FAAH_ARATH
ID FAAH_ARATH Reviewed; 607 AA.
AC Q7XJJ7; Q93ZI9; Q9FGF2; Q9LLC0;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Fatty acid amide hydrolase {ECO:0000303|PubMed:12824167};
DE Short=AtFAAH {ECO:0000303|PubMed:16880402};
DE EC=3.5.1.99 {ECO:0000269|PubMed:12824167};
DE AltName: Full=N-acylethanolamine amidohydrolase {ECO:0000303|PubMed:12824167};
GN Name=FAAH {ECO:0000303|PubMed:12824167};
GN OrderedLocusNames=At5g64440 {ECO:0000312|EMBL:AED97893.1};
GN ORFNames=T12B11.3 {ECO:0000312|EMBL:BAB11605.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chang W.-Z., Soll D.;
RT "Cloning and characterization of an amidase gene frome Arabidopsis
RT thaliana.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Leaf;
RX PubMed=12824167; DOI=10.1074/jbc.m305613200;
RA Shrestha R., Dixon R.A., Chapman K.D.;
RT "Molecular identification of a functional homologue of the mammalian fatty
RT acid amide hydrolase in Arabidopsis thaliana.";
RL J. Biol. Chem. 278:34990-34997(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16624618; DOI=10.1016/j.bbalip.2006.03.004;
RA Shrestha R., Kim S.C., Dyer J.M., Dixon R.A., Chapman K.D.;
RT "Plant fatty acid (ethanol) amide hydrolases.";
RL Biochim. Biophys. Acta 1761:324-334(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=16738862; DOI=10.1007/s00425-006-0304-2;
RA Pollmann S., Neu D., Lehmann T., Berkowitz O., Schaefer T., Weiler E.W.;
RT "Subcellular localization and tissue specific expression of amidase 1 from
RT Arabidopsis thaliana.";
RL Planta 224:1241-1253(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16880402; DOI=10.1073/pnas.0603571103;
RA Wang Y.S., Shrestha R., Kilaru A., Wiant W., Venables B.J., Chapman K.D.,
RA Blancaflor E.B.;
RT "Manipulation of Arabidopsis fatty acid amide hydrolase expression modifies
RT plant growth and sensitivity to N-acylethanolamines.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12197-12202(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18643971; DOI=10.1111/j.1365-313x.2008.03603.x;
RA Kang L., Wang Y.S., Uppalapati S.R., Wang K., Tang Y., Vadapalli V.,
RA Venables B.J., Chapman K.D., Blancaflor E.B., Mysore K.S.;
RT "Overexpression of a fatty acid amide hydrolase compromises innate immunity
RT in Arabidopsis.";
RL Plant J. 56:336-349(2008).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-205; 281-SER-SER-282; SER-305; ARG-307 AND SER-360.
RX PubMed=19801664; DOI=10.1074/jbc.m109.059022;
RA Kim S.C., Kang L., Nagaraj S., Blancaflor E.B., Mysore K.S., Chapman K.D.;
RT "Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic
RT activity influences growth but not sensitivity to abscisic acid or
RT pathogens.";
RL J. Biol. Chem. 284:34065-34074(2009).
RN [11]
RP FUNCTION.
RX PubMed=22645580; DOI=10.3389/fpls.2012.00032;
RA Teaster N.D., Keereetaweep J., Kilaru A., Wang Y.S., Tang Y., Tran C.N.,
RA Ayre B.G., Chapman K.D., Blancaflor E.B.;
RT "Overexpression of fatty acid amide hydrolase induces early flowering in
RT Arabidopsis thaliana.";
RL Front. Plant Sci. 3:32-32(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=24918118; DOI=10.1021/cb500191a;
RA Palmer A.G., Senechal A.C., Mukherjee A., Ane J.M., Blackwell H.E.;
RT "Plant responses to bacterial N-acyl L-homoserine lactones are dependent on
RT enzymatic degradation to L-homoserine.";
RL ACS Chem. Biol. 9:1834-1845(2014).
RN [13]
RP FUNCTION.
