ID ACES_TORCA Reviewed; 586 AA. AC P04058; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 16-JUN-2009, entry version 106. DE RecName: Full=Acetylcholinesterase; DE Short=AChE; DE EC=3.1.1.7; DE Flags: Precursor; GN Name=ache; OS Torpedo californica (Pacific electric ray). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea; OC Torpediniformes; Torpedinoidei; Torpedinidae; Torpedo. OX NCBI_TaxID=7787; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-586. RX MEDLINE=86118676; PubMed=3753747; DOI=10.1038/319407a0; RA Schumacher M., Camp S., Maulet Y., Newton M., McPhee-Quigley K., RA Taylor S.S., Friedmann T., Taylor P.; RT "Primary structure of Torpedo californica acetylcholinesterase deduced RT from its cDNA sequence."; RL Nature 319:407-409(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. RX MEDLINE=89066695; PubMed=3198606; RA Schumacher M.; RT "Multiple messenger RNA species give rise to the structural diversity RT in acetylcholinesterase."; RL J. Biol. Chem. 263:18979-18987(1988). RN [3] RP PROTEIN SEQUENCE OF 22-45 AND 214-237. RX MEDLINE=86008285; PubMed=3900071; RA MacPhee-Quigley K., Taylor P., Taylor S.; RT "Primary structures of the catalytic subunits from two molecular forms RT of acetylcholinesterase. A comparison of NH2-terminal and active RT center sequences."; RL J. Biol. Chem. 260:12185-12189(1985). RN [4] RP PROTEIN SEQUENCE OF 100-108. RX MEDLINE=91296772; PubMed=2068091; DOI=10.1073/pnas.88.14.6117; RA Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.; RT "Anionic subsites of the catalytic center of acetylcholinesterase from RT Torpedo and from cobra venom."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991). RN [5] RP PROTEIN SEQUENCE OF 552-558. RX MEDLINE=88087239; PubMed=3335534; RA Gibney G., Macphee-Quigley K., Thompson B., Vedvick T., Low M.G., RA Taylor S.S., Taylor P.; RT "Divergence in primary structure between the molecular forms of RT acetylcholinesterase."; RL J. Biol. Chem. 263:1140-1145(1988). RN [6] RP ALTERNATIVE SPLICING. RX MEDLINE=90166618; PubMed=2306366; DOI=10.1016/0896-6273(90)90103-M; RA Maulet Y., Camp S., Gibney G., Rachinsky T.L., Ekstroem T.J., RA Taylor P.; RT "Single gene encodes glycophospholipid-anchored and asymmetric RT acetylcholinesterase forms: alternative coding exons contain inverted RT repeat sequences."; RL Neuron 4:289-301(1990). RN [7] RP DISULFIDE BONDS. RX MEDLINE=87008586; PubMed=3759980; RA McPhee-Quigley K., Vedvick T.S., Taylor P., Taylor S.S.; RT "Profile of the disulfide bonds in acetylcholinesterase."; RL J. Biol. Chem. 261:13565-13570(1986). RN [8] RP STRUCTURE OF THE GPI-ANCHOR. RX MEDLINE=94079692; PubMed=8257440; RA Mehlert A., Varon L., Silman I., Homans S.W., Ferguson M.A.; RT "Structure of the glycosyl-phosphatidylinositol membrane anchor of RT acetylcholinesterase from the electric organ of the electric-fish, RT Torpedo californica."; RL Biochem. J. 296:473-479(1993). RN [9] RP GPI-ANCHOR AT SER-564. RX