DCE2_HUMAN
ID DCE2_HUMAN Reviewed; 585 AA.
AC Q05329; Q9UD87;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Glutamate decarboxylase 2 {ECO:0000305};
DE EC=4.1.1.15 {ECO:0000305|PubMed:8999827};
DE AltName: Full=65 kDa glutamic acid decarboxylase;
DE Short=GAD-65;
DE AltName: Full=Glutamate decarboxylase 65 kDa isoform;
GN Name=GAD2 {ECO:0000312|HGNC:HGNC:4093}; Synonyms=GAD65;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=1924293; DOI=10.1073/pnas.88.19.8337;
RA Karlsen A.E., Hagopian W.A., Grubin C.E., Dube S., Disteche C.M.,
RA Adler D.A., Barmeier H., Mathewes S., Grant F.J., Foster D., Lernmark A.;
RT "Cloning and primary structure of a human islet isoform of glutamic acid
RT decarboxylase from chromosome 10.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8337-8341(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549570; DOI=10.1073/pnas.89.6.2115;
RA Bu D.-F., Erlander M.G., Hitz B.C., Tillakaratne N.J., Kaufman D.L.,
RA Wagner-Mcpherson C.B., Evans G.A., Tobin A.J.;
RT "Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each
RT encoded by a single gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2115-2119(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8088791; DOI=10.1006/geno.1994.1246;
RA Bu D.-F., Tobin A.J.;
RT "The exon-intron organization of the genes (GAD1 and GAD2) encoding two
RT human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive
RT from a common ancestral GAD.";
RL Genomics 21:222-228(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-12; ASN-124; ARG-286
RP AND GLN-375.
RG NIEHS SNPs program;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-585.
RC TISSUE=Pancreas;
RX PubMed=7680313; DOI=10.1111/j.1432-1033.1993.tb17698.x;
RA Mauch L., Abney C.C., Berg H., Scherbaum W.A., Liedvogel B., Northemann W.;
RT "Characterization of a linear epitope within the human pancreatic 64-kDa
RT glutamic acid decarboxylase and its autoimmune recognition by sera from
RT insulin-dependent diabetes mellitus patients.";
RL Eur. J. Biochem. 212:597-603(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 245-585.
RX PubMed=8243826; DOI=10.2337/diab.42.12.1799;
RA Kim J., Richter W., Aanstoot H.-J., Shi Y., Fu Q., Rajotte R., Warnock G.,
RA Baekkeskov S.;
RT "Differential expression of GAD65 and GAD67 in human, rat, and mouse
RT pancreatic islets.";
RL Diabetes 42:1799-1808(1993).
RN [7]
RP PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, BIOPHYSICOCHEMICAL
RP PROPERTIES, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF 3-SER--SER-13.
RX PubMed=8999827; DOI=10.1074/jbc.272.3.1548;
RA Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.;
RT "Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane
RT anchored from soluble glutamic acid decarboxylase 65 and is restricted to
RT glutamic acid decarboxylase 65alpha.";
RL J. Biol. Chem. 272:1548-1557(1997).
RN [8]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-30 AND CYS-45.
RX PubMed=12356867; DOI=10.1083/jcb.200205053;
RA Kanaani J., El-Din El-Husseini A., Aguilera-Moreno A., Diacovo J.M.,
RA Bredt D.S., Baekkeskov S.;
RT "A combination of three distinct trafficking signals mediates axonal
RT targeting and presynaptic clustering of GAD65.";
RL J. Cell Biol. 158:1229-1238(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 222-235 IN COMPLEX WITH MHC.
RX PubMed=10775108; DOI=10.1126/science.288.5465.505;
RA Corper A.L., Stratmann T., Apostolopoulos V., Scott C.A., Garcia K.C.,
RA Kang A.S., Wilson I.A., Teyton L.;
RT "A structural framework for deciphering the link between I-Ag7 and
RT autoimmune diabetes.";
RL Science 288:505-511(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-584 IN COMPLEX WITH SUBSTRATE,
RP SUBUNIT, AND COFACTOR.
