ID ADA_BOVIN Reviewed; 363 AA. AC P56658; Q9MYY1; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 152. DE RecName: Full=Adenosine deaminase; DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P00813}; DE AltName: Full=Adenosine aminohydrolase; GN Name=ADA; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11067872; DOI=10.1084/jem.192.9.1223; RA Richard E., Arredondo-Vega F.X., Santisteban I., Kelly S.J., Patel D.D., RA Hershfield M.S.; RT "The binding site of human adenosine deaminase for CD26/dipeptidyl RT peptidase IV: the Arg142Gln mutation impairs binding to CD26 but does not RT cause immune deficiency."; RL J. Exp. Med. 192:1223-1236(2000). RN [2] RP PROTEIN SEQUENCE OF 2-357, AND MASS SPECTROMETRY. RX PubMed=8877857; DOI=10.1016/0731-7085(96)01845-6; RA Kelly M.A., Vestling M.M., Murphy C.M., Hua S., Sumpter T., Fenselau C.; RT "Primary structure of bovine adenosine deaminase."; RL J. Pharm. Biomed. Anal. 14:1513-1519(1996). RN [3] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=23240012; DOI=10.1371/journal.pone.0051287; RA Casanova V., Naval-Macabuhay I., Massanella M., Rodriguez-Garcia M., RA Blanco J., Gatell J.M., Garcia F., Gallart T., Lluis C., Mallol J., RA Franco R., Climent N., McCormick P.J.; RT "Adenosine deaminase enhances the immunogenicity of human dendritic cells RT from healthy and HIV-infected individuals."; RL PLoS ONE 7:E51287-E51287(2012). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-356 IN COMPLEX WITH ZINC IONS RP AND TRANSITION STATE ANALOG 6-HYDROXY-1,6-DIHYDROPURINE RIBOSIDE. RX PubMed=12554940; DOI=10.1107/s090744490202190x; RA Kinoshita T., Nishio N., Nakanishi I., Sato A., Fujii T.; RT "Structure of bovine adenosine deaminase complexed with 6-hydroxy-1,6- RT dihydropurine riboside."; RL Acta Crystallogr. D 59:299-303(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR RP AND ZINC IONS. RX PubMed=14709046; DOI=10.1021/ja038606l; RA Terasaka T., Kinoshita T., Kuno M., Nakanishi I.; RT "A highly potent non-nucleoside adenosine deaminase inhibitor: efficient RT drug discovery by intentional lead hybridization."; RL J. Am. Chem. Soc. 126:34-35(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-357 IN COMPLEX WITH ZINC IONS RP AND DPP4, AND SUBUNIT. RX PubMed=15213224; DOI=10.1074/jbc.m405001200; RA Weihofen W.A., Liu J., Reutter W., Saenger W., Fan H.; RT "Crystal structure of CD26/dipeptidyl-peptidase IV in complex with RT adenosine deaminase reveals a highly amphiphilic interface."; RL J. Biol. Chem. 279:43330-43335(2004). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR. RX PubMed=15139750; DOI=10.1021/jm0499559; RA Terasaka T., Okumura H., Tsuji K., Kato T., Nakanishi I., Kinoshita T., RA Kato Y., Kuno M., Seki N., Naoe Y., Inoue T., Tanaka K., Nakamura K.; RT "Structure-based design and synthesis of non-nucleoside, potent, and orally RT bioavailable adenosine deaminase inhibitors."; RL J. Med. Chem. 47:2728-2731(2004). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR. RX PubMed=15239652; DOI=10.1021/jm0306374; RA Terasaka T., Kinoshita T., Kuno M., Seki N., Tanaka K., Nakanishi I.; RT "Structure-based design, synthesis, and structure-activity relationship RT studies of novel non-nucleoside adenosine deaminase inhibitors."; RL J. Med. Chem. 47:3730-3743(2004). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR. RX PubMed=16060665; DOI=10.1021/bi050529e; RA Kinoshita T., Nakanishi I., Terasaka T., Kuno M., Seki N., Warizaya M., RA Matsumura H., Inoue T., Takano K., Adachi H., Mori Y., Fujii T.; RT "Structural basis of compound recognition by adenosine deaminase."; RL Biochemistry 44:10562-10569(2005). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 2-362 IN COMPLEX WITH DPP4 AND A RP HIV-1 TAT PEPTIDE. RX PubMed=15695814; DOI=10.1074/jbc.m413400200; RA Weihofen W.A., Liu J., Reutter W., Saenger W., Fan H.; RT "Crystal structures of HIV-1 Tat-derived nonapeptides Tat-(1-9) and Trp2- RT Tat-(1-9) bound to the active site of dipeptidyl-peptidase IV (CD26)."; RL J. Biol. Chem. 280:14911-14917(2005). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-356 IN COMPLEX WITH INHIBITOR RP AND ZINC IONS. RX PubMed=16033254; DOI=10.1021/jm050413g; RA Terasaka T., Tsuji K., Kato T., Nakanishi I., Kinoshita T., Kato Y., RA Kuno M., Inoue T., Tanaka K., Nakamura K.; RT "Rational design of non-nucleoside, potent, and orally bioavailable RT adenosine deaminase inhibitors: predicting enzyme conformational change and RT metabolism."; RL J. Med. Chem. 48:4750-4753(2005). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 2-357 IN COMPLEX WITH EHNA. RX PubMed=18549808; DOI=10.1016/j.bbrc.2008.05.180; RA Kinoshita T., Tada T., Nakanishi I.; RT "Conformational change of adenosine deaminase during ligand-exchange in a RT crystal."; RL Biochem. Biophys. Res. Commun. 