MEDLINE=96176849; PubMed=8597567; DOI=10.1016/0167-4838(95)00205-7; RA Bucht G., Hjalmarsson K.; RT "Residues in Torpedo californica acetylcholinesterase necessary for RT processing to a glycosyl phosphatidylinositol-anchored form."; RL Biochim. Biophys. Acta 1292:223-232(1996). RN [10] RP MUTAGENESIS. RX MEDLINE=91017542; PubMed=2217185; DOI=10.1073/pnas.87.19.7546; RA Gibney G., Camp S., Dionne M., McPhee-Quigley K., Taylor P.; RT "Mutagenesis of essential functional residues in RT acetylcholinesterase."; RL Proc. Natl. Acad. Sci. U.S.A. 87:7546-7550(1990). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-558, ACTIVE SITE, RP GLYCOSYLATION AT ASN-437, DISULFIDE BONDS, AND SUBUNIT. RX MEDLINE=91343928; PubMed=1678899; DOI=10.1126/science.1678899; RA Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., RA Silman I.; RT "Atomic structure of acetylcholinesterase from Torpedo californica: a RT prototypic acetylcholine-binding protein."; RL Science 253:872-879(1991). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-556 IN COMPLEX WITH RP SUBSTRATE ANALOGS. RX PubMed=8415649; DOI=10.1073/pnas.90.19.9031; RA Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., RA Hirth C., Axelsen P.H., Silman I., Sussman J.L.; RT "Quaternary ligand binding to aromatic residues in the active-site RT gorge of acetylcholinesterase."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-558 IN COMPLEX WITH RP FASCICULIN. RX MEDLINE=96363673; PubMed=8747462; DOI=10.1016/S0969-2126(01)00273-8; RA Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L.; RT "Crystal structure of an acetylcholinesterase-fasciculin complex: RT interaction of a three-fingered toxin from snake venom with its RT target."; RL Structure 3:1355-1366(1995). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-558 IN COMPLEX WITH THE RP INHIBITOR HUPERZINE A. RX MEDLINE=97143314; PubMed=8989325; DOI=10.1038/nsb0197-57; RA Raves M.L., Harel M., Pang Y.P., Silman I., Kozikowski A.P., RA Sussman J.L.; RT "Structure of acetylcholinesterase complexed with the nootropic RT alkaloid, (-)-huperzine A."; RL Nat. Struct. Biol. 4:57-63(1997). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-558. RX MEDLINE=99249780; PubMed=10231521; DOI=10.1021/bi982723p; RA Bartolucci C., Perola E., Cellai L., Brufani M., Lamba D.; RT "'Back door' opening implied by the crystal structure of a RT carbamoylated acetylcholinesterase."; RL Biochemistry 38:5714-5719(1999). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-558. RX MEDLINE=99282167; PubMed=10353814; DOI=10.1021/bi982678l; RA Millard C.B., Kryger G., Ordentlich A., Greenblatt H.M., Harel M., RA Raves M.L., Segall Y., Barak D., Shafferman A., Silman I., RA Sussman J.L.; RT "Crystal structures of aged phosphonylated acetylcholinesterase: nerve RT agent reaction products at the atomic level."; RL Biochemistry 38:7032-7039(1999). