ID DPP9_HUMAN Reviewed; 863 AA. AC Q86TI2; O75273; O75868; Q1ZZB8; Q6AI37; Q6UAL0; Q6ZMT2; Q6ZNJ5; Q8N2J7; AC Q8N3F5; Q8WXD8; Q96NT8; Q9BVR3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 3. DT 27-MAR-2024, entry version 174. DE RecName: Full=Dipeptidyl peptidase 9 {ECO:0000303|PubMed:12459266}; DE Short=DP9; DE EC=3.4.14.5 {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:33731929}; 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 {ECO:0000303|PubMed:12459266, ECO:0000312|HGNC:HGNC:18648}; GN Synonyms=DPRP2; 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] (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 of RT dipeptidyl peptidase IV."; RL Gene 299:185-193(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND RP 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 of RT 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], FUNCTION, 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 characterization RT compared with dipeptidyl peptidase IV."; RL Biochem. J. 396:391-399(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., 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., 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 [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 project: RT 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19667070; DOI=10.1074/jbc.m109.041871; RA Geiss-Friedlander R., Parmentier N., Moeller U., Urlaub H., RA Van den Eynde B.J., Melchior F.; RT "The cytoplasmic peptidase DPP9 is rate-limiting for degradation of RT proline-containing peptides."; RL J. Biol. Chem. 284:27211-27219(2009). RN [12] 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP SUBCELLULAR LOCATION (ISOFORM 2), AND NUCLEAR LOCALIZATION SIGNAL (ISOFORM RP 2). RX PubMed=24562348; DOI=10.1007/s00018-014-1591-6; RA Justa-Schuch D., Moller U., Geiss-Friedlander R.; RT "The amino terminus extension in the long dipeptidyl peptidase 9 isoform RT contains a nuclear localization signal targeting the active peptidase to RT the nucleus."; RL Cell. Mol. Life Sci. 71:3611-3626(2014). RN [15] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=27820798; DOI=10.1038/nchembio.2229; RA Okondo M.C., Johnson D.C., Sridharan R., Go E.B., Chui A.J., Wang M.S., RA Poplawski S.E., Wu W., Liu Y., Lai J.H., Sanford D.G., Arciprete M.O., RA Golub T.R., Bachovchin W.W., Bachovchin D.A.; RT "DPP8 and DPP9 inhibition induces pro-caspase-1-dependent monocyte and RT macrophage pyroptosis."; RL Nat. Chem. Biol. 13:46-53(2017). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF SER-730. RX PubMed=30291141; DOI=10.1074/jbc.ra118.004350; RA Zhong F.L., Robinson K., Teo D.E.T., Tan K.Y., Lim C., Harapas C.R., RA Yu C.H., Xie W.H., Sobota R.M., Au V.B., Hopkins R., D'Osualdo A., RA Reed J.C., Connolly J.E., Masters S.L., Reversade B.; RT "Human DPP9 represses NLRP1 inflammasome and protects against RT autoinflammatory diseases via both peptidase activity and FIIND domain RT binding."; RL J. Biol. Chem. 293:18864-18878(2018). RN [17] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=29967349; DOI=10.1038/s41591-018-0082-y; RA Johnson D.C., Taabazuing C.Y., Okondo M.C., Chui A.J., Rao S.D., RA Brown F.C., Reed C., Peguero E., de Stanchina E., Kentsis A., RA Bachovchin D.A.; RT "DPP8/DPP9 inhibitor-induced pyroptosis for treatment of acute myeloid RT leukemia."; RL Nat. Med. 24:1151-1156(2018). RN [18] RP FUNCTION. RX PubMed=31525884; DOI=10.1021/acschembio.9b00462; RA Griswold A.R., Ball D.P., Bhattacharjee A., Chui A.J., Rao S.D., RA Taabazuing C.Y., Bachovchin D.A.; RT "DPP9's enzymatic activity and not its binding to CARD8 inhibits RT inflammasome activation."; RL ACS Chem. Biol. 14:2424-2429(2019). RN [19] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=32796818; DOI=10.1038/s41419-020-02865-4; RA Johnson D.C., Okondo M.C., Orth E.L., Rao S.D., Huang H.C., Ball D.P., RA Bachovchin D.A.; RT "DPP8/9 inhibitors activate the CARD8 inflammasome in resting RT lymphocytes."; RL Cell Death Dis. 11:628-628(2020). RN [20] RP FUNCTION, INTERACTION WITH NLRP1 AND CARD8, CATALYTIC ACTIVITY, AND RP MUTAGENESIS OF LEU-102 AND SER-730. RX PubMed=33731929; DOI=10.1038/s41586-021-03320-w; RA Huang M., Zhang X., Toh G.A., Gong Q., Wang J., Han Z., Wu B., Zhong F., RA Chai J.; RT "Structural and biochemical mechanisms of NLRP1 inhibition by DPP9."; RL Nature 592:773-777(2021). RN [21] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=36357533; DOI=10.1038/s41589-022-01182-5; RA Clark K.M., Kim J.G., Wang Q., Gao H., Presti R.M., Shan L.; RT "Chemical inhibition of DPP9 sensitizes the CARD8 inflammasome in HIV-1- RT infected cells."; RL Nat. Chem. Biol. 0:0-0(2022). RN [22] RP INVOLVEMENT IN HATIS, VARIANTS HATIS 82-ARG--LEU-863 DEL; SER-138; RP 185-SER--LEU-863 DEL AND 822-GLN--LEU-863 DEL, CHARACTERIZATION OF VARIANT RP HATIS SER-138 AND 822-GLN--LEU-863 DEL, AND FUNCTION. RX PubMed=36112693; DOI=10.1126/sciimmunol.abi4611; RA Harapas C.R., Robinson K.S., Lay K., Wong J., Moreno Traspas R., RA Nabavizadeh N., Rass-Rothschild A., Boisson B., Drutman S.B., RA Laohamonthonkul P., Bonner D., Xiong J.R., Gorrell M.D., Davidson S., RA Yu C.H., Fleming M.D., Gudera J., Stein J., Ben-Harosh M., Groopman E., RA Shimamura A., Tamary H., Kayserili H., Hatipoglu N., Casanova J.L., RA Bernstein J.A., Zhong F.L., Masters S.L., Reversade B.; RT "DPP9 deficiency: An inflammasomopathy that can be rescued by lowering RT NLRP1/IL-1 signaling."; RL Sci. Immunol. 7:eabi4611-eabi4611(2022). RN [23] {ECO:0007744|PDB:6EOQ, ECO:0007744|PDB:6EOR} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND RP SUBUNIT. RX PubMed=29382749; DOI=10.1073/pnas.1717565115; RA Ross B., Krapp S., Augustin M., Kierfersauer R., Arciniega M., RA Geiss-Friedlander R., Huber R.; RT "Structures and mechanism of dipeptidyl peptidases 8 and 9, important RT players in cellular homeostasis and cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E1437-E1445(2018). RN [24] {ECO:0007744|PDB:7JKQ, ECO:0007744|PDB:7JN7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH CARD8 AND RP VAL-BOROPRO, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CARD8, AND RP MUTAGENESIS OF 96-ARG-LYS-97; 100-LEU-LEU-101 AND 102-LEU-LEU-103. RX PubMed=34019797; DOI=10.1016/j.immuni.2021.04.024; RA Sharif H., Hollingsworth L.R., Griswold A.R., Hsiao J.C., Wang Q., RA Bachovchin D.A., Wu H.; RT "Dipeptidyl peptidase 9 sets a threshold for CARD8 inflammasome formation RT by sequestering its active C-terminal fragment."; RL Immunity 54:1392-1404(2021). RN [25] {ECO:0007744|PDB:6X6A, ECO:0007744|PDB:6X6C} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH NLRP1 AND RP VAL-BOROPRO, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH NLRP1, AND RP MUTAGENESIS OF 100-LEU-LEU-101 AND GLU-597. RX PubMed=33731932; DOI=10.1038/s41586-021-03350-4; RA Hollingsworth L.R., Sharif H., Griswold A.R., Fontana P., Mintseris J., RA Dagbay K.B., Paulo J.A., Gygi S.P., Bachovchin D.A., Wu H.; RT "DPP9 sequesters the C terminus of NLRP1 to repress inflammasome RT activation."; RL Nature 592:778-783(2021). CC -!- FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides CC from proteins having a Pro or Ala residue at position 2 CC (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, CC PubMed:30291141, PubMed:33731929, PubMed:36112693). Acts as a key CC inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in CC resting cells by preventing activation of NLRP1 and CARD8 CC (PubMed:27820798, PubMed:29967349, PubMed:30291141, PubMed:31525884, CC PubMed:32796818, PubMed:36357533, PubMed:36112693). Sequesters the CC cleaved C-terminal part of NLRP1 and CARD8, which respectively CC constitute the active part of the NLRP1 and CARD8 inflammasomes, in a CC ternary complex, thereby preventing their oligomerization