RX PubMed=17384644; DOI=10.1038/nsmb1228;
RA Fenalti G., Law R.H.P., Buckle A.M., Langendorf C., Tuck K., Rosado C.J.,
RA Faux N.G., Mahmood K., Hampe C.S., Banga J.P., Wilce M., Schmidberger J.,
RA Rossjohn J., El-Kabbani O., Pike R.N., Smith A.I., Mackay I.R.,
RA Rowley M.J., Whisstock J.C.;
RT "GABA production by glutamic acid decarboxylase is regulated by a dynamic
RT catalytic loop.";
RL Nat. Struct. Mol. Biol. 14:280-286(2007).
CC -!- FUNCTION: Catalyzes the production of GABA.
CC {ECO:0000305|PubMed:8999827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000305|PubMed:8999827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000305|PubMed:8999827};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17384644};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.15 mM for glutamate {ECO:0000269|PubMed:8999827};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10775108,
CC ECO:0000269|PubMed:17384644}.
CC -!- INTERACTION:
CC Q05329; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-9304251, EBI-2813554;
CC Q05329; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-9304251, EBI-741181;
CC Q05329; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-9304251, EBI-11522760;
CC Q05329; P55056: APOC4; NbExp=3; IntAct=EBI-9304251, EBI-18302142;
CC Q05329; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-9304251, EBI-11343438;
CC Q05329; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-9304251, EBI-714543;
CC Q05329; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-9304251, EBI-23667468;
CC Q05329; Q8WZ55: BSND; NbExp=3; IntAct=EBI-9304251, EBI-7996695;
CC Q05329; Q06432: CACNG1; NbExp=3; IntAct=EBI-9304251, EBI-9686780;
CC Q05329; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-9304251, EBI-2548702;
CC Q05329; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-9304251, EBI-11522780;
CC Q05329; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-9304251, EBI-18013275;
CC Q05329; Q8N8Q1: CYB561D1; NbExp=3; IntAct=EBI-9304251, EBI-12873482;
CC Q05329; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-9304251, EBI-398977;
CC Q05329; Q96Q80: DERL3; NbExp=3; IntAct=EBI-9304251, EBI-12831318;
CC Q05329; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-9304251, EBI-12831978;
CC Q05329; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-9304251, EBI-7943171;
CC Q05329; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-9304251, EBI-3943864;
CC Q05329; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-9304251, EBI-10973142;
CC Q05329; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-9304251, EBI-11793142;
CC Q05329; A8MV81: HIGD1C; NbExp=3; IntAct=EBI-9304251, EBI-12809676;
CC Q05329; Q96B96: LDAF1; NbExp=6; IntAct=EBI-9304251, EBI-7055862;
CC Q05329; Q9H400: LIME1; NbExp=3; IntAct=EBI-9304251, EBI-2830566;
CC Q05329; Q969L2: MAL2; NbExp=6; IntAct=EBI-9304251, EBI-944295;
CC Q05329; Q5EB52: MEST; NbExp=3; IntAct=EBI-9304251, EBI-1050204;
CC Q05329; Q9HC36: MRM3; NbExp=3; IntAct=EBI-9304251, EBI-1045440;
CC Q05329; Q96AL5: PBX3; NbExp=3; IntAct=EBI-9304251, EBI-741171;
CC Q05329; O60664: PLIN3; NbExp=3; IntAct=EBI-9304251, EBI-725795;
CC Q05329; Q8IZV5: RDH10; NbExp=3; IntAct=EBI-9304251, EBI-11913715;
CC Q05329; Q6ZWK4: RHEX; NbExp=3; IntAct=EBI-9304251, EBI-18304046;
CC Q05329; Q9NS64: RPRM; NbExp=3; IntAct=EBI-9304251, EBI-1052363;
CC Q05329; O15126: SCAMP1; NbExp=3; IntAct=EBI-9304251, EBI-954338;
CC Q05329; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-9304251, EBI-3923480;
CC Q05329; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-9304251, EBI-8652744;
CC Q05329; O60906: SMPD2; NbExp=3; IntAct=EBI-9304251, EBI-12828299;
CC Q05329; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9304251, EBI-742688;
CC Q05329; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-9304251, EBI-11958386;
CC Q05329; O43761: SYNGR3; NbExp=3; IntAct=EBI-9304251, EBI-11321949;
CC Q05329; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-9304251, EBI-10171534;
CC Q05329; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-9304251, EBI-10694905;
CC Q05329; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-9304251, EBI-1044859;
CC Q05329; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-9304251, EBI-12045841;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12356867}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:12356867}. Presynaptic cell
CC membrane {ECO:0000269|PubMed:12356867}; Lipid-anchor
CC {ECO:0000269|PubMed:12356867}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12356867}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12356867}; Cytoplasmic side
CC {ECO:0000269|PubMed:12356867}. Note=Associated to cytoplasmic vesicles.
