-3-Amino-4-(2,4,5-trifluorophenyl)butanoyl]-3-(2,2,2-trifluoroethyl)-1,4-diazepan-2-one.
DR DrugBank; DB08672; 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE.
DR DrugBank; DB03660; 4-Iodo-L-phenylalanine.
DR DrugBank; DB02004; 5-(Aminomethyl)-6-(2,4-Dichlorophenyl)-2-(3,5-Dimethoxyphenyl)Pyrimidin-4-Amine.
DR DrugBank; DB08504; 6-(4-{(1S,2S)-2-AMINO-1-[(DIMETHYLAMINO)CARBONYL]-3-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-3-OXOPROPYL}PHENYL)-1H-[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-4-IUM.
DR DrugBank; DB07239; 7-(aminomethyl)-6-(2-chlorophenyl)-1-methyl-1H-benzimidazole-5-carbonitrile.
DR DrugBank; DB08530; 7-BENZYL-1,3-DIMETHYL-8-PIPERAZIN-1-YL-3,7-DIHYDRO-PURINE-2,6-DIONE.
DR DrugBank; DB08044; ABT-341.
DR DrugBank; DB06203; Alogliptin.
DR DrugBank; DB06011; AMG-222.
DR DrugBank; DB01076; Atorvastatin.
DR DrugBank; DB06127; Bisegliptin.
DR DrugBank; DB04491; Diisopropylphosphono Group.
DR DrugBank; DB11723; Dutogliptin.
DR DrugBank; DB01276; Exenatide.
DR DrugBank; DB08382; Gosogliptin.
DR DrugBank; DB08882; Linagliptin.
DR DrugBank; DB06655; Liraglutide.
DR DrugBank; DB07328; METHYL 4-{[({[(2R,5S)-5-{[(2S)-2-(AMINOMETHYL)PYRROLIDIN-1-YL]CARBONYL}PYRROLIDIN-2-YL]METHYL}AMINO)CARBONYL]AMINO}BENZOATE.
DR DrugBank; DB06939; N-(TRANS-4-{(1S,2S)-2-AMINO-3-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-1-METHYL-3-OXOPROPYL}CYCLOHEXYL)-N-METHYLACETAMIDE.
DR DrugBank; DB07779; N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE.
DR DrugBank; DB08429; N-({(2S)-1-[(3R)-3-amino-4-(3-chlorophenyl)butanoyl]pyrrolidin-2-yl}methyl)-3-(methylsulfonyl)benzamide.
DR DrugBank; DB05001; PSN9301.
DR DrugBank; DB06335; Saxagliptin.
DR DrugBank; DB13928; Semaglutide.
DR DrugBank; DB01261; Sitagliptin.
DR DrugBank; DB04876; Vildagliptin.
DR DrugCentral; P27487; -.
DR GuidetoPHARMACOLOGY; 1612; -.
DR ESTHER; human-DPP4; DPP4N_Peptidase_S9.
DR MEROPS; S09.003; -.
DR MoonProt; P27487; -.
DR TCDB; 8.A.51.1.5; the dipeptidyl-aminopeptidase-like protein 6 beta subunit of kv4 channels (dpp6) family.
DR GlyConnect; 1177; 20 N-Linked glycans (4 sites).
DR GlyGen; P27487; 12 sites, 21 N-linked glycans (4 sites).
DR iPTMnet; P27487; -.
DR PhosphoSitePlus; P27487; -.
DR BioMuta; DPP4; -.
DR DMDM; 1352311; -.
DR CPTAC; CPTAC-1292; -.
DR jPOST; P27487; -.
DR MassIVE; P27487; -.
DR MaxQB; P27487; -.
DR PaxDb; P27487; -.
DR PeptideAtlas; P27487; -.
DR PRIDE; P27487; -.
DR ProteomicsDB; 54396; -.
DR ABCD; P27487; 15 sequenced antibodies.
DR Antibodypedia; 19093; 1761 antibodies from 45 providers.
DR DNASU; 1803; -.
DR Ensembl; ENST00000360534.8; ENSP00000353731.3; ENSG00000197635.11.
DR GeneID; 1803; -.
DR KEGG; hsa:1803; -.
DR MANE-Select; ENST00000360534.8; ENSP00000353731.3; NM_001935.4; NP_001926.2.
DR UCSC; uc002ubz.4; human.
DR CTD; 1803; -.
DR DisGeNET; 1803; -.
DR GeneCards; DPP4; -.
DR HGNC; HGNC:3009; DPP4.
DR HPA; ENSG00000197635; Tissue enhanced (intestine, parathyroid gland, placenta, prostate).
DR MIM; 102720; gene.
DR neXtProt; NX_P27487; -.
DR OpenTargets; ENSG00000197635; -.
DR PharmGKB; PA27467; -.
DR VEuPathDB; HostDB:ENSG00000197635; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000161291; -.
DR HOGENOM; CLU_006105_4_3_1; -.
DR InParanoid; P27487; -.
DR OMA; AYVWKND; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; P27487; -.
DR TreeFam; TF313309; -.
DR BRENDA; 3.4.14.5; 2681.
DR PathwayCommons; P27487; -.
DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR SABIO-RK; P27487; -.
DR SignaLink; P27487; -.
DR SIGNOR; P27487; -.
DR BioGRID-ORCS; 1803; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; DPP4; human.
DR EvolutionaryTrace; P27487; -.
DR GeneWiki; Dipeptidyl_peptidase-4; -.
DR GenomeRNAi; 1803; -.
DR Pharos; P27487; Tclin.
DR PRO; PR:P27487; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P27487; protein.
DR Bgee; ENSG00000197635; Expressed in calcaneal tendon and 156 other tissues.