RX PubMed=28112243; DOI=10.1038/srep41121;
RA Khan B.R., Faure L., Chapman K.D., Blancaflor E.B.;
RT "A chemical genetic screen uncovers a small molecule enhancer of the N-
RT acylethanolamine degrading enzyme, fatty acid amide hydrolase, in
RT Arabidopsis.";
RL Sci. Rep. 7:41121-41121(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RX PubMed=30894416; DOI=10.1074/jbc.ra118.006672;
RA Aziz M., Wang X., Tripathi A., Bankaitis V.A., Chapman K.D.;
RT "Structural analysis of a plant fatty acid amide hydrolase provides
RT insights into the evolutionary diversity of bioactive acylethanolamides.";
RL J. Biol. Chem. 294:7419-7432(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of bioactive endogenous fatty acid
CC amides to their corresponding acids (PubMed:12824167). The hydrolysis
CC of endogenous amidated lipids terminates their participation as lipid
CC mediators in various signaling systems (Probable). Converts a wide
CC range of N-acylethanolamines (NAEs) to their corresponding free fatty
CC acids and ethanolamine (PubMed:12824167, PubMed:16624618,
CC PubMed:16738862, PubMed:16880402). Can use oleamide as substrate, but
CC not indole-3-acetamide, 1-naphtalene-acetamide, nicotinic acid amide or
CC L-asparagine (PubMed:16738862). Can use 2-arachidonylglycerol as
CC substrate (PubMed:19801664). Participates in the regulation of plant
CC growth (PubMed:16880402). Hydrolyzes N-dodecanoylethanolamine, which is
CC has a growth inhibitory effect on seedling growth (PubMed:28112243).
CC Involved in plant defense signaling (PubMed:18643971). Involved in
CC abscisic acid (ABA) signaling through mechanisms that are independent
CC of the catalytic activity (PubMed:19801664). Involved in the regulation
CC of flowering time (PubMed:22645580). Catalyzes the hydrolysis of N-acyl
CC L-homoserine lactones (AHLs), which are a class of signaling molecules
CC produced by bacteria for quorum sensing (PubMed:24918118). Accumulation
CC of L-homoserine appears to encourage plant growth at low concentrations
CC by stimulating transpiration, but higher concentrations inhibit growth
CC by stimulating ethylene production (PubMed:24918118).
CC {ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618,
CC ECO:0000269|PubMed:16738862, ECO:0000269|PubMed:16880402,
CC ECO:0000269|PubMed:18643971, ECO:0000269|PubMed:19801664,
CC ECO:0000269|PubMed:22645580, ECO:0000269|PubMed:24918118,
CC ECO:0000269|PubMed:28112243, ECO:0000305|PubMed:12824167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine;
CC Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99;
CC Evidence={ECO:0000269|PubMed:12824167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137;
CC Evidence={ECO:0000269|PubMed:12824167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z,12Z-octadecadienoyl)-ethanolamine = (9Z,12Z)-
CC octadecadienoate + ethanolamine; Xref=Rhea:RHEA:35567,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30245, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:64032; Evidence={ECO:0000269|PubMed:12824167,
CC ECO:0000269|PubMed:16624618, ECO:0000269|PubMed:16738862,
CC ECO:0000269|PubMed:16880402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35568;
CC Evidence={ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618,
CC ECO:0000269|PubMed:16738862, ECO:0000269|PubMed:16880402};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine +
CC hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464;
CC Evidence={ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618,
CC ECO:0000269|PubMed:16738862, ECO:0000269|PubMed:19801664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065;
CC Evidence={ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618,
CC ECO:0000269|PubMed:16738862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetradecanoylethanolamine = ethanolamine +
CC tetradecanoate; Xref=Rhea:RHEA:45452, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57603, ChEBI:CHEBI:85262;