CC In neurons, cytosolic leaflet of Golgi membranes and presynaptic
CC clusters.
CC -!- PTM: Phosphorylated; which does not affect kinetic parameters or
CC subcellular location. {ECO:0000269|PubMed:8999827}.
CC -!- PTM: Palmitoylated; which is required for presynaptic clustering.
CC {ECO:0000269|PubMed:12356867}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49554.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gad2/";
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DR EMBL; M81882; AAA62367.1; -; mRNA.
DR EMBL; M74826; AAA58491.1; -; mRNA.
DR EMBL; AY340073; AAP88040.1; -; Genomic_DNA.
DR EMBL; X69936; CAA49554.1; ALT_INIT; mRNA.
DR EMBL; M70435; AAA52513.1; -; mRNA.
DR CCDS; CCDS7149.1; -.
DR PIR; A41935; A41292.
DR RefSeq; NP_000809.1; NM_000818.2.
DR RefSeq; NP_001127838.1; NM_001134366.1.
DR PDB; 1ES0; X-ray; 2.60 A; B=207-220.
DR PDB; 2OKK; X-ray; 2.30 A; A=88-584.
DR PDBsum; 1ES0; -.
DR PDBsum; 2OKK; -.
DR AlphaFoldDB; Q05329; -.
DR SMR; Q05329; -.
DR BioGRID; 108846; 46.
DR ComplexPortal; CPX-3033; Glutamate decarboxylase 2 complex.
DR ComplexPortal; CPX-3065; Glutamate decarboxylase 1/2 complex.
DR DIP; DIP-29293N; -.
DR IntAct; Q05329; 40.
DR STRING; 9606.ENSP00000365437; -.
DR ChEMBL; CHEMBL2952; -.
DR DrugBank; DB00142; Glutamic acid.
DR iPTMnet; Q05329; -.
DR PhosphoSitePlus; Q05329; -.
DR SwissPalm; Q05329; -.
DR BioMuta; GAD2; -.
DR DMDM; 1352216; -.
DR jPOST; Q05329; -.
DR MassIVE; Q05329; -.
DR PaxDb; Q05329; -.
DR PeptideAtlas; Q05329; -.
DR PRIDE; Q05329; -.
DR ProteomicsDB; 58319; -.
DR ABCD; Q05329; 12 sequenced antibodies.
DR Antibodypedia; 3635; 735 antibodies from 44 providers.
DR DNASU; 2572; -.
DR Ensembl; ENST00000259271.7; ENSP00000259271.3; ENSG00000136750.13.
DR Ensembl; ENST00000376261.8; ENSP00000365437.3; ENSG00000136750.13.
DR GeneID; 2572; -.
DR KEGG; hsa:2572; -.
DR MANE-Select; ENST00000376261.8; ENSP00000365437.3; NM_001134366.2; NP_001127838.1.