and CC activation (PubMed:34019797, PubMed:33731929, PubMed:33731932). The CC dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; CC however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, CC suggesting the existence of substrate(s) required for NLRP1 and CARD8 CC inhibition (PubMed:33731929). {ECO:0000269|PubMed:12662155, CC ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, CC ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29382749, CC ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:30291141, CC ECO:0000269|PubMed:31525884, ECO:0000269|PubMed:32796818, CC ECO:0000269|PubMed:33731929, ECO:0000269|PubMed:33731932, CC ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36112693, CC ECO:0000269|PubMed:36357533}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither CC Pro nor hydroxyproline.; EC=3.4.14.5; CC Evidence={ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913, CC ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, CC ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:30291141, CC ECO:0000269|PubMed:33731929}; CC -!- ACTIVITY REGULATION: Inhibited by the serine proteinase inhibitor 4-(2- CC aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di- CC isopropylfluorophosphate (PubMed:12662155). Inhibited by Val-boroPro CC (Talabostat, PT-100), a non-selective inhibitor, which triggers CC pyroptosis in monocytes and macrophages (PubMed:27820798, CC PubMed:29967349, PubMed:32796818, PubMed:33731932, PubMed:36357533). CC Val-boroPro inhibits activity by binding to the active site, mimicking CC a substrate-bound state, thereby displacing the C-terminal fragment of CC NLRP1, leading to activation of the NLRP1 inflammasome CC (PubMed:34019797, PubMed:33731932, PubMed:36357533). In contrast, Val- CC boroPro does not directly displaces CARD8: it acts by promoting CC degradation of the N-terminal part of CARD8, leading to indirect CC disruption of the ternary complex (PubMed:34019797). Chemical CC inhibition of DPP9 by Val-boroPro in HIV-1-infected cells activates the CC CARD8 inflammasome, triggering cell death, offering a promising CC strategy for the elimination of HIV-1 reservoirs in people living with CC HIV-1 (PubMed:36357533). {ECO:0000269|PubMed:12662155, CC ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29967349, CC ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731932, CC ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36357533}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=161 uM for Ala-Pro-AMC {ECO:0000269|PubMed:12662155, CC ECO:0000269|PubMed:15245913}; CC KM=180 uM for Ala-Pro-AFC {ECO:0000269|PubMed:12662155, CC ECO:0000269|PubMed:15245913}; CC KM=222 uM for Gly-Pro-AMC {ECO:0000269|PubMed:29382749}; CC KM=122 uM for Lys-Pro-AMC {ECO:0000269|PubMed:29382749}; CC KM=72.6 uM for Trp-Pro-AMC {ECO:0000269|PubMed:29382749}; CC KM=96 uM for Val-Pro-AMC {ECO:0000269|PubMed:29382749}; CC Note=kcat is 121 sec(-1) with Gly-Pro-AMC substrate CC (PubMed:29382749). kcat is 52.6 sec(-1) with Lys-Pro-AMC substrate CC (PubMed:29382749). kcat is 54 sec(-1) with Asp-Pro-AMC substrate CC (PubMed:29382749). kcat is 40.3 sec(-1) with Trp-Pro-AMC substrate CC (PubMed:29382749). kcat is 79.9 sec(-1) with Val-Pro-AMC substrate CC (PubMed:29382749). {ECO:0000269|PubMed:29382749}; CC pH dependence: CC Optimum pH is 7.5-8.5. Little activity below pH 6.5. CC {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913}; CC -!- SUBUNIT: Homodimer (PubMed:16475979, PubMed:29382749). Forms a ternary CC complex with NLRP1, composed of a DPP9 homodimer, one full-length NLRP1 CC protein, and one cleaved C-terminus of NLRP1 (NACHT, LRR and PYD CC domains-containing protein 1, C-terminus) (PubMed:33731929, CC PubMed:33731932). Forms a ternary complex with CARD8, composed of a CC DPP9 homodimer, one full-length NLRP1 protein, and one cleaved C- CC terminus of CARD8 (Caspase recruitment domain-containing protein 8, C- CC terminus) (PubMed:33731929, PubMed:34019797). In the ternary complex, CC only one subunit of the DPP9 homodimer is bound to NLRP1 or CARD8 CC (PubMed:34019797, PubMed:33731932). {ECO:0000269|PubMed:16475979, CC ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:33731929, CC ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797}. CC -!