ID AMYP_PIG Reviewed; 511 AA. AC P00690; Q9TUE4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 3. DT 08-NOV-2023, entry version 182. DE RecName: Full=Pancreatic alpha-amylase; DE Short=PA; DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746}; DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase; DE Flags: Precursor; GN Name=AMY2; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pancreas; RX PubMed=10082956; DOI=10.1016/s0167-4838(99)00011-4; RA Darnis S., Juge N., Guo X.-J., Marchis-Mouren G., Puigserver A., RA Chaix J.-C.; RT "Molecular cloning and primary structure analysis of porcine pancreatic RT alpha-amylase."; RL Biochim. Biophys. Acta 1430:281-289(1999). RN [2] RP PROTEIN SEQUENCE OF 16-511, AND DISULFIDE BONDS. RX PubMed=3484639; DOI=10.1016/0167-4838(86)90289-x; RA Pasero L., Mazzei-Pierron Y., Abadie B., Chicheportiche Y., RA Marchis-Mouren G.; RT "Complete amino acid sequence and location of the five disulfide bridges in RT porcine pancreatic alpha-amylase."; RL Biochim. Biophys. Acta 869:147-157(1986). RN [3] RP DISULFIDE BONDS. RX PubMed=6188459; DOI=10.1016/0006-291x(83)91021-5; RA Pasero L., Mazzei Y., Abadie B., Moinier D., Fougereau M., RA Marchis-Mouren G.; RT "Localization of the two free thiol groups in the porcine pancreatic alpha- RT amylase I sequence."; RL Biochem. Biophys. Res. Commun. 110:726-732(1983). RN [4] RP SUBUNIT, AND INTERACTION WITH THE SEA ANEMONE INHIBITOR MAGNIFICAMIDE. RX PubMed=31546678; DOI=10.3390/md17100542; RA Sintsova O., Gladkikh I., Kalinovskii A., Zelepuga E., Monastyrnaya M., RA Kim N., Shevchenko L., Peigneur S., Tytgat J., Kozlovskaya E., RA Leychenko E.; RT "Magnificamide, a beta-defensin-like peptide from the mucus of the sea RT anemone Heteractis magnifica, is a strong inhibitor of mammalian alpha- RT amylases."; RL Mar. Drugs 17:0-0(2019). RN [5] RP X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS). RA Payan F., Haser R., Pierrot M., Frey M., Astier J.-P., Abadie B., Duee E., RA Buisson G.; RT "The three-dimensional structure of alpha-amylase from porcine pancreas at RT 5-A resolution -- the active-site location."; RL Acta Crystallogr. B 36:416-421(1980). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, AND DISULFIDE BONDS. RX PubMed=3502087; DOI=10.1002/j.1460-2075.1987.tb02731.x; RA Buisson G., Duee E., Haser R., Payan F.; RT "Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A RT resolution. Role of calcium in structure and activity."; RL EMBO J. 6:3909-3916(1987). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION. RX PubMed=8515451; DOI=10.1006/jmbi.1993.1326; RA Qian M., Haser R., Payan F.; RT "Structure and molecular model refinement of pig pancreatic alpha-amylase RT at 2.1-A resolution."; RL J. Mol. Biol. 231:785-799(1993). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM, RP DISULFIDE BONDS, AND COFACTOR. RX PubMed=8193143; DOI=10.1021/bi00186a031; RA Qian M., Haser R., Buisson G., Duee E., Payan F.; RT "The active center of a mammalian alpha-amylase. Structure of the complex RT of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2- RT A resolution."; RL Biochemistry 33:6284-6294(1994). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; RP CALCIUM AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR. RX PubMed=7897663; DOI=10.1006/jmbi.1994.0125; RA Wiegand G., Epp O., Huber R.; RT "The crystal structure of porcine pancreatic alpha-amylase in complex with RT the microbial inhibitor Tendamistat."; RL J. Mol. Biol. 247:99-110(1995). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; RP GLUCOSE AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR. RX PubMed=8757803; DOI=10.1006/jmbi.1996.0410; RA Machius M., Vertesy L., Huber R., Wiegand G.; RT "Carbohydrate and protein-based inhibitors of porcine pancreatic alpha- RT amylase: structure analysis and comparison of their binding RT characteristics."; RL J. Mol. Biol. 260:409-421(1996). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM, RP SEQUENCE REVISION, COFACTOR, AND DISULFIDE BONDS. RX PubMed=8681972; DOI=10.1111/j.1432-1033.1996.0561z.x; RA Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.; RT "Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex RT with the carbohydrate inhibitor acarbose."; RL Eur. J. Biochem. 238:561-569(1996). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH INHIBITOR RP AND CALCIUM, COFACTOR, AND DISULFIDE BONDS. RX PubMed=8994970; DOI=10.1016/s0969-2126(96)00151-7; RA Bompard-Gilles C., Rousseau P., Rouge P., Payan F.; RT "Substrate mimicry in the active center of a mammalian alpha-amylase: RT structural analysis of an enzyme-inhibitor complex."; RL Structure 4:1441-1452(1996). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM RP AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR. RX PubMed=9385631; DOI=10.1002/pro.5560061102; RA Qian M., Spinelli S., Driguez H., Payan F.; RT "Structure of a pancreatic alpha-amylase bound to a substrate analogue at RT 2.03-A resolution."; RL Protein Sci. 6:2285-2296(1997). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE RP AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, AND DISULFIDE BOND. RX PubMed=11412124; DOI=10.1021/bi0102050; RA Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.; RT "Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High- RT resolution structural analysis of an enzyme-inhibitor complex."; RL Biochemistry 40:7700-7709(2001). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM RP AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR. RX PubMed=11960990; DOI=10.1074/jbc.m202327200; RA Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., RA Cambillau C.; RT "Three camelid VHH domains in complex with porcine pancreatic alpha- RT amylase. Inhibition and versatility of binding topology."; RL J. Biol. Chem. 277:23645-23650(2002). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH THE SEA ANEMONE RP INHIBITOR HELIANTHAMIDE, SUBUNIT, AND INTERACTION WITH THE SEA ANEMONE RP INHIBITOR HELIANTHAMIDE. RX PubMed=27066537; DOI=10.1021/acscentsci.5b00399; RA Tysoe C., Williams L.K., Keyzers R., Nguyen N.T., Tarling C., Wicki J., RA Goddard-Borger E.D., Aguda A.H., Perry S., Foster L.J., Andersen R.J., RA Brayer G.D., Withers S.G.; RT "Potent human alpha-amylase inhibition by the beta-defensin-like protein RT helianthamide."; RL ACS Cent. Sci. 2:154-161(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in CC polysaccharides containing three or more (1->4)-alpha-linked D- CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, CC ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, CC ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, CC ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, CC ECO:0000269|PubMed:9385631}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11412124, CC ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, CC ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, CC ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, CC ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631}; CC -!- COFACTOR: CC Name=chloride; Xref=ChEBI:CHEBI:17996; CC Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, CC ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663, CC ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631}; CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11412124, CC ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087, CC ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, CC ECO:0000269|PubMed:9385631}; CC -!- SUBUNIT: Binds to the sea anemone inhibitor helianthamide and CC magnificamide. {ECO:0000269|PubMed:27066537, CC ECO:0000305|PubMed:31546678}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- MISCELLANEOUS: The two forms of this enzyme, I and II, show very CC similar activities, molecular masses, and compositions and differ only CC in their isoelectric points. As no evidence for two variants were in CC the cDNA library of PubMed:10082956, it is most likely that isoform I CC (PPAI) and isoform II (PPAII) are two forms of the same protein. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/AA/"; 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; AF064742; AAF02828.1; -; mRNA. DR PIR; A25412; ALPGP. DR RefSeq; NP_999360.1; NM_214195.1. DR PDB; 1BVN; X-ray; 2.50 A; P=16-511. DR PDB; 1DHK; X-ray; 1.85 A; A=17-511. DR PDB; 1HX0; X-ray; 1.38 A; A=16-511. DR PDB; 1JFH; X-ray; 2.03 A; A=17-511. DR PDB; 1KXQ; X-ray; 1.60 A; A/B/C/D=16-511. DR PDB; 1KXT; X-ray; 2.00 A; A/C/E=16-511. DR PDB; 1KXV; X-ray; 1.60 A; A/B=16-511. DR PDB; 1OSE; X-ray; 2.30 A; A=17-511. DR PDB; 1PIF; X-ray; 2.30 A; A=17-511. DR PDB; 1PIG; X-ray; 2.20 A; A=17-511. DR PDB; 1PPI; X-ray; 2.20 A; A=16-511. DR PDB; 1UA3; X-ray; 2.01 A; A=16-511. DR PDB; 1VAH; X-ray; 2.40 A; A=16-511. DR PDB; 1WO2; X-ray; 2.01 A; A=16-511. DR PDB; 3L2L; X-ray; 2.11 A; A=16-511. DR PDB; 3L2M; X-ray; 1.97 A; A=16-511. DR PDB; 4X0N; X-ray; 2.60 A; A=17-511. DR PDBsum; 1BVN; -. DR PDBsum; 1DHK; -. DR PDBsum; 1HX0; -. DR PDBsum; 1JFH; -. DR PDBsum; 1KXQ; -. DR PDBsum; 1KXT; -. DR PDBsum; 1KXV; -. DR PDBsum; 1OSE; -. DR PDBsum; 1PIF; -. DR PDBsum; 1PIG; -. DR PDBsum; 1PPI; -. DR PDBsum; 1UA3; -. DR PDBsum; 1VAH; -. DR PDBsum; 1WO2; -. DR PDBsum; 3L2L; -. DR PDBsum; 3L2M; -. DR PDBsum; 4X0N; -. DR AlphaFoldDB; P00690; -. DR SMR; P00690; -. DR MINT; P00690; -. DR STRING; 9823.ENSSSCP00000007308; -. DR BindingDB; P00690; -. DR ChEMBL; CHEMBL5730; -. DR DrugCentral; P00690; -. DR Allergome; 970; Sus s Amylase. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GlyCosmos; P00690; 1 site, No reported glycans. DR PaxDb; 9823-ENSSSCP00000007308; -. DR PeptideAtlas; P00690; -. DR ABCD; P00690; 3 sequenced antibodies. DR GeneID; 397397; -. DR KEGG; ssc:397397; -. DR CTD; 397397; -. DR eggNOG; KOG2212; Eukaryota. DR InParanoid; P00690; -. DR OrthoDB; 3249969at2759; -. DR BRENDA; 3.2.1.1; 6170. DR SABIO-RK; P00690; -. DR EvolutionaryTrace; P00690; -. DR PRO; PR:P00690; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB. DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Chloride; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..15 FT /evidence="ECO:0000269|PubMed:3484639" FT CHAIN 16..511 FT /note="Pancreatic alpha-amylase" FT /id="PRO_0000001399" FT ACT_SITE 212 FT /note="Nucleophile" FT ACT_SITE 248 FT /note="Proton donor" FT BINDING 115 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631" FT BINDING 173 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631" FT BINDING 210 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631" FT BINDING 313 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000305" FT BINDING 352 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631" FT SITE 315 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P04746" FT MOD_RES 16 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P04746" FT CARBOHYD 427 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 43..101 FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087" FT DISULFID 85..130 FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087" FT DISULFID 156..175 FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087" FT DISULFID 393..399 FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087" FT DISULFID 465..477 FT /evidence="ECO:0000269|PubMed:11412124, FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087" FT CONFLICT 138 FT /note="N -> S (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="Q -> E (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 405 FT /note="Q -> E (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 419 FT /note="Q -> E (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 426 FT /note="A -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 27..31 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 36..45 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 46..51 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 73..77 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1PIF" FT HELIX 91..103 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:1KXQ" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 158..162 FT /evidence="ECO:0007829|PDB:1KXV" FT HELIX 169..174 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 188..204 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 219..226 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 253..257 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 272..281 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 289..294 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:1KXQ" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 333..345 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 348..355 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 363..366 FT /evidence="ECO:0007829|PDB:3L2M" FT TURN 369..372 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 404..415 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 416..418 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 421..426 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 428..436 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 437..439 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 440..445 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 451..456 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:1HX0" FT TURN 467..469 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 476..479 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 481..484 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 488..494 FT /evidence="ECO:0007829|PDB:1HX0" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:1KXQ" FT STRAND 502..506 FT /evidence="ECO:0007829|PDB:1HX0" FT HELIX 507..509 FT /evidence="ECO:0007829|PDB:1HX0" SQ SEQUENCE 511 AA; 57086 MW; 117489E020807378 CRC64; MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK GFGGVQVSPP NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR CNNVGVRIYV DAVINHMCGS GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD FNDGKCKTAS GGIESYNDPY QVRDCQLVGL LDLALEKDYV RSMIADYLNK LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG SRPFIFQEVI DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF TRVMSSYRWA RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE HRWRQIRNMV WFRNVVDGQP FANWWANGSN QVAFGRGNRG FIVFNNDDWQ LSSTLQTGLP GGTYCDVISG DKVGNSCTGI KVYVSSDGTA QFSISNSAED PFIAIHAESK L //