TPP2_DROME
ID TPP2_DROME Reviewed; 1441 AA.
AC Q9V6K1; B5RJ14; O76251; Q8IH59; Q8ML58;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Tripeptidyl-peptidase 2;
DE Short=TPP-2;
DE EC=3.4.14.10 {ECO:0000269|PubMed:9668104};
DE AltName: Full=Tripeptidyl aminopeptidase;
DE AltName: Full=Tripeptidyl-peptidase II;
DE Short=TPP-II;
DE Short=dTPP II;
GN Name=TppII; ORFNames=CG3991;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9668104; DOI=10.1074/jbc.273.30.19173;
RA Renn S.C.P., Tomkinson B., Taghert P.H.;
RT "Characterization and cloning of tripeptidyl peptidase II from the fruit
RT fly, Drosophila melanogaster.";
RL J. Biol. Chem. 273:19173-19182(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.W.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT.
RX PubMed=12426370; DOI=10.1093/emboj/cdf601;
RA Rockel B., Peters J., Kuhlmorgen B., Glaeser R.M., Baumeister W.;
RT "A giant protease with a twist: the TPP II complex from Drosophila studied
RT by electron microscopy.";
RL EMBO J. 21:5979-5984(2002).
RN [7]
RP SUBUNIT, AND STRUCTURE OF THE HOMOOLIGOMER.
RX PubMed=16006508; DOI=10.1073/pnas.0504569102;
RA Rockel B., Peters J., Mueller S.A., Seyit G., Ringler P., Hegerl R.,
RA Glaeser R.M., Baumeister W.;
RT "Molecular architecture and assembly mechanism of Drosophila tripeptidyl
RT peptidase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10135-10140(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 89-1441, ELECTRON MICROSCOPY (14
RP ANGSTROMS), SUBUNIT, MECHANISM OF ACTION, AND ACTIVE SITE.
RX PubMed=20676100; DOI=10.1038/nsmb.1870;
RA Chuang C.K., Rockel B., Seyit G., Walian P.J., Schonegge A.M., Peters J.,
RA Zwart P.H., Baumeister W., Jap B.K.;
RT "Hybrid molecular structure of the giant protease tripeptidyl peptidase
RT II.";
RL Nat. Struct. Mol. Biol. 17:990-996(2010).
CC -!- FUNCTION: Component of the proteolytic cascade acting downstream of the
CC 26S proteasome in the ubiquitin-proteasome pathway (By similarity).
CC Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-
CC polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does
CC not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000269|PubMed:9668104};
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF)
CC and butabindide, but not by peptidase inhibitor pepstatin, EDTA, nor
CC bestatin. {ECO:0000269|PubMed:9668104}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-7.8. {ECO:0000269|PubMed:9668104};
CC -!- SUBUNIT: Homooligomer; forms a complex of 6 MDa probably composed of 40
CC subunits. Forms a structure consisting of 2 segmented and twisted
CC strands that form a spindle-shaped structure. Each strand is composed
CC of 10 segments (a segment being a homodimer oriented head to head),
CC stacking of these segments leads to the formation of a twisted single
CC strand. 2 strands compose the fully assembled spindle.
CC {ECO:0000269|PubMed:12426370, ECO:0000269|PubMed:16006508,
CC ECO:0000269|PubMed:20676100}.
CC -!- INTERACTION:
CC Q9V6K1-2; Q9V6K1-2: TppII; NbExp=3; IntAct=EBI-3416753, EBI-3416753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=D;
CC IsoId=Q9V6K1-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q9V6K1-2; Sequence=VSP_015220;
CC -!- MISCELLANEOUS: The limitation of proteolytic products to tripeptides is
CC achieved by tailoring the size of the substrate-binding cleft: the two
CC negatively charged residues Glu-399 and Glu-430 that are blocking
CC position P4 limit the number of residues that can be accommodated in
CC the binding cleft and thus create a molecular ruler. At the same time,
CC they orient substrates so that the tripeptides are removed exclusively
CC from the N-terminus (PubMed:20676100). {ECO:0000305|PubMed:20676100}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF035251; AAC28563.1; -; mRNA.