DR ExpressionAtlas; P27487; baseline and differential.
DR Genevisible; P27487; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045499; F:chemorepellent activity; IDA:CACAO.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IDA:CACAO.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0043542; P:endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0120116; P:glucagon processing; TAS:Reactome.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0061025; P:membrane fusion; IC:ComplexPortal.
DR GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IDA:UniProtKB.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; IMP:CACAO.
DR GO; GO:0016486; P:peptide hormone processing; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:CAFA.
DR GO; GO:0036343; P:psychomotor behavior; IEA:Ensembl.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IC:ComplexPortal.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IC:ComplexPortal.
DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IC:ComplexPortal.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Hydrolase; Membrane; Protease; Receptor;
KW Reference proteome; Secreted; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..766
FT /note="Dipeptidyl peptidase 4 membrane form"
FT /id="PRO_0000027213"
FT CHAIN 39..766
FT /note="Dipeptidyl peptidase 4 soluble form"
FT /id="PRO_0000027214"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..766
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 630
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 708
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 740
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
FT ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603,
FT ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
FT ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
FT ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12483204,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 328..339
FT /evidence="ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT DISULFID 385..394
FT /evidence="ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT DISULFID 444..447
FT /evidence="ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT DISULFID 454..472
FT /evidence="ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT DISULFID 649..762
FT /evidence="ECO:0000269|PubMed:23835475,
FT ECO:0007744|PDB:4L72"
FT VARIANT 266
FT /note="V -> I (in dbSNP:rs56179129)"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084545"
FT MUTAGEN 85
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 92
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 150
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 205
FT /note="E->K: Inhibits dipeptidyl peptidase activity."
FT /evidence="ECO:0000269|PubMed:10570924"
FT MUTAGEN 206
FT /note="E->L: Inhibits dipeptidyl peptidase activity."
FT /evidence="ECO:0000269|PubMed:10570924"
FT MUTAGEN 219
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 229
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 281
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 321
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 520
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 685
FT /note="N->A: Does not inhibit dipeptidyl peptidase
FT activity, interaction with ADA and homodimer formation."
FT /evidence="ECO:0000269|PubMed:14691230"
FT MUTAGEN 750
FT /note="H->A: Inhibits weakly homodimerization and
FT dipeptidyl peptidase activity."
FT /evidence="ECO:0000269|PubMed:15448155,
FT ECO:0000269|PubMed:17287217"
FT MUTAGEN 750
FT /note="H->E: Inhibits strongly homodimerization, dipeptidyl
FT peptidase activity, interaction with CARD11 and T-cell
FT costimulation activity."
FT /evidence="ECO:0000269|PubMed:15448155,
FT ECO:0000269|PubMed:17287217"
FT CONFLICT 6
FT /note="K -> R (in Ref. 2; AAA52308)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="V -> I (in Ref. 1; CAA43118)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="S -> I (in Ref. 1; CAA43118)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="T -> I (in Ref. 2; AAA52308)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="D -> E (in Ref. 2; AAA52308)"
FT /evidence="ECO:0000305"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3VJM"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 92..97
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5T4B"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 111..122
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3F8S"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4N8D"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1NU8"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2G5P"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3SWW"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:1PFQ"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 465..472
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 485..488
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:3G0B"
FT STRAND 511..519
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 522..530
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:1PFQ"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 563..569
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 592..594
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:5Y7J"
FT HELIX 601..614
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:3VJK"
FT STRAND 619..629
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 631..640
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 648..654
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 664..671
FT /evidence="ECO:0007829|PDB:4A5S"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 680..685
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 689..697
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 698..705
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 714..725
FT /evidence="ECO:0007829|PDB:4A5S"
FT STRAND 731..735
FT /evidence="ECO:0007829|PDB:4A5S"
FT HELIX 745..762
FT /evidence="ECO:0007829|PDB:4A5S"
SQ SEQUENCE 766 AA; 88279 MW; 5FB4A2C6662D6117 CRC64;
MKTPWKVLLG LLGAAALVTI ITVPVVLLNK GTDDATADSR KTYTLTDYLK NTYRLKLYSL
RWISDHEYLY KQENNILVFN AEYGNSSVFL ENSTFDEFGH SINDYSISPD GQFILLEYNY
VKQWRHSYTA SYDIYDLNKR QLITEERIPN NTQWVTWSPV GHKLAYVWNN DIYVKIEPNL
PSYRITWTGK EDIIYNGITD WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF
YSDESLQYPK TVRVPYPKAG AVNPTVKFFV VNTDSLSSVT NATSIQITAP ASMLIGDHYL
CDVTWATQER ISLQWLRRIQ NYSVMDICDY DESSGRWNCL VARQHIEMST TGWVGRFRPS
EPHFTLDGNS FYKIISNEEG YRHICYFQID KKDCTFITKG TWEVIGIEAL TSDYLYYISN
EYKGMPGGRN LYKIQLSDYT KVTCLSCELN PERCQYYSVS FSKEAKYYQL RCSGPGLPLY
TLHSSVNDKG LRVLEDNSAL DKMLQNVQMP SKKLDFIILN ETKFWYQMIL PPHFDKSKKY
PLLLDVYAGP CSQKADTVFR LNWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
FEVEDQIEAA RQFSKMGFVD NKRIAIWGWS YGGYVTSMVL GSGSGVFKCG IAVAPVSRWE
YYDSVYTERY MGLPTPEDNL DHYRNSTVMS RAENFKQVEY LLIHGTADDN VHFQQSAQIS
KALVDVGVDF QAMWYTDEDH GIASSTAHQH IYTHMSHFIK QCFSLP