- INTERACTION: CC Q86TI2; Q86TI2: DPP9; NbExp=2; IntAct=EBI-7475352, EBI-7475352; CC Q86TI2-2; Q6NUP5: AGTR1; NbExp=3; IntAct=EBI-21529239, EBI-10232010; CC Q86TI2-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-21529239, EBI-10988864; CC Q86TI2-2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-21529239, EBI-2837444; CC Q86TI2-2; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-21529239, EBI-21553822; CC Q86TI2-2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-21529239, EBI-12593112; CC Q86TI2-2; O14645: DNALI1; NbExp=3; IntAct=EBI-21529239, EBI-395638; CC Q86TI2-2; Q01658: DR1; NbExp=3; IntAct=EBI-21529239, EBI-750300; CC Q86TI2-2; P29692-2: EEF1D; NbExp=3; IntAct=EBI-21529239, EBI-5280572; CC Q86TI2-2; Q06787-7: FMR1; NbExp=3; IntAct=EBI-21529239, EBI-25856644; CC Q86TI2-2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-21529239, EBI-1054873; CC Q86TI2-2; O14901: KLF11; NbExp=3; IntAct=EBI-21529239, EBI-948266; CC Q86TI2-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-21529239, EBI-2811583; CC Q86TI2-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-21529239, EBI-748974; CC Q86TI2-2; Q06830: PRDX1; NbExp=3; IntAct=EBI-21529239, EBI-353193; CC Q86TI2-2; P14678-2: SNRPB; NbExp=3; IntAct=EBI-21529239, EBI-372475; CC Q86TI2-2; P49458: SRP9; NbExp=3; IntAct=EBI-21529239, EBI-350743; CC Q86TI2-2; Q11203: ST3GAL3; NbExp=3; IntAct=EBI-21529239, EBI-717142; CC Q86TI2-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-21529239, EBI-372899; CC Q86TI2-2; P14927: UQCRB; NbExp=3; IntAct=EBI-21529239, EBI-743128; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol CC {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:24562348}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=DPP9-S, Short; CC IsoId=Q86TI2-1; Sequence=Displayed; CC Name=2; Synonyms=DPP9-L, Long; CC IsoId=Q86TI2-2; Sequence=VSP_013865; 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 {ECO:0000269|PubMed:12459266, ECO:0000269|PubMed:12662155, CC ECO:0000269|PubMed:15245913}. CC -!- DISEASE: Hatipoglu immunodeficiency syndrome (HATIS) [MIM:620331]: An CC autosomal recessive immunologic disorder manifesting in infancy or CC early childhood, and characterized by failure to thrive, short stature, CC skin pigmentation abnormalities, pancytopenia, and susceptibility to CC recurrent infections. {ECO:0000269|PubMed:36112693}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: Active peptidase. Contains a nuclear CC localization signal at positions 2-9. {ECO:0000269|PubMed:24562348}. CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC33801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAC62840.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAH37948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAL47179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAO73880.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB70784.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC11362.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC85150.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAD18643.