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-564 IN COMPLEX WITH RP GALANTHAMINE. RX MEDLINE=20074924; PubMed=10606746; DOI=10.1016/S0014-5793(99)01637-3; RA Greenblatt H.M., Kryger G., Lewis T., Silman I., Sussman J.L.; RT "Structure of acetylcholinesterase complexed with (-)-galanthamine at RT 2.3-A resolution."; RL FEBS Lett. 463:321-326(1999). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE RP SYNTHETIC INHIBITOR ARICEPT, AND GLYCOSYLATION AT ASN-80; ASN-437; RP ASN-478 AND ASN-554. RX MEDLINE=99197295; PubMed=10368299; DOI=10.1016/S0969-2126(99)80040-9; RA Kryger G., Silman I., Sussman J.L.; RT "Structure of acetylcholinesterase complexed with E2020 (Aricept(R)): RT implications for the design of new anti-Alzheimer drugs."; RL Structure 7:297-307(1999). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE RP SYNTHETIC INHIBITOR HUPRINE. RX PubMed=11863435; DOI=10.1021/bi011652i; RA Dvir H., Wong D.M., Harel M., Barril X., Orozco M., Luque F.J., RA Munoz-Torrero D., Camps P., Rosenberry T.L., Silman I., Sussman J.L.; RT "3D structure of Torpedo californica acetylcholinesterase complexed RT with huprine X at 2.1 A resolution: kinetic and molecular dynamic RT correlates."; RL Biochemistry 41:2970-2981(2002). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-556 IN COMPLEX WITH THE RP SYNTHETIC INHIBITOR RIVASTIGMINE. RX PubMed=11888271; DOI=10.1021/bi020016x; RA Bar-On P., Millard C.B., Harel M., Dvir H., Enz A., Sussman J.L., RA Silman I.; RT "Kinetic and structural studies on the interaction of cholinesterases RT with the anti-Alzheimer drug rivastigmine."; RL Biochemistry 41:3555-3564(2002). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE RP SYNTHETIC INHIBITOR CPT-11. RX PubMed=15772291; DOI=10.1124/mol.104.009944; RA Harel M., Hyatt J.L., Brumshtein B., Morton C.L., Yoon K.J., RA Wadkins R.M., Silman I., Sussman J.L., Potter P.M.; RT "The crystal structure of the complex of the anticancer prodrug 7- RT ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT- RT 11) with Torpedo californica acetylcholinesterase provides a molecular RT explanation for its cholinergic action."; RL Mol. Pharmacol. 67:1874-1881(2005). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-558 IN COMPLEXES WITH RP SUBSTRATE AND SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-80 AND ASN-437, RP ACTIVE SITE, AND ENZYME REGULATION. RX PubMed=16763558; DOI=10.1038/sj.emboj.7601175; RA Colletier J.-P., Fournier D., Greenblatt H.M., Stojan J., RA Sussman J.L., Zaccai G., Silman I., Weik M.; RT "Structural insights into substrate traffic and inhibition in RT acetylcholinesterase."; RL EMBO J. 25:2746-2756(2006). CC -!- FUNCTION: Terminates signal transduction at the neuromuscular CC junction by rapid hydrolysis of the acetylcholine released into CC the synaptic cleft. May be involved in cell-cell interactions. CC -!- CATALYTIC ACTIVITY: Acetylcholine + H(2)O = choline + acetate. CC -!- ENZYME REGULATION: Inhibited by substrate concentrations above 0.5 CC mM. CC -!