CC Evidence={ECO:0000269|PubMed:12824167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45453;
CC Evidence={ECO:0000269|PubMed:12824167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine;
CC Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:85263;
CC Evidence={ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618,
CC ECO:0000269|PubMed:16880402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457;
CC Evidence={ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618,
CC ECO:0000269|PubMed:16880402};
CC -!- ACTIVITY REGULATION: Inhibited by methyl arachidonyl fluorophosphonate
CC (MAFP). {ECO:0000269|PubMed:12824167, ECO:0000269|PubMed:16624618}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.6 uM for N-acylethanolamine 20:4 {ECO:0000269|PubMed:12824167};
CC KM=26.2 uM for N-acylethanolamine 18:2 {ECO:0000269|PubMed:12824167};
CC KM=54 uM for N-acylethanolamine 18:2 {ECO:0000269|PubMed:16624618};
CC KM=50.8 uM for N-acylethanolamine 16:0 {ECO:0000269|PubMed:12824167};
CC KM=20 uM for N-acylethanolamine 16:0 {ECO:0000269|PubMed:16624618};
CC KM=23 uM for N-acylethanolamine 16:0 {ECO:0000269|PubMed:19801664};
CC KM=37.0 uM for N-acylethanolamine 14:0 {ECO:0000269|PubMed:12824167};
CC KM=17.6 uM for N-acylethanolamine 12:0 {ECO:0000269|PubMed:12824167};
CC KM=25 uM for N-acylethanolamine 12:0 {ECO:0000269|PubMed:16624618};
CC Vmax=17.9 umol/h/mg enzyme with N-acylethanolamine 20:4 as substrate
CC {ECO:0000269|PubMed:12824167};
CC Vmax=14.1 umol/h/mg enzyme with N-acylethanolamine 18:2 as substrate
CC {ECO:0000269|PubMed:12824167};
CC Vmax=12.1 umol/h/mg enzyme with N-acylethanolamine 16:0 as substrate
CC {ECO:0000269|PubMed:12824167};
CC Vmax=181.7 umol/h/mg enzyme with N-acylethanolamine 16:0 as substrate
CC {ECO:0000269|PubMed:19801664};
CC Vmax=9.1 umol/h/mg enzyme with N-acylethanolamine 14:0 as substrate
CC {ECO:0000269|PubMed:12824167};
CC Vmax=13.9 umol/h/mg enzyme with N-acylethanolamine 12:0 as substrate
CC {ECO:0000269|PubMed:12824167};
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:30894416}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18643971}. Cell membrane
CC {ECO:0000269|PubMed:18643971}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers
CC (PubMed:16738862). Expressed in seedlings, flowers, roots, siliques,
CC seeds and leaves (PubMed:16880402). {ECO:0000269|PubMed:16738862,
CC ECO:0000269|PubMed:16880402}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during seed germination and early
CC postgerminative seedling growth. {ECO:0000269|PubMed:16880402}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:16880402). Enhanced sensitivity to inhibition of
CC seedling growth induced by exogenous N-acylethanolamine.
CC {ECO:0000269|PubMed:16880402}.
CC -!- MISCELLANEOUS: Plants overexpressing FAAH exhibit accelerated seedling
CC growth (PubMed:16880402). Plants overexpressing FAAH exhibit enhanced
CC susceptibility to the bacterial pathogen Pseudomons syringae pv tomato
CC (PubMed:18643971). Plants overexpressing FAAH exhibit enhanced
CC sensitivity to abscisic acid (ABA) (PubMed:19801664). Plants
CC overexpressing FAAH exhibit early flowering (PubMed:22645580).
CC {ECO:0000269|PubMed:16880402, ECO:0000269|PubMed:18643971,
CC ECO:0000269|PubMed:19801664, ECO:0000269|PubMed:22645580}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09742.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF223949; AAF73891.1; -; mRNA.
DR EMBL; AY308736; AAP83139.1; -; mRNA.
DR EMBL; AB025640; BAB11605.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97893.1; -; Genomic_DNA.
DR EMBL; AY057501; AAL09742.1; ALT_FRAME; mRNA.
DR EMBL; AY143870; AAN28809.1; -; mRNA.
DR RefSeq; NP_201249.2; NM_125840.4.
DR PDB; 6DHV; X-ray; 2.10 A; A/B=1-607.
DR PDB; 6DII; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-607.
DR PDBsum; 6DHV; -.
DR PDBsum; 6DII; -.
DR AlphaFoldDB; Q7XJJ7; -.
DR SMR; Q7XJJ7; -.
DR STRING; 3702.AT5G64440.1; -.
DR SwissLipids; SLP:000001900; -.
DR iPTMnet; Q7XJJ7; -.