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305}; CC Sequence=CAD39039.3; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS45928.1; -. [Q86TI2-2] DR CCDS; CCDS92491.1; -. [Q86TI2-1] DR RefSeq; NP_631898.3; NM_139159.4. [Q86TI2-2] DR RefSeq; XP_005259730.1; XM_005259673.2. DR RefSeq; XP_011526710.1; XM_011528408.1. DR RefSeq; XP_011526712.1; XM_011528410.1. DR PDB; 6EOQ; X-ray; 3.00 A; A/B/C/D=1-863. DR PDB; 6EOR; X-ray; 2.90 A; A/B/C/D=1-863. DR PDB; 6QZV; X-ray; 3.00 A; A/B/C/D=1-863. DR PDB; 6X6A; EM; 3.60 A; A/D=1-863. DR PDB; 6X6C; EM; 2.90 A; A/D=1-863. DR PDB; 7A3F; X-ray; 2.90 A; A/B/C/D=1-863. DR PDB; 7JKQ; EM; 3.30 A; A/D=1-863. DR PDB; 7JN7; EM; 3.30 A; A/D=1-863. DR PDB; 7SVL; X-ray; 2.46 A; A/B/C/D=1-863. DR PDB; 7SVN; X-ray; 2.78 A; A/B/C/D=1-863. DR PDB; 7ZXS; X-ray; 1.81 A; A/B/C/D=20-863. DR PDBsum; 6EOQ; -. DR PDBsum; 6EOR; -. DR PDBsum; 6QZV; -. DR PDBsum; 6X6A; -. DR PDBsum; 6X6C; -. DR PDBsum; 7A3F; -. DR PDBsum; 7JKQ; -. DR PDBsum; 7JN7; -. DR PDBsum; 7SVL; -. DR PDBsum; 7SVN; -. DR PDBsum; 7ZXS; -. DR AlphaFoldDB; Q86TI2; -. DR EMDB; EMD-22074; -. DR EMDB; EMD-22075; -. DR EMDB; EMD-22367; -. DR EMDB; EMD-22402; -. DR SMR; Q86TI2; -. DR BioGRID; 124789; 126. DR IntAct; Q86TI2; 47. DR MINT; Q86TI2; -. DR STRING; 9606.ENSP00000262960; -. DR BindingDB; Q86TI2; -. DR ChEMBL; CHEMBL4793; -. DR DrugCentral; Q86TI2; -. DR GuidetoPHARMACOLOGY; 2357; -. DR ESTHER; human-DPP9; DPP4N_Peptidase_S9. DR MEROPS; S09.019; -. DR iPTMnet; Q86TI2; -. DR MetOSite; Q86TI2; -. DR PhosphoSitePlus; Q86TI2; -. DR SwissPalm; Q86TI2; -. DR BioMuta; DPP9; -. DR DMDM; 67460390; -. DR EPD; Q86TI2; -. DR jPOST; Q86TI2; -. DR MassIVE; Q86TI2; -. DR MaxQB; Q86TI2; -. DR PaxDb; 9606-ENSP00000262960; -. DR PeptideAtlas; Q86TI2; -. DR ProteomicsDB; 69697; -. [Q86TI2-1] DR ProteomicsDB; 69698; -. [Q86TI2-2] DR ProteomicsDB; 69700; -. [Q86TI2-4] DR Pumba; Q86TI2; -. DR Antibodypedia; 23705; 478 antibodies from 29 providers. DR DNASU; 91039; -. DR Ensembl; ENST00000262960.14; ENSP00000262960.8; ENSG00000142002.19. [Q86TI2-2] DR Ensembl; ENST00000593973.2; ENSP00000515514.1; ENSG00000142002.19. [Q86TI2-1] DR Ensembl; ENST00000594671.5; ENSP00000472224.1; ENSG00000142002.19. [Q86TI2-4] DR Ensembl; ENST00000598800.5; ENSP00000469603.1; ENSG00000142002.19. [Q86TI2-1] DR Ensembl; ENST00000600621.6; ENSP00000472549.2; ENSG00000142002.19. [Q86TI2-2] DR Ensembl; ENST00000601130.6; ENSP00000471629.2; ENSG00000142002.19. [Q86TI2-2] DR GeneID; 91039; -. DR KEGG; hsa:91039; -. DR MANE-Select; ENST00000262960.14; ENSP00000262960.8; NM_139159.5; NP_631898.3. [Q86TI2-2] DR UCSC; uc002mba.5; human. [Q86TI2-1] DR AGR; HGNC:18648; -. DR CTD; 91039; -. DR DisGeNET; 91039; -. DR GeneCards; DPP9; -. DR HGNC; HGNC:18648; DPP9. DR HPA; ENSG00000142002; Low tissue specificity. DR MalaCards; DPP9; -. DR MIM; 608258; gene. DR MIM; 620331; phenotype. DR neXtProt; NX_Q86TI2; -. DR OpenTargets; ENSG00000142002; -. DR Orphanet; 2032; Idiopathic pulmonary fibrosis. DR PharmGKB; PA38620; -. DR VEuPathDB; HostDB:ENSG00000142002; -. DR eggNOG; KOG2281; Eukaryota. DR GeneTree; ENSGT00940000158174; -. DR HOGENOM; CLU_006105_1_0_1; -. DR InParanoid; Q86TI2; -. DR OMA; VTHMTPQ; -. DR OrthoDB; 170111at2759; -. DR PhylomeDB; Q86TI2; -. DR TreeFam; TF313309; -. DR BRENDA; 3.4.13.19; 2681. DR PathwayCommons; Q86TI2; -. DR SABIO-RK; Q86TI2; -. DR SignaLink; Q86TI2; -. DR BioGRID-ORCS; 91039; 27 hits in 1157 CRISPR screens. DR ChiTaRS; DPP9; human. DR GeneWiki; DPP9; -. DR GenomeRNAi; 91039; -. DR Pharos; Q86TI2; Tchem. DR PRO; PR:Q86TI2; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q86TI2; Protein. DR Bgee; ENSG00000142002; Expressed in gastrocnemius and 164 other cell types or tissues. DR ExpressionAtlas; Q86TI2; baseline and differential. DR GO; GO:0031252; C:cell leading edge; IDA:CACAO. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005874; C:microtubule; IDA:CACAO. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0043069; P:negative regulation of programmed cell death; IDA:UniProt. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0070269; P:pyroptosis; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR045785; Dpp_8/9_N. DR InterPro; IPR001375; Peptidase_S9. DR InterPro; IPR002469; Peptidase_S9B_N. DR PANTHER; PTHR11731:SF109; DIPEPTIDYL PEPTIDASE 9; 1. DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1. DR Pfam; PF19520; Dpp_8_9_N; 1. DR Pfam; PF00930; DPPIV_N; 1. DR Pfam; PF00326; Peptidase_S9; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1. DR Genevisible; Q86TI2; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminopeptidase; Cytoplasm; KW Disease variant; Hydrolase; Nucleus; Protease; Reference proteome; KW Serine protease. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..863 FT /note="Dipeptidyl peptidase 9" FT /id="PRO_0000122415" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 730 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:30291141" FT ACT_SITE 808 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:Q6V1X1" FT ACT_SITE 840 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:Q6V1X1" FT BINDING 730 FT /ligand="Val-boroPro" FT /ligand_id="ChEBI:CHEBI:187904" FT /ligand_note="inhibitor" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:33731932, FT ECO:0000269|PubMed:34019797, ECO:0007744|PDB:6X6C, FT ECO:0007744|PDB:7JN7" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT VAR_SEQ 1 FT /note="M -> MRKVKKLRLDKENTGSWRSFSLNSEGAERM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12459266, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15245913, FT ECO:0000303|PubMed:15489334" FT /id="VSP_013865" FT VAR_SEQ 832..858 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_013869" FT VARIANT 82..863 FT /note="Missing (in HATIS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:36112693" FT /id="VAR_088502" FT VARIANT 138 FT /note="G -> S (in HATIS; likely pathogenic; decreased FT dipeptidyl-peptidase activity; less able to maintain NLRP1 FT in the inactive state)" FT /evidence="ECO:0000269|PubMed:36112693" FT /id="VAR_088503" FT VARIANT 185..863 FT /note="Missing (in HATIS; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:36112693" FT /id="VAR_088504" FT VARIANT 822..863 FT /note="Missing (in HATIS; likely pathogenic; no protein FT detected by Wester blot analysis in homozygous patient FT cells)" FT /evidence="ECO:0000269|PubMed:36112693" FT /id="VAR_088505" FT MUTAGEN 96..97 FT /note="RK->EE: Reduced interaction with CARD8 without FT affecting the peptidase activity." FT /evidence="ECO:0000269|PubMed:34019797" FT MUTAGEN 100..101 FT /note="LL->EE: Reduced interaction with NLRP1 and CARD8 FT without affecting the peptidase activity." FT /evidence="ECO:0000269|PubMed:33731932, FT ECO:0000269|PubMed:34019797" FT MUTAGEN 102..103 FT /note="LL->EE: Reduced interaction with CARD8 without FT affecting the peptidase activity." FT /evidence="ECO:0000269|PubMed:34019797" FT MUTAGEN 102 FT /note="L->E: Reduced interaction with NLRP1 without FT affecting the peptidase activity." FT /evidence="ECO:0000269|PubMed:33731929" FT MUTAGEN 597 FT /note="E->R: Reduced interaction with NLRP1 without FT affecting the peptidase activity." FT /evidence="ECO:0000269|PubMed:33731932" FT MUTAGEN 730 FT /note="S->A: Abolished dipeptidyl peptidase activity and FT ability to sequester NLRP1 and inhibit pyroptosis." FT /evidence="ECO:0000269|PubMed:30291141, FT ECO:0000269|PubMed:33731929" FT CONFLICT 204 FT /note="I -> N (in Ref. 3; AAO73880/AAQ83119)" FT /evidence="ECO:0000305" FT CONFLICT 461 FT /note="L -> F (in Ref. 9; CAD39039)" FT /evidence="ECO:0000305" FT CONFLICT 571 FT /note="C -> W (in Ref. 5; BAC85150)" FT /evidence="ECO:0000305" FT CONFLICT 709 FT /note="L -> P (in Ref. 5; BAD18643)" FT /evidence="ECO:0000305" FT CONFLICT 753 FT /note="G -> C (in Ref. 5; BAB70784)" FT /evidence="ECO:0000305" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:7SVL" FT HELIX 31..48 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 64..76 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 82..93 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:7SVL" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:6X6C" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 