DR CTD; 2572; -.
DR DisGeNET; 2572; -.
DR GeneCards; GAD2; -.
DR HGNC; HGNC:4093; GAD2.
DR HPA; ENSG00000136750; Group enriched (brain, retina).
DR MIM; 138275; gene.
DR neXtProt; NX_Q05329; -.
DR OpenTargets; ENSG00000136750; -.
DR PharmGKB; PA28508; -.
DR VEuPathDB; HostDB:ENSG00000136750; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000157951; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; Q05329; -.
DR OMA; VACTCDQ; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; Q05329; -.
DR TreeFam; TF314688; -.
DR BioCyc; MetaCyc:HS06208-MON; -.
DR BRENDA; 4.1.1.15; 2681.
DR PathwayCommons; Q05329; -.
DR Reactome; R-HSA-888568; GABA synthesis.
DR Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-HSA-9022927; MECP2 regulates transcription of genes involved in GABA signaling.
DR SABIO-RK; Q05329; -.
DR SignaLink; Q05329; -.
DR SIGNOR; Q05329; -.
DR BioGRID-ORCS; 2572; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; GAD2; human.
DR EvolutionaryTrace; Q05329; -.
DR GeneWiki; GAD2; -.
DR GenomeRNAi; 2572; -.
DR Pharos; Q05329; Tbio.
DR PRO; PR:Q05329; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q05329; protein.
DR Bgee; ENSG00000136750; Expressed in islet of Langerhans and 89 other tissues.
DR ExpressionAtlas; Q05329; baseline and differential.
DR Genevisible; Q05329; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006540; P:glutamate decarboxylation to succinate; IBA:GO_Central.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Decarboxylase; Golgi apparatus; Lipoprotein; Lyase;
KW Membrane; Neurotransmitter biosynthesis; Palmitate; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Synapse.
FT CHAIN 1..585
FT /note="Glutamate decarboxylase 2"
FT /id="PRO_0000146968"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..183
FT /ligand="substrate"
FT BINDING 558
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17384644"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8999827"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8999827"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8999827"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8999827"
FT MOD_RES 396
FT /note="N6-(pyridoxal phosphate)lysine"
FT LIPID 30
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12356867"
FT LIPID 45
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12356867"
FT VARIANT 12
FT /note="G -> R (in dbSNP:rs8190591)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018821"
FT VARIANT 124
FT /note="K -> N (in dbSNP:rs8190600)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018822"
FT VARIANT 153
FT /note="P -> Q (in dbSNP:rs2839672)"
FT /id="VAR_029176"
FT VARIANT 232
FT /note="G -> E (in dbSNP:rs2839673)"
FT /id="VAR_029177"
FT VARIANT 286
FT /note="K -> R (in dbSNP:rs8190671)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018823"
FT VARIANT 326
FT /note="G -> A (in dbSNP:rs2839678)"
FT /id="VAR_029178"
FT VARIANT 375
FT /note="R -> Q (in dbSNP:rs8190730)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018824"
FT MUTAGEN 3..13
FT /note="SPGSGFWSFGS->APGAGFWAFGA: No effect on glutamate
FT decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:8999827"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 104..126
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:2OKK"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 211..228
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:2OKK"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:2OKK"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 414..419
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 452..486
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:2OKK"
FT TURN 511..515
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 529..540
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:2OKK"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:2OKK"
FT HELIX 568..581
FT /evidence="ECO:0007829|PDB:2OKK"
SQ SEQUENCE 585 AA; 65411 MW; 0322509F0E2C32EE CRC64;
MASPGSGFWS FGSEDGSGDS ENPGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG
SQPPRAAARK AACACDQKPC SCSKVDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
PGGAISNMYA MMIARFKMFP EVKEKGMAAL PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQNCNQ
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH VDKCLELAEY
LYNIIKNREG YEMVFDGKPQ HTNVCFWYIP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