373:53-57(2008). CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- CC deoxyadenosine (By similarity). Plays an important role in purine CC metabolism and in adenosine homeostasis (By similarity). Modulates CC signaling by extracellular adenosine, and so contributes indirectly to CC cellular signaling events (By similarity). Acts as a positive regulator CC of T-cell coactivation, by binding DPP4 (By similarity). Its CC interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By CC similarity). Enhances dendritic cell immunogenicity by affecting CC dendritic cell costimulatory molecule expression and cytokines and CC chemokines secretion (PubMed:23240012). Enhances CD4+ T-cell CC differentiation and proliferation (By similarity). Acts as a positive CC modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their CC ligand affinity via conformational change (By similarity). Stimulates CC plasminogen activation (By similarity). Plays a role in male fertility CC (By similarity). Plays a protective role in early postimplantation CC embryonic development (By similarity). {ECO:0000250|UniProtKB:P00813, CC ECO:0000250|UniProtKB:P03958, ECO:0000269|PubMed:23240012}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+); CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; CC Evidence={ECO:0000250|UniProtKB:P00813}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; CC Evidence={ECO:0000250|UniProtKB:P00813}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+); CC Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; CC Evidence={ECO:0000250|UniProtKB:P00813}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; CC Evidence={ECO:0000250|UniProtKB:P00813}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, CC ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:16033254}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12554940}; CC -!- SUBUNIT: Interacts with DPP4 (via extracellular domain). Interacts with CC PLG (via Kringle 4 domain); the interaction stimulates PLG activation CC when in complex with DPP4. {ECO:0000250|UniProtKB:P00813}. CC -!- INTERACTION: CC P56658; P27487: DPP4; Xeno; NbExp=5; IntAct=EBI-7475530, EBI-2871277; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00813}; CC Peripheral membrane protein {ECO:0000250}; Extracellular side CC {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. CC Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P03958}. Cytoplasm CC {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. CC Note=Colocalized with DPP4 at the cell surface. CC {ECO:0000250|UniProtKB:P00813}. CC -!- TISSUE SPECIFICITY: Expressed in gastrointestinal tissues (at protein CC level). {ECO:0000269|PubMed:23240012}. CC -!- MASS SPECTROMETRY: Mass=40549; Mass_error=16; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:8877857}; CC -!- PHARMACEUTICAL: Available under the name Adagen (Enzon). This is a PEG- CC conjugated form (pegademase). Used to treat patients with severe CC combined immunodeficiency diseases (SCID). CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/ADA/"; 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; AF280603; AAF91430.1; -; mRNA. DR RefSeq; NP_776312.1; NM_173887.2. DR PDB; 1KRM; X-ray; 2.50 A; A=2-357. DR PDB; 1NDV; X-ray; 2.30 A; A=2-357. DR PDB; 1NDW; X-ray; 2.00 A; A=2-357. DR PDB; 1NDY; X-ray; 2.00 A; A=2-357. DR PDB; 1NDZ; X-ray; 2.00 A; A=2-357. DR PDB; 1O5R; X-ray; 2.35 A; A=2-357. DR PDB; 1QXL; X-ray; 2.25 A; A=2-357. DR PDB; 1UML; X-ray; 2.50 A; A=2-357. DR PDB; 1V79; X-ray; 2.50 A; A=2-357. DR PDB; 1V7A; X-ray; 2.50 A; A=2-357. DR PDB; 1VFL; X-ray; 1.80 A; A=2-357. DR PDB; 1W1I; X-ray; 3.03 A; E/F/G/H=1-357. DR PDB; 1WXY; X-ray; 2.50 A; A=2-357. DR PDB; 1WXZ; X-ray; 2.80 A; A=2-357. DR PDB; 2BGN; X-ray; 3.15 A; E/F/G/H=2-363. DR PDB; 2E1W; X-ray; 2.50 A; A=2-357. DR PDB; 2Z7G; X-ray; 2.52 A; A=2-357. DR PDBsum; 1KRM; -. DR PDBsum; 1NDV; -. DR PDBsum; 1NDW; -. DR PDBsum; 1NDY; -. DR PDBsum; 1NDZ; -. DR PDBsum; 1O5R; -. DR PDBsum; 1QXL; -. DR PDBsum; 1UML; -. DR PDBsum; 1V79; -. DR PDBsum; 1V7A; -. DR PDBsum; 1VFL; -. DR PDBsum; 1W1I; -. DR PDBsum; 1WXY; -. DR PDBsum; 1WXZ; -. DR PDBsum; 2BGN; -. DR PDBsum; 2E1W; -. DR PDBsum; 2Z7G; -. DR AlphaFoldDB; P56658; -. DR SMR; P56658; -. DR IntAct; P56658; 1. DR MINT; P56658; -. DR STRING; 9913.ENSBTAP00000065615; -. DR BindingDB; P56658; -. DR ChEMBL; CHEMBL2966; -. DR DrugCentral; P56658; -. DR PaxDb; 9913-ENSBTAP00000006947; -. DR PeptideAtlas; P56658; -. DR GeneID; 280712; -. DR KEGG; bta:280712; -. DR CTD; 100; -. DR eggNOG; KOG1097; Eukaryota. DR InParanoid; P56658; -. DR BRENDA; 3.5.4.4; 908. DR EvolutionaryTrace; P56658; -. DR PRO; PR:P56658; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell. DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0004000; F:adenosine deaminase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0006154; P:adenosine catabolic process; ISS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central. DR GO; GO:0046103; P:inosine biosynthetic process; ISS:UniProtKB. DR GO; GO:0060169; P:negative regulation of adenosine receptor signaling pathway; IBA:GO_Central. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro. DR GO; GO:0042110; P:T cell activation; IBA:GO_Central. DR CDD; cd01320; ADA; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_00540; A_deaminase; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR028893; A_deaminase. DR InterPro; IPR001365; A_deaminase_dom. DR InterPro; IPR006330; Ado/ade_deaminase. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01430; aden_deam; 1. DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1. DR PANTHER; PTHR11409:SF43; ADENOSINE DEAMINASE; 1. DR Pfam; PF00962; A_deaminase; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell adhesion; Cell junction; Cell membrane; KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Hydrolase; KW Lysosome; Membrane; Metal-binding; Nucleotide metabolism; Pharmaceutical; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00813, FT ECO:0000269|PubMed:8877857" FT CHAIN 2..363 FT /note="Adenosine deaminase" FT /id="PRO_0000194351" FT ACT_SITE 217 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P03958" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL" FT BINDING 17 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, FT ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, FT ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL" FT BINDING 17 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL" FT BINDING 19 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, FT ECO:0007744|PDB:1QXL" FT BINDING 184 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:14709046, FT ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY, FT ECO:0007744|PDB:1WXY" FT BINDING 214 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL" FT BINDING 295 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, FT ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, FT ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, FT ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, FT ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, FT ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12554940, FT ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, FT ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, FT ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, FT ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, FT ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL" FT SITE 58 FT /note="Important for interaction with adenosine receptors FT and increasing their affinity for agonists" FT /evidence="ECO:0000250|UniProtKB:P00813" FT SITE 62 FT /note="Important for interaction with adenosine receptors FT and increasing their affinity for agonists" FT /evidence="ECO:0000250|UniProtKB:P00813" FT SITE 238 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:P03958" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P00813" FT MOD_RES 54 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00813" FT MOD_RES 232 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00813" FT VARIANT 199 FT /note="K -> Q" FT VARIANT 246 FT /note="A -> T" FT VARIANT 352 FT /note="G -> R" FT CONFLICT 8 FT /note="N -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 32..33 FT /note="RK -> KR (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="S -> T (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 60 FT /note="E -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 77..79 FT /note="EAV -> DAI (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 261 FT /note="V -> I (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 279..281 FT /note="PVV -> AVI (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 313..314 FT /note="NE -> KD (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 18..20 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 24..33 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 43..50 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 58..72 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 76..92 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 95..102 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1NDY" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 126..144 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 147..155 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 162..171 FT /evidence="ECO:0007829|PDB:1VFL" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 177..184 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 210..219 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 246..254 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 263..269 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 279..285 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 297..300 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 304..313 FT /evidence="ECO:0007829|PDB:1VFL" FT HELIX 319..331 FT /evidence="ECO:0007829|PDB:1VFL" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:1QXL" FT HELIX 337..351 FT /evidence="ECO:0007829|PDB:1VFL" SQ SEQUENCE 363 AA; 40919 MW; 69F6D25ACFF2A3E5 CRC64; MAQTPAFNKP KVELHVHLDG AIKPETILYY GRKRGIALPA DTPEELQNII GMDKPLSLPE FLAKFDYYMP AIAGCREAVK RIAYEFVEMK AKDGVVYVEV RYSPHLLANS KVEPIPWNQA EGDLTPDEVV SLVNQGLQEG ERDFGVKVRS ILCCMRHQPS WSSEVVELCK KYREQTVVAI DLAGDETIEG SSLFPGHVKA YAEAVKSGVH RTVHAGEVGS ANVVKEAVDT LKTERLGHGY HTLEDATLYN RLRQENMHFE VCPWSSYLTG AWKPDTEHPV VRFKNDQVNY SLNTDDPLIF KSTLDTDYQM TKNEMGFTEE EFKRLNINAA KSSFLPEDEK KELLDLLYKA YGMPSPASAE QCL //