DR EMBL; AE013599; AAF58422.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68593.1; -; Genomic_DNA.
DR EMBL; BT001404; AAN71159.1; -; mRNA.
DR EMBL; BT003260; AAO25017.1; -; mRNA.
DR EMBL; BT044288; ACH92353.1; -; mRNA.
DR PIR; T13930; T13930.
DR RefSeq; NP_001286376.1; NM_001299447.1. [Q9V6K1-2]
DR RefSeq; NP_477247.1; NM_057899.3. [Q9V6K1-2]
DR RefSeq; NP_725252.1; NM_165966.2. [Q9V6K1-1]
DR PDB; 3LXU; X-ray; 3.14 A; X=88-1441.
DR PDBsum; 3LXU; -.
DR AlphaFoldDB; Q9V6K1; -.
DR SMR; Q9V6K1; -.
DR BioGRID; 62211; 7.
DR DIP; DIP-59032N; -.
DR IntAct; Q9V6K1; 8.
DR STRING; 7227.FBpp0086887; -.
DR MEROPS; S08.090; -.
DR iPTMnet; Q9V6K1; -.
DR PaxDb; Q9V6K1; -.
DR PRIDE; Q9V6K1; -.
DR DNASU; 36444; -.
DR EnsemblMetazoa; FBtr0087774; FBpp0086887; FBgn0020370. [Q9V6K1-1]
DR EnsemblMetazoa; FBtr0087775; FBpp0086888; FBgn0020370. [Q9V6K1-2]
DR EnsemblMetazoa; FBtr0344199; FBpp0310608; FBgn0020370. [Q9V6K1-2]
DR GeneID; 36444; -.
DR KEGG; dme:Dmel_CG3991; -.
DR CTD; 36444; -.
DR FlyBase; FBgn0020370; TppII.
DR VEuPathDB; VectorBase:FBgn0020370; -.
DR eggNOG; KOG1114; Eukaryota.
DR GeneTree; ENSGT00390000014623; -.
DR InParanoid; Q9V6K1; -.
DR PhylomeDB; Q9V6K1; -.
DR BRENDA; 3.4.14.10; 1994.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 36444; 0 hits in 1 CRISPR screen.
DR ChiTaRS; TppII; fly.
DR GenomeRNAi; 36444; -.
DR PRO; PR:Q9V6K1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0020370; Expressed in egg cell and 45 other tissues.
DR ExpressionAtlas; Q9V6K1; baseline and differential.
DR Genevisible; Q9V6K1; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR DisProt; DP02711; -.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR022229; Peptidase_S8A_TPPII.
DR InterPro; IPR022232; Peptidase_S8A_TPPII_art.
DR InterPro; IPR034051; TPP_II_domain.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF12583; TPPII_N; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aminopeptidase; Cytoplasm; Hydrolase;
KW Phosphoprotein; Protease; Reference proteome; Serine protease.
FT CHAIN 1..1441
FT /note="Tripeptidyl-peptidase 2"
FT /id="PRO_0000076425"
FT DOMAIN 107..608
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 62..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:20676100"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:20676100"
FT ACT_SITE 549
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:20676100"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9668104, ECO:0000303|Ref.5"
FT /id="VSP_015220"
FT CONFLICT 103
FT /note="V -> M (in Ref. 4; AAN71159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1377
FT /note="A -> G (in Ref. 1; AAC28563)"
FT /evidence="ECO:0000305"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 265..282
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 401..416
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 439..449
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 552..568
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 575..583
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 618..621
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 622..628
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 629..632
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 647..659
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 674..681
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 697..703
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 710..723
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 730..739
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 746..749
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 783..790
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 799..808
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 818..830
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 832..837
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 842..850
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 858..867
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 869..871
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 874..877
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 878..880
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 886..894
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 896..911
