ID TOXA_PSEAE Reviewed; 638 AA. AC P11439; Q9I4I7; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=Exotoxin A {ECO:0000303|PubMed:6201861}; DE Short=ETA {ECO:0000303|PubMed:6201861}; DE EC=2.4.2.36 {ECO:0000269|PubMed:2170123}; DE AltName: Full=NAD(+)--diphthamide ADP-ribosyltransferase; DE AltName: Full=Pseudomonas exotoxin {ECO:0000303|PubMed:2118903}; DE Short=PE {ECO:0000303|PubMed:2118903}; DE Flags: Precursor; GN Name=eta {ECO:0000303|PubMed:6201861}; OrderedLocusNames=PA1148; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-53. RX PubMed=6201861; DOI=10.1073/pnas.81.9.2645; RA Gray G.L., Smith D.H., Baldridge J.S., Harkins R.N., Vasil M.L., Chen E.Y., RA Heyneker H.L.; RT "Cloning, nucleotide sequence, and expression in Escherichia coli of the RT exotoxin A structural gene of Pseudomonas aeruginosa."; RL Proc. Natl. Acad. Sci. U.S.A. 81:2645-2649(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [3] RP ACTIVE SITE. RX PubMed=2885323; DOI=10.1016/s0021-9258(18)47472-8; RA Carroll S.F., Collier R.J.; RT "Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is RT photolabeled by NAD and shows functional homology with glutamic acid 148 of RT diphtheria toxin."; RL J. Biol. Chem. 262:8707-8711(1987). RN [4] RP DOMAINS, AND MUTAGENESIS OF LYS-82; 266-PRO--PHE-275 AND 271-HIS--HIS-274. RX PubMed=2118903; DOI=10.1016/s0021-9258(17)46223-5; RA Chaudhary V.K., Jinno Y., Galo M.G., Fitzgerald D., Pastan I.; RT "Mutagenesis of Pseudomonas exotoxin in identification of sequences RT responsible for the animal toxicity."; RL J. Biol. Chem. 265:16306-16310(1990). RN [5] RP PROTEIN SEQUENCE OF 396-408 AND 415-424, FUNCTION, CATALYTIC ACTIVITY, AND RP DOMAINS. RX PubMed=2170123; DOI=10.1111/j.1432-1033.1990.tb19238.x; RA Bourdenet S., Vacheron M.-J., Guinand M., Michel G., Arminjon F.; RT "Biochemical and immunochemical studies of proteolytic fragments of RT exotoxin A from Pseudomonas aeruginosa."; RL Eur. J. Biochem. 192:379-385(1990). RN [6] RP RECEPTOR-BINDING, AND MUTAGENESIS OF LYS-82. RX PubMed=1618748; DOI=10.1016/s0021-9258(18)42291-0; RA Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K., RA Saelinger C.B.; RT "The alpha 2-macroglobulin receptor/low density lipoprotein receptor- RT related protein binds and internalizes Pseudomonas exotoxin A."; RL J. Biol. Chem. 267:12420-12423(1992). RN [7] RP DISULFIDE BOND. RX PubMed=10600112; DOI=10.1021/bi991308+; RA McKee M.L., FitzGerald D.J.; RT "Reduction of furin-nicked Pseudomonas exotoxin A: an unfolding story."; RL Biochemistry 38:16507-16513(1999). RN [8] RP FUNCTION AS A TOXIN, FUNCTION AS A GLYCOHYDROLASE, FUNCTION AS AN RP ADP-RIBOSYLTRANSFERASE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-578. RX PubMed=18276581; DOI=10.1074/jbc.m710008200; RA Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H., RA Merrill A.R.; RT "Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae."; RL J. Biol. Chem. 283:10671-10678(2008). RN [9] RP ACTIVITY REGULATION, AND TOXIC DOSE. RX PubMed=21135177; DOI=10.1128/aac.01164-10; RA Turgeon Z., Jorgensen R., Visschedyk D., Edwards P.R., Legree S., RA McGregor C., Fieldhouse R.J., Mangroo D., Schapira M., Merrill A.R.; RT "Newly discovered and characterized antivirulence compounds inhibit RT bacterial mono-ADP-ribosyltransferase toxins."; RL Antimicrob. Agents Chemother. 55:983-991(2011). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 424-638. RX PubMed=7568123; DOI=10.1073/pnas.92.20.9308; RA Li M., Dyda F., Benhar I., Pastan I., Davies D.R.; RT "The crystal structure of Pseudomonas aeruginosa exotoxin domain III with RT nicotinamide and AMP: conformational differences with the intact RT exotoxin."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9308-9312(1995). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 424-638. RX PubMed=8692916; DOI=10.1073/pnas.93.14.6902; RA Li M., Dyda F., Benhar I., Pastan I., Davies D.R.; RT "Crystal structure of the catalytic domain of Pseudomonas exotoxin A RT complexed with a nicotinamide adenine dinucleotide analog: implications for RT the activation process and for ADP ribosylation."; RL Proc. Natl. Acad. Sci. U.S.A. 93:6902-6906(1996). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 425-630 IN COMPLEX WITH YEAST RP EEF2 AND NAD, AND MUTAGENESIS OF ARG-481; GLU-571; ARG-576 AND GLU-578. RX PubMed=18583986; DOI=10.1038/embor.2008.90; RA Jorgensen R., Wang Y., Visschedyk D., Merrill A.R.; RT "The nature and character of the transition state for the ADP- RT ribosyltransferase reaction."; RL EMBO Rep. 9:802-809(2008). CC -!- FUNCTION: An NAD-dependent ADP-ribosyltransferase (ADPRT). Catalyzes CC the transfer of the ADP ribosyl moiety of oxidized NAD (NAD(+)) onto CC eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis CC (PubMed:2170123, PubMed:18276581). Has an LD(50) of 65 ng/ml against CC the human lung epithelial cell line C38 (PubMed:21135177). CC {ECO:0000269|PubMed:18276581, ECO:0000269|PubMed:21135177, CC ECO:0000269|PubMed:2170123}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphthamide-[translation elongation factor 2] + NAD(+) = H(+) CC + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + CC nicotinamide; Xref=Rhea:RHEA:11820, Rhea:RHEA-COMP:10174, Rhea:RHEA- CC COMP:10175, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:17154, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:82697; EC=2.4.2.36; CC Evidence={ECO:0000269|PubMed:18276581, ECO:0000269|PubMed:2170123}; CC -!- ACTIVITY REGULATION: Inhibited by 1,8-naphthalimide (NAP) as well as a CC number of poly(ADP-ribose) polymerase inhibitors and other compounds. CC {ECO:0000269|PubMed:21135177}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=121 uM for NAD; CC Note=For ADP-ribosyltransferase activity of the catalytic fragment CC 399-605.; CC -!- DOMAIN: Domain I (which is divided into 2 non-contiguous regions Ia and CC Ib) is required for binding to cells, but not for ADPRT activity CC (Probable) (PubMed:2170123). A subtilisin-digested fragment starting CC about residue 417 and extending to the C-terminus has full ADPRT CC activity (PubMed:2170123). {ECO:0000269|PubMed:2170123, CC ECO:0000305|PubMed:2118903}. CC -!- PTM: The 8 cysteines participate in intrachain disulfide bonds. 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; K01397; AAB59097.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04537.1; -; Genomic_DNA. DR PIR; A30347; A30347. DR PIR; C83503; C83503. DR RefSeq; NP_249839.1; NC_002516.2. DR RefSeq; WP_003112478.1; NZ_QZGE01000006.1. DR PDB; 1AER; X-ray; 2.30 A; A/B=425-634. DR PDB; 1DMA; X-ray; 2.50 A; A/B=425-638. DR PDB; 1IKP; X-ray; 1.45 A; A=26-638. DR PDB; 1IKQ; X-ray; 1.62 A; A=26-638. DR PDB; 1XK9; X-ray; 2.10 A; A/B=424-638. DR PDB; 1ZM2; X-ray; 3.07 A; B/D/F=424-630. DR PDB; 1ZM3; X-ray; 3.07 A; B/D/F=424-630. DR PDB; 1ZM4; X-ray; 2.90 A; B/D/F=424-630. DR PDB; 1ZM9; X-ray; 2.80 A; B/D/F=424-630. DR PDB; 2ZIT; X-ray; 3.00 A; B/D/F=425-630. DR PDB; 3B78; X-ray; 2.50 A; B/D/F=425-630. DR PDB; 3B82; X-ray; 2.35 A; B/D/F=425-630. DR PDB; 3B8H; X-ray; 2.50 A; B/D/F=425-630. DR PDBsum; 1AER; -. DR PDBsum; 1DMA; -. DR PDBsum; 1IKP; -. DR PDBsum; 1IKQ; -. DR PDBsum; 1XK9; -. DR PDBsum; 1ZM2; -. DR PDBsum; 1ZM3; -. DR PDBsum; 1ZM4; -. DR PDBsum; 1ZM9; -. DR PDBsum; 2ZIT; -. DR PDBsum; 3B78; -. DR PDBsum; 3B82; -. DR PDBsum; 3B8H; -. DR AlphaFoldDB; P11439; -. DR SMR; P11439; -. DR STRING; 208964.PA1148; -. DR DrugBank; DB02701; Nicotinamide. DR DrugBank; DB08348; N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE. DR TCDB; 1.C.73.1.1; the pseudomonas exotoxin a (p-exoa) family. DR PaxDb; 208964-PA1148; -. DR ABCD; P11439; 2 sequenced antibodies. DR GeneID; 877850; -. DR KEGG; pae:PA1148; -. DR PATRIC; fig|208964.12.peg.1194; -. DR PseudoCAP; PA1148; -. DR HOGENOM; CLU_426954_0_0_6; -. DR InParanoid; P11439; -. DR OrthoDB; 6479700at2; -. DR BioCyc; MetaCyc:MONOMER-15587; -. DR BioCyc; PAER208964:G1FZ6-1174-MONOMER; -. DR BRENDA; 2.4.2.36; 5087. DR SABIO-RK; P11439; -. DR EvolutionaryTrace; P11439; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0047286; F:NAD+-diphthamide ADP-ribosyltransferase activity; IDA:CACAO. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR CDD; cd01436; Dipth_tox_like; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 3.90.175.10; Diphtheria Toxin, domain 1; 1. DR Gene3D; 3.90.1350.10; Exotoxin A, middle domain; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR015185; Exotox-A_bind. DR InterPro; IPR015099; Exotox-A_cataly_dom. DR InterPro; IPR015186; Exotox-A_middle_dom. DR InterPro; IPR036478; Exotox-A_middle_dom_sf. DR Pfam; PF09101; Exotox-A_bind; 1. DR Pfam; PF09009; Exotox-A_cataly; 1. DR Pfam; PF09102; Exotox-A_target; 1. DR SUPFAM; SSF56399; ADP-ribosylation; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF56864; Exotoxin A, middle domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; KW Glycosyltransferase; NAD; Nucleotidyltransferase; Reference proteome; KW Signal; Toxin; Transferase; Virulence. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:6201861" FT CHAIN 26..638 FT /note="Exotoxin A" FT /id="PRO_0000019365" FT REGION 26..277 FT /note="Domain Ia (required for target cell recognition)" FT /evidence="ECO:0000305|PubMed:2118903" FT REGION 278..389 FT /note="II (required for translocation in target cell FT cytoplasm)" FT REGION 390..429 FT /note="Domain Ib" FT REGION 430..638 FT /note="III (required for ADP-ribosyl activity)" FT REGION 596..638 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 578 FT /evidence="ECO:0000269|PubMed:2885323" FT BINDING 465..467 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:18583986" FT BINDING 474 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:18583986" FT BINDING 479..485 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:18583986" FT BINDING 578 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:18583986" FT DISULFID 290..312 FT /evidence="ECO:0000269|PubMed:10600112" FT MUTAGEN 82 FT /note="K->E: Loss of toxicity, no binding to LRP1 receptor. FT 100-fold less cytotoxic, 5-fold less toxic in mice." FT /evidence="ECO:0000269|PubMed:1618748, FT ECO:0000269|PubMed:2118903" FT MUTAGEN 266..275 FT /note="Missing: Loss of cytotoxicity; when associated with FT E-82." FT /evidence="ECO:0000269|PubMed:2118903" FT MUTAGEN 271..274 FT /note="HRLH->EELE: Slight decrease in cytotoxicity. Loss of FT cytotoxicity, 150-fold less toxic in mice; when associated FT with E-82." FT /evidence="ECO:0000269|PubMed:2118903" FT MUTAGEN 271..274 FT /note="HRLH->GGLG: Loss of cytotoxicity; when associated FT with E-82." FT /evidence="ECO:0000269|PubMed:2118903" FT MUTAGEN 271..274 FT /note="HRLH->KKLK: 100-fold reduction of cytotoxicity; when FT associated with E-82." FT /evidence="ECO:0000269|PubMed:2118903" FT MUTAGEN 481 FT /note="R->H: 52-fold decrease in ADPRT activity, 55-fold FT reduction in GH activity, 31-fold increase in dissociation FT constant for NAD(+)." FT /evidence="ECO:0000269|PubMed:18583986" FT MUTAGEN 571 FT /note="E->A: 833-fold decrease in ADPRT activity, 4-fold FT reduction in GH activity, 2-fold increase in dissociation FT constant for NAD(+)." FT /evidence="ECO:0000269|PubMed:18583986" FT MUTAGEN 576 FT /note="R->A: 2-fold decrease in ADPRT activity, 14-fold FT reduction in GH activity, 3-fold increase in dissociation FT constant for NAD(+)." FT /evidence="ECO:0000269|PubMed:18583986" FT MUTAGEN 578 FT /note="E->A: 666-fold decrease in ADPRT activity, 14-fold FT reduction in GH activity, 2-fold increase in dissociation FT constant for NAD(+), loss of toxicity against mouse cells." FT /evidence="ECO:0000269|PubMed:18276581, FT ECO:0000269|PubMed:18583986" FT CONFLICT 4 FT /note="T -> I (in Ref. 1; AAB59097)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="F -> S (in Ref. 1; AAB59097)" FT /evidence="ECO:0000305" FT CONFLICT 204 FT /note="A -> T (in