123..131 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:6X6C" FT STRAND 183..186 FT /evidence="ECO:0007829|PDB:6X6C" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 200..205 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 237..240 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 244..250 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:7SVL" FT STRAND 271..281 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:6EOQ" FT STRAND 287..291 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 307..310 FT /evidence="ECO:0007829|PDB:6X6C" FT STRAND 314..324 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 330..340 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 342..345 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 351..357 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 364..369 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:6QZV" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 393..402 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 410..416 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:6X6C" FT STRAND 438..446 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 447..449 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 453..460 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 468..470 FT /evidence="ECO:0007829|PDB:7SVL" FT TURN 476..479 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 483..490 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 492..494 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 508..511 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 512..517 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 526..534 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 546..552 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 556..564 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 566..568 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 571..579 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 584..586 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 588..596 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 609..614 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 620..626 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 636..642 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 653..655 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 658..660 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 662..669 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 673..678 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 683..685 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 687..690 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 691..693 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 697..700 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 701..716 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 719..729 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 731..742 FT /evidence="ECO:0007829|PDB:7ZXS" FT TURN 744..746 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 748..754 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 759..761 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 764..771 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 774..776 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 778..784 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 786..792 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 795..798 FT /evidence="ECO:0007829|PDB:7JN7" FT STRAND 799..805 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 809..811 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 814..825 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 831..835 FT /evidence="ECO:0007829|PDB:7ZXS" FT STRAND 839..841 FT /evidence="ECO:0007829|PDB:7ZXS" FT HELIX 845..862 FT /evidence="ECO:0007829|PDB:7ZXS" 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 //