- SUBUNIT: Isoform H form is an homodimer; the asymmetric form is a CC disulfide-bonded oligomer composed of a collagenic subunit (Q) and CC a variable number of T catalytic subunits. CC -!- SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI- CC anchor. Cell junction, synapse. CC -!- SUBCELLULAR LOCATION: Isoform T: Cell membrane; Peripheral CC membrane protein. Cell junction, synapse. Note=Attached to the CC membrane through disulfide linkage with the collagenic subunit, CC itself bound to the membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=H; Synonyms=Globular; CC IsoId=P04058-1; Sequence=Displayed; CC Note=GPI-anchored form; CC Name=T; CC IsoId=P04058-2; Sequence=VSP_001460; CC -!- TISSUE SPECIFICITY: Found in the synapses and to a lower extent in CC extrajunctional areas of muscle and nerve, and on erythrocyte CC membranes. CC -!- PTM: An interchain disulfide bond is present in what becomes CC position 593 of the T isoform. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03439; CAA27169.1; -; mRNA. DR EMBL; X56516; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X56517; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A00773; ACRYE. DR PDB; 1ACJ; X-ray; 2.80 A; A=22-556. DR PDB; 1ACL; X-ray; 2.80 A; A=22-556. DR PDB; 1AMN; X-ray; 2.80 A; A=22-558. DR PDB; 1AX9; X-ray; 2.80 A; A=22-558. DR PDB; 1CFJ; X-ray; 2.60 A; A=22-558. DR PDB; 1DX6; X-ray; 2.30 A; A=22-564. DR PDB; 1E3Q; X-ray; 2.85 A; A=22-564. DR PDB; 1E66; X-ray; 2.10 A; A=22-564. DR PDB; 1EA5; X-ray; 1.80 A; A=22-558. DR PDB; 1EEA; X-ray; 4.50 A; A=22-555. DR PDB; 1EVE; X-ray; 2.50 A; A=22-564. DR PDB; 1FSS; X-ray; 3.00 A; A=22-558. DR PDB; 1GPK; X-ray; 2.10 A; A=22-558. DR PDB; 1GPN; X-ray; 2.35 A; A=22-558. DR PDB; 1GQR; X-ray; 2.20 A; A=25-556. DR PDB; 1GQS; X-ray; 3.00 A; A=25-556. DR PDB; 1H22; X-ray; 2.15 A; A=22-564. DR PDB; 1H23; X-ray; 2.15 A; A=22-564. DR PDB; 1HBJ; X-ray; 2.50 A; A=22-564. DR PDB; 1JGA; Model; -; A=1-586. DR PDB; 1JGB; Model; -; A=1-586. DR PDB; 1JJB; X-ray; 2.30 A; A=25-556. DR PDB; 1OCE; X-ray; 2.70 A; A=22-558. DR PDB; 1ODC; X-ray; 2.20 A; A=22-564. DR PDB; 1QID; X-ray; 2.05 A; A=22-558. DR PDB; 1QIE; X-ray; 2.10 A; A=22-558. DR PDB; 1QIF; X-ray; 2.10 A; A=22-558. DR PDB; 1QIG; X-ray; 2.30 A; A=22-558. DR PDB; 1QIH; X-ray; 2.50 A; A=22-558. DR PDB; 1QII; X-ray; 2.65 A; A=22-558. DR PDB; 1QIJ; X-ray; 2.80 A; A=22-558. DR PDB; 1QIK; X-ray; 2.90 A; A=22-558. DR PDB; 1QIM; X-ray; 3.00 A; A=22-558. DR PDB; 1QTI; X-ray; 2.50 A; A=22-537. DR PDB; 1SOM; X-ray; 2.20 A; A=22-564. DR PDB; 1U65; X-ray; 2.61 A; A=22-564. DR PDB; 1UT6; X-ray; 2.40 A; A=22-556. DR PDB; 1VOT; X-ray; 2.50 A; A=22-558. DR PDB; 1VXO; X-ray; 2.40 A; A=22-558. DR PDB; 1VXR; X-ray; 2.20 A; A=22-558. DR PDB; 1W4L; X-ray; 2.16 A; A=22-564. DR PDB; 1W6R; X-ray; 2.05 A; A=22-564. DR PDB; 1W75; X-ray; 2.40 A; A/B=22-564. DR PDB; 1W76; X-ray; 2.30 A; A/B=22-564. DR PDB; 1ZGB; X-ray; 2.30 A; A=22-564. DR PDB; 1ZGC; X-ray; 2.10 A; A/B=22-564. DR PDB; 2ACE; X-ray; 