DPP9_HUMAN
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 03-AUG-2022, entry version 165.
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] {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 [21]
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 [22] {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 [23] {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). Acts as a key inhibitor of caspase-
CC 1-dependent monocyte and macrophage pyroptosis in resting cells by
CC preventing activation of NLRP1 and CARD8 (PubMed:27820798,
CC PubMed:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818).
CC Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which
CC respectively constitute the active part of the NLRP1 and CARD8
CC inflammasomes, in a ternary complex, thereby preventing their
CC oligomerization and activation (PubMed:34019797, PubMed:33731929,
CC PubMed:33731932). The dipeptidyl peptidase activity is required to
CC suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona
CC fide substrates of DPP9, suggesting the existence of substrate(s)
CC required for NLRP1 and CARD8 inhibition (PubMed:33731929).
CC {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:16475979,
CC ECO:0000269|PubMed:19667070, ECO:0000269|PubMed:27820798,
CC ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:29967349,
CC ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:31525884,
CC ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731929,
CC ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797}.
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). Val-boroPro
CC inhibits activity by binding to the active site, mimicking a substrate-
CC bound state, thereby displacing the C-terminal fragment of NLRP1,
CC leading to activation of the NLRP1 inflammasome (PubMed:34019797,
CC PubMed:33731932). In contrast, Val-boroPro does not directly displaces
CC CARD8: it acts by promoting degradation of the N-terminal part of
CC CARD8, leading to indirect disruption of the ternary complex
CC (PubMed:34019797). {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}.
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 -!- 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};
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DR EMBL; AF452102; AAL47179.1; ALT_INIT; mRNA.
DR EMBL; AY172660; AAO17262.1; -; mRNA.
DR EMBL; AF542510; AAO73880.2; ALT_INIT; mRNA.
DR EMBL; AY374518; AAQ83119.1; -; mRNA.
DR EMBL; DQ417928; ABD83624.1; -; mRNA.
DR EMBL; AK054656; BAB70784.1; ALT_INIT; mRNA.
DR EMBL; AK075030; BAC11362.1; ALT_INIT; mRNA.
DR EMBL; AK122654; BAG53644.1; -; mRNA.
DR EMBL; AK131100; BAC85150.1; ALT_SEQ; mRNA.
DR EMBL; AK131499; BAD18643.1; ALT_SEQ; mRNA.
DR EMBL; AC005594; AAC33801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005783; AAC62840.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471139; EAW69199.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69201.1; -; Genomic_DNA.
DR EMBL; BC000970; AAH00970.1; -; mRNA.
DR EMBL; BC037948; AAH37948.1; ALT_INIT; mRNA.
DR EMBL; AL834376; CAD39039.3; ALT_FRAME; mRNA.
DR EMBL; CR627380; CAH10477.1; -; mRNA.
DR CCDS; CCDS45928.1; -. [Q86TI2-2]
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. [Q86TI2-2]
DR RefSeq; XP_011526712.1; XM_011528410.1. [Q86TI2-1]
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 PDBsum; 6EOQ; -.
DR PDBsum; 6EOR; -.
DR PDBsum; 6QZV; -.
DR PDBsum; 6X6A; -.
DR PDBsum; 6X6C; -.
DR PDBsum; 7A3F; -.
DR PDBsum; 7JKQ; -.
DR PDBsum; 7JN7; -.
DR AlphaFoldDB; Q86TI2; -.
DR SMR; Q86TI2; -.
DR BioGRID; 124789; 118.
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 PhosphoSitePlus; Q86TI2; -.
DR BioMuta; DPP9; -.
DR DMDM; 67460390; -.
DR EPD; Q86TI2; -.
DR jPOST; Q86TI2; -.
DR MassIVE; Q86TI2; -.
DR MaxQB; Q86TI2; -.
DR PaxDb; Q86TI2; -.
DR PeptideAtlas; Q86TI2; -.
DR PRIDE; Q86TI2; -.
DR ProteomicsDB; 69697; -. [Q86TI2-1]
DR ProteomicsDB; 69698; -. [Q86TI2-2]
DR ProteomicsDB; 69700; -. [Q86TI2-4]
DR Antibodypedia; 23705; 410 antibodies from 29 providers.
DR DNASU; 91039; -.
DR Ensembl; ENST00000262960.14; ENSP00000262960.8; ENSG00000142002.18. [Q86TI2-2]
DR Ensembl; ENST00000594671.5; ENSP00000472224.1; ENSG00000142002.18. [Q86TI2-4]
DR Ensembl; ENST00000598800.5; ENSP00000469603.1; ENSG00000142002.18. [Q86TI2-1]
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 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 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; 137965at2759; -.
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 1077 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 162 other tissues.
DR ExpressionAtlas; Q86TI2; baseline and differential.
DR Genevisible; Q86TI2; HS.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0070269; P:pyroptosis; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 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 Pfam; PF19520; Dpp_8_9_N; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminopeptidase; Cytoplasm;
KW Hydrolase; Nucleus; Protease; Reference proteome; 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 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 HELIX 20..22
FT /evidence="ECO:0007829|PDB:6X6C"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:7JKQ"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6X6C"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7A3F"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6X6C"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6X6C"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6X6C"
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:6EOR"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6X6C"
FT STRAND 271..281
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6EOQ"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6X6C"
FT STRAND 314..324
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 330..340
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6QZV"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:6X6C"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 483..490
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 508..511
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 556..564
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 571..579
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 620..626
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 636..642
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 658..661
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 662..670
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 687..691
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 692..695
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 700..715
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 719..729
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 731..742
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 744..746
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 748..754
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 759..761
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 764..771
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 778..783
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 786..792
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 795..805
FT /evidence="ECO:0007829|PDB:6EOR"
FT TURN 809..813
FT /evidence="ECO:0007829|PDB:6EOR"
FT HELIX 814..826
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 831..835
FT /evidence="ECO:0007829|PDB:6EOR"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:6EOQ"
FT HELIX 845..862
FT /evidence="ECO:0007829|PDB:6EOR"
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