DR PaxDb; Q7XJJ7; -.
DR PRIDE; Q7XJJ7; -.
DR ProteomicsDB; 222339; -.
DR EnsemblPlants; AT5G64440.1; AT5G64440.1; AT5G64440.
DR GeneID; 836565; -.
DR Gramene; AT5G64440.1; AT5G64440.1; AT5G64440.
DR KEGG; ath:AT5G64440; -.
DR Araport; AT5G64440; -.
DR TAIR; locus:2179371; AT5G64440.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_0_2_1; -.
DR InParanoid; Q7XJJ7; -.
DR OMA; NVLGWPS; -.
DR OrthoDB; 1036483at2759; -.
DR PhylomeDB; Q7XJJ7; -.
DR BioCyc; ARA:AT5G64440-MON; -.
DR BRENDA; 3.5.1.99; 399.
DR SABIO-RK; Q7XJJ7; -.
DR PRO; PR:Q7XJJ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q7XJJ7; baseline and differential.
DR Genevisible; Q7XJJ7; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0103073; F:anandamide amidohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047412; F:N-(long-chain-acyl)ethanolamine deacylase activity; IMP:TAIR.
DR GO; GO:0102077; F:oleamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IMP:TAIR.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Endoplasmic reticulum; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..607
FT /note="Fatty acid amide hydrolase"
FT /id="PRO_0000414026"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:19801664"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:19801664"
FT ACT_SITE 305
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|PubMed:19801664"
FT BINDING 302..305
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30894416,
FT ECO:0007744|PDB:6DII"
FT MUTAGEN 205
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19801664"
FT MUTAGEN 281..282
FT /note="SS->AA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19801664"
FT MUTAGEN 305
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19801664"
FT MUTAGEN 307
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19801664"
FT MUTAGEN 360
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:19801664"
FT CONFLICT 127
FT /note="R -> W (in Ref. 3; BAB11605 and 1; AAF73891)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="M -> R (in Ref. 1; AAF73891)"
FT /evidence="ECO:0000305"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6DII"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6DII"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:6DHV"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6DII"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:6DHV"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6DHV"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 293..304
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:6DHV"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:6DII"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 362..368
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 405..422
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 434..458
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 481..504
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:6DII"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 532..538
FT /evidence="ECO:0007829|PDB:6DHV"
FT TURN 539..542
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 543..548
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 552..559
FT /evidence="ECO:0007829|PDB:6DHV"
FT STRAND 565..573
FT /evidence="ECO:0007829|PDB:6DHV"
FT HELIX 577..590
FT /evidence="ECO:0007829|PDB:6DHV"
SQ SEQUENCE 607 AA; 66079 MW; B659CFA60EFC1633 CRC64;
MGKYQVMKRA SEVDLSTVKY KAETMKAPHL TGLSFKLFVN LLEAPLIGSL IVDYLKKDNG
MTKIFRNTVI PEEPMFRPEF PSQEPEHDVV IVGEDESPID RLETALKCLP QYDPSRSLHA
DPVSSFRYWK IRDYAYAYRS KLTTPLQVAK RIISIIEEFG YDKPPTPFLI RFDANEVIKQ
AEASTRRFEQ GNPISVLDGI FVTIKDDIDC LPHPTNGGTT WLHEDRSVEK DSAVVSKLRS
CGAILLGKAN MHELGMGTTG NNSNYGTTRN PHDPKRYTGG SSSGSAAIVA AGLCSAALGT
DGGGSVRIPS ALCGITGLKT TYGRTDMTGS LCEGGTVEII GPLASSLEDA FLVYAAILGS
SSADRYNLKP SPPCFPKLLS HNGSNAIGSL RLGKYTKWFN DVSSSDISDK CEDILKLLSN
NHGCKVVEIV VPELEEMRAA HVISIGSPTL SSLTPYCEAG KNSKLSYDTR TSFAIFRSFS
ASDYIAAQCL RRRLMEYHLN IFKDVDVIVT PTTGMTAPVI PPDALKNGET NIQVTTDLMR
FVLAANLLGF PAISVPVGYD KEGLPIGLQI MGRPWAEATV LGLAAAVEEL APVTKKPAIF
YDILNTN