Ref. 1; AAB59097)" FT /evidence="ECO:0000305" FT CONFLICT 389 FT /note="S -> N (in Ref. 1; AAB59097)" FT /evidence="ECO:0000305" FT CONFLICT 432 FT /note="I -> V (in Ref. 1; AAB59097)" FT /evidence="ECO:0000305" FT CONFLICT 540 FT /note="G -> S (in Ref. 1; AAB59097)" FT /evidence="ECO:0000305" FT HELIX 32..35 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 49..54 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 63..74 FT /evidence="ECO:0007829|PDB:1IKP" FT TURN 76..79 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:1IKP" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 95..102 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 122..131 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 136..145 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 151..154 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 164..170 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 173..180 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 189..201 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 218..223 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 230..235 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 249..255 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 280..290 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 294..298 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 307..311 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 313..325 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 333..342 FT /evidence="ECO:0007829|PDB:1IKP" FT TURN 344..347 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 348..356 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 358..376 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 392..396 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 399..403 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 413..418 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 422..424 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:1DMA" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:1DMA" FT HELIX 444..456 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 459..467 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 469..477 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 489..491 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 493..499 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 500..504 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 522..529 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 530..535 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 536..538 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 543..545 FT /evidence="ECO:0007829|PDB:3B8H" FT HELIX 548..556 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 558..561 FT /evidence="ECO:0007829|PDB:1DMA" FT STRAND 566..572 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 577..581 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 583..587 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 590..593 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 609..611 FT /evidence="ECO:0007829|PDB:1IKP" FT HELIX 614..617 FT /evidence="ECO:0007829|PDB:1IKP" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:1IKP" SQ SEQUENCE 638 AA; 69284 MW; 7B9AAD56A27C700A CRC64; MHLTPHWIPL VASLGLLAGG SFASAAEEAF DLWNECAKAC VLDLKDGVRS SRMSVDPAIA DTNGQGVLHY SMVLEGGNDA LKLAIDNALS ITSDGLTIRL EGGVEPNKPV RYSYTRQARG SWSLNWLVPI GHEKPSNIKV FIHELNAGNQ LSHMSPIYTI EMGDELLAKL ARDATFFVRA HESNEMQPTL AISHAGVSVV MAQAQPRREK RWSEWASGKV LCLLDPLDGV YNYLAQQRCN LDDTWEGKIY RVLAGNPAKH DLDIKPTVIS HRLHFPEGGS LAALTAHQAC HLPLETFTRH RQPRGWEQLE QCGYPVQRLV ALYLAARLSW NQVDQVIRNA LASPGSGGDL GEAIREQPEQ ARLALTLAAA ESERFVRQGT GNDEAGAASA DVVSLTCPVA AGECAGPADS GDALLERNYP TGAEFLGDGG DISFSTRGTQ NWTVERLLQA HRQLEERGYV FVGYHGTFLE AAQSIVFGGV RARSQDLDAI WRGFYIAGDP ALAYGYAQDQ EPDARGRIRN GALLRVYVPR SSLPGFYRTG LTLAAPEAAG EVERLIGHPL PLRLDAITGP EEEGGRLETI LGWPLAERTV VIPSAIPTDP RNVGGDLDPS SIPDKEQAIS ALPDYASQPG KPPREDLK //