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 916..920
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 923..928
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 929..931
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 935..947
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 949..954
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 956..960
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 972..975
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 981..985
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 994..996
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 998..1010
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1012..1015
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1016..1018
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1023..1035
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1038..1040
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1041..1045
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1054..1056
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1058..1065
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1070..1074
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 1075..1077
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1082..1093
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1095..1100
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1103..1108
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1190..1205
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1210..1223
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1229..1241
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1248..1253
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1265..1268
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1271..1289
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1293..1296
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 1297..1299
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1307..1310
FT /evidence="ECO:0007829|PDB:3LXU"
FT STRAND 1312..1314
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1317..1345
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1349..1351
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1352..1362
FT /evidence="ECO:0007829|PDB:3LXU"
FT TURN 1371..1373
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1374..1384
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1387..1400
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1404..1417
FT /evidence="ECO:0007829|PDB:3LXU"
FT HELIX 1420..1433
FT /evidence="ECO:0007829|PDB:3LXU"
SQ SEQUENCE 1441 AA; 158737 MW; D71CF8558BE30922 CRC64;
MFNRFRLVHK QLRLYKNFGL LGQKASVGLT LPIISLSRPY MAYMGTERSV VMITAPATKE
FAESSERSNS SKKTTNKEQS DKSAESRMAT SGIVESFPTG ALVPKAETGV LNFLQKYPEY
DGRDVTIAIF DSGVDPRATG LETLCDGKTV KVIERYDCSG CGDVDMKKKV TPDENGNIKG
LSGNSLKLSP ELMALNTDPE KAVRVGLKSF SDLLPSKVRN NIVAQAKLKH WDKPHKTATA
NASRKIVEFE SQNPGEASKL PWDKKILKEN LDFELEMLNS YEKVYGDIKT SYDCILFPTA
DGWLTIVDTT EQGDLDQALR IGEYSRTHET RNVDDFLSIS VNVHDEGNVL EVVGMSSPHG
THVSSIASGN HSSRDVDGVA PNAKIVSMTI GDGRLGSMET GTALVRAMTK VMELCRDGRR
IDVINMSYGE HANWSNSGRI GELMNEVVNK YGVVWVASAG NHGPALCTVG TPPDISQPSL
IGVGAYVSPQ MMEAEYAMRE KLPGNVYTWT SRDPCIDGGQ GVTVCAPGGA IASVPQFTMS
KSQLMNGTSM AAPHVAGAVA LLISGLKQQN IEYSPYSIKR AISVTATKLG YVDPFAQGHG
LLNVEKAFEH LTEHRQSKDN MLRFSVRVGN NADKGIHLRQ GVQRNSIDYN VYIEPIFYND
KEADPKDKFN FNVRLNLIAS QPWVQCGAFL DLSYGTRSIA VRVDPTGLQP GVHSAVIRAY
DTDCVQKGSL FEIPVTVVQP HVLESDQNTP VFEPASSKGD NSVEFQPNTI QRDFILVPER
ATWAELRMRI TDPNRGEDIG KFFVHTNQLL PKQSCRKLET MKIVSVGSEN ESIMAFKVKS
GRILELCIAK YWSNYGQSHL KYSLRFRGVE AHNPNAYVMH AGRGIHKLEI EALVAEDVQP
QLQLKNAEVV LKPTEAKISP LSATRDVIPD GRQVYQNLLA FNLNVAKAAD VSIYAPIFND
LLYEAEFESQ MWMLFDANKA LVATGDAHSH TSFTKLDKGE YTIRLQVRHE KRDLLEKISE
ANLVASFKLT SPLTLDFYEN YNQCIVGGRK YVSSPLRLST RVLYIAPITQ ERLTKANLPA
QCAWLSGNLV FPQDEVGRRV AQHPFTYILN PAEKKSHTNG SSNGSSAAGS TATAAAVTTA
NGAKPKAPAT PQAATSVTNP AAGDGISVQN DPPVDSSGSP ASPKKGKANA DDYAESFRDF
QCSQIVKCEL EMAEKIYNDV VAAHPKHLQA NLLLIQNIES NQLKSQLPLT FVNAQKTSPP
EAGESADKQK EDQKKVRSAL ERIVKLADKV IQETDSEALL SYYGLKNDTR ADAAKIKTNM
DKQKNTLIEA LSKKGIAVAK LAVLDDCIKD SLAEINELYT EIIKFVDAND SKAIQFALWH
AYAHGHYGRM YKYVVKLIEE KRTRDHFVEL AAINGALGHE HIRTVINRMM ITAFPSSFRL
F