2.50 A; A=22-558. DR PDB; 2ACK; X-ray; 2.40 A; A=22-558. DR PDB; 2BAG; X-ray; 2.40 A; A=22-564. DR PDB; 2C4H; X-ray; 2.15 A; A=22-558. DR PDB; 2C58; X-ray; 2.30 A; A=22-558. DR PDB; 2C5F; X-ray; 2.60 A; A=22-558. DR PDB; 2C5G; X-ray; 1.95 A; A=22-558. DR PDB; 2CEK; X-ray; 2.20 A; A=22-556. DR PDB; 2CKM; X-ray; 2.15 A; A=22-564. DR PDB; 2CMF; X-ray; 2.50 A; A=22-564. DR PDB; 2DFP; X-ray; 2.30 A; A=23-556. DR PDB; 2J3D; X-ray; 2.60 A; A=22-564. DR PDB; 2J3Q; X-ray; 2.80 A; A=22-564. DR PDB; 2J4F; X-ray; 2.80 A; A=22-564. DR PDB; 2V96; X-ray; 2.40 A; A/B=22-558. DR PDB; 2V97; X-ray; 2.40 A; A/B=22-558. DR PDB; 2V98; X-ray; 3.00 A; A/B=22-558. DR PDB; 2VA9; X-ray; 2.40 A; A/B=22-558. DR PDB; 2VJA; X-ray; 2.30 A; A/B=22-558. DR PDB; 2VJB; X-ray; 2.39 A; A/B=22-558. DR PDB; 2VJC; X-ray; 2.20 A; A/B=22-558. DR PDB; 2VJD; X-ray; 2.30 A; A/B=22-558. DR PDB; 2VQ6; X-ray; 2.71 A; A=22-564. DR PDB; 2VT6; X-ray; 2.40 A; A/B=22-558. DR PDB; 2VT7; X-ray; 2.20 A; A/B=22-558. DR PDB; 2W6C; X-ray; 2.69 A; X=1-586. DR PDB; 3ACE; Model; -; A=22-558. DR PDB; 4ACE; Model; -; A=22-558. DR PDBsum; 1ACJ; -. DR PDBsum; 1ACL; -. DR PDBsum; 1AMN; -. DR PDBsum; 1AX9; -. DR PDBsum; 1CFJ; -. DR PDBsum; 1DX6; -. DR PDBsum; 1E3Q; -. DR PDBsum; 1E66; -. DR PDBsum; 1EA5; -. DR PDBsum; 1EEA; -. DR PDBsum; 1EVE; -. DR PDBsum; 1FSS; -. DR PDBsum; 1GPK; -. DR PDBsum; 1GPN; -. DR PDBsum; 1GQR; -. DR PDBsum; 1GQS; -. DR PDBsum; 1H22; -. DR PDBsum; 1H23; -. DR PDBsum; 1HBJ; -. DR PDBsum; 1JGA; -. DR PDBsum; 1JGB; -. DR PDBsum; 1JJB; -. DR PDBsum; 1OCE; -. DR PDBsum; 1ODC; -. DR PDBsum; 1QID; -. DR PDBsum; 1QIE; -. DR PDBsum; 1QIF; -. DR PDBsum; 1QIG; -. DR PDBsum; 1QIH; -. DR PDBsum; 1QII; -. DR PDBsum; 1QIJ; -. DR PDBsum; 1QIK; -. DR PDBsum; 1QIM; -. DR PDBsum; 1QTI; -. DR PDBsum; 1SOM; -. DR PDBsum; 1U65; -. DR PDBsum; 1UT6; -. DR PDBsum; 1VOT; -. DR PDBsum; 1VXO; -. DR PDBsum; 1VXR; -. DR PDBsum; 1W4L; -. DR PDBsum; 1W6R; -. DR PDBsum; 1W75; -. DR PDBsum; 1W76; -. DR PDBsum; 1ZGB; -. DR PDBsum; 1ZGC; -. DR PDBsum; 2ACE; -. DR PDBsum; 2ACK; -. DR PDBsum; 2BAG; -. DR PDBsum; 2C4H; -. DR PDBsum; 2C58; -. DR PDBsum; 2C5F; -. DR PDBsum; 2C5G; -. DR PDBsum; 2CEK; -. DR PDBsum; 2CKM; -. DR PDBsum; 2CMF; -. DR PDBsum; 2DFP; -. DR PDBsum; 2J3D; -. DR PDBsum; 2J3Q; -. DR PDBsum; 2J4F; -. DR PDBsum; 2V96; -. DR PDBsum; 2V97; -. DR PDBsum; 2V98; -. DR PDBsum; 2VA9; -. DR PDBsum; 2VJA; -. DR PDBsum; 2VJB; -. DR PDBsum; 2VJC; -. DR PDBsum; 2VJD; -. DR PDBsum; 2VQ6; -. DR PDBsum; 2VT6; -. DR PDBsum; 2VT7; -. DR PDBsum; 2W6C; -. DR PDBsum; 3ACE; -. DR PDBsum; 4ACE; -. DR MEROPS; S09.979; -. DR HOVERGEN; P04058; -. DR BRENDA; 3.1.1.7; 74507. DR DrugBank; DB00674; Galantamine. DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0003990; F:acetylcholinesterase activity; IEA:EC. DR GO; GO:0004104; F:cholinesterase activity; IEA:InterPro. DR GO; GO:0001507; P:acetylcholine catabolic process in synaptic...; IEA:InterPro. DR InterPro; IPR000908; Acylcholinesterase_fish/snake. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019826; Carboxylesterase_B_AS. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR000997; Cholinesterase. DR PANTHER; PTHR11559; CarbesteraseB; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR00879; ACHEFISH. DR PRINTS; PR00878; CHOLNESTRASE. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; KW Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; KW Serine esterase; Signal; Synapse. FT SIGNAL 1 21 FT CHAIN 22 564 Acetylcholinesterase. FT /FTId=PRO_0000008595. FT PROPEP 565 586 Removed in mature form. FT /FTId=PRO_0000008596. FT ACT_SITE 221 221 Acyl-ester intermediate. FT ACT_SITE 348 348 Charge relay system. FT ACT_SITE 461 461 Charge relay system. FT LIPID 564 564 GPI-anchor amidated serine. FT CARBOHYD 80 80 N-linked (GlcNAc...). FT CARBOHYD 437 437 N-linked (GlcNAc...). FT CARBOHYD 478 478 N-linked (GlcNAc...). FT CARBOHYD 554 554 N-linked (GlcNAc...). FT DISULFID 88 115 FT DISULFID 275 286 FT DISULFID 423 542 FT DISULFID 558 558 Interchain. FT VAR_SEQ 557 586 ACDGELSSSGTSSSKGIIFYVLFSILYLIF -> ETIDEAE FT RQWKTEFHRWSSYMMHWKNQFDHYSRHESCAEL (in FT isoform T). FT /FTId=VSP_001460. FT MUTAGEN 220 220 E->H: Loss of activity. FT MUTAGEN 220 220 E->Q,D: Decrease in activity. FT MUTAGEN 221 221 S->C: Loss of activity. FT MUTAGEN 221 221 S->V: Loss of activity. FT MUTAGEN 446 446 H->Q: Almost no loss of activity. FT MUTAGEN 461 461 H->Q: Loss of activity. FT STRAND 28 31 FT STRAND 34 37 FT STRAND 39 43 FT STRAND 46 55 FT HELIX 62 64 FT STRAND 76 80 FT HELIX 100 103 FT STRAND 117 122 FT STRAND 128 136 FT TURN 140 142 FT HELIX 149 151 FT HELIX 154 160 FT STRAND 163 166 FT HELIX 172 176 FT STRAND 183 185 FT HELIX 189 204 FT HELIX 205 208 FT STRAND 210 220 FT HELIX 222 232 FT TURN 234 236 FT HELIX 237 239 FT STRAND 241 247 FT HELIX 259 272 FT HELIX 280 289 FT HELIX 292 296 FT HELIX 297 302 FT STRAND 304 306 FT STRAND 319 324 FT HELIX 326 332 FT STRAND 340 345 FT HELIX 350 356 FT HELIX 370 380 FT HELIX 386 396 FT HELIX 405 420 FT HELIX 422 435 FT STRAND 439 444 FT HELIX 455 457 FT TURN 461 464 FT HELIX 465 468 FT HELIX 471 473 FT HELIX 475 477 FT HELIX 481 500 FT TURN 518 520 FT STRAND 522 529 FT STRAND 533 536 FT HELIX 539 546 FT HELIX 548 555 SQ SEQUENCE 586 AA; 65906 MW; 731D5F0F3ABA62A8 CRC64; MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA FLGIPFAEPP VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS GSEMWNPNRE MSEDCLYLNI WVPSPRPKST TVMVWIYGGG FYSGSSTLDV YNGKYLAYTE EVVLVSLSYR VGAFGFLALH GSQEAPGNVG LLDQRMALQW VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF RRAILQSGSP NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS FFLLYGAPGF SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM DDNNGIKNRD GLDDIVGDHN VICPLMHFVN KYTKFGNGTY LYFFNHRASN LVWPEWMGVI HGYEIEFVFG LPLVKELNYT AEEEALSRRI MHYWATFAKT GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ MCVFWNQFLP KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF //