ASE2_ARATH
ID ASE2_ARATH Reviewed; 561 AA.
AC Q9STG9; Q39000; Q5MAT8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Amidophosphoribosyltransferase 2, chloroplastic;
DE Short=AtATase2;
DE Short=AtPURF2;
DE Short=PRPP2;
DE EC=2.4.2.14;
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase 2;
DE Short=AtGPRAT2;
DE AltName: Full=Protein CHLOROPLAST IMPORT APPARATUS 1;
DE AltName: Full=Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS;
DE Flags: Precursor;
GN Name=ASE2; Synonyms=CIA1, DOV1, GPRAT2, PURF2; OrderedLocusNames=At4g34740;
GN ORFNames=T4L20.320;
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 [GENOMIC DNA].
RC STRAIN=cv. En-1;
RA Maurer A., Rogers E.E.;
RT "Purine biosynthesis links chloroplast development and altered metal
RT homeostasis in Arabidopsis thaliana.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-561, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower, Leaf, and Root;
RX PubMed=7948903; DOI=10.1007/bf00039565;
RA Ito T., Shiraishi H., Okada K., Shimura Y.;
RT "Two amidophosphoribosyltransferase genes of Arabidopsis thaliana expressed
RT in different organs.";
RL Plant Mol. Biol. 26:529-533(1994).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=14977588; DOI=10.2741/1344;
RA van der Graaff E., Hooykaas P., Lein W., Lerchl J., Kunze G., Sonnewald U.,
RA Boldt R.;
RT "Molecular analysis of 'de novo' purine biosynthesis in solanaceous species
RT and in Arabidopsis thaliana.";
RL Front. Biosci. 9:1803-1816(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-187, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15266056; DOI=10.1104/pp.104.040956;
RA Hung W.-F., Chen L.-J., Boldt R., Sun C.-W., Li H.-M.;
RT "Characterization of Arabidopsis glutamine phosphoribosyl pyrophosphate
RT amidotransferase-deficient mutants.";
RL Plant Physiol. 135:1314-1323(2004).
RN [8]
RP FUNCTION, MUTAGENESIS OF ARG-264; PRO-265; GLY-371; PRO-476 AND TYR-494,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=17616508; DOI=10.1104/pp.107.099705;
RA Walsh T.A., Bauer T., Neal R., Merlo A.O., Schmitzer P.R., Hicks G.R.,
RA Honma M., Matsumura W., Wolff K., Davies J.P.;
RT "Chemical genetic identification of glutamine phosphoribosylpyrophosphate
RT amidotransferase as the target for a novel bleaching herbicide in
RT Arabidopsis.";
RL Plant Physiol. 144:1292-1304(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Catalyzes the first committed step of 'de novo purine
CC biosynthesis from glutamine. Required for chloroplast biogenesis and
CC cell division. Confers sensitivity to the phenyltriazole acetic acid
CC compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic
CC acid (DAS734), a bleaching herbicide. {ECO:0000269|PubMed:14977588,
CC ECO:0000269|PubMed:15266056, ECO:0000269|PubMed:17616508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14;
CC Evidence={ECO:0000269|PubMed:17616508};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by the phenyltriazole acetic acid
CC compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic
CC acid (DAS734), a bleaching herbicide. {ECO:0000269|PubMed:17616508}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.34 mM for glutamine {ECO:0000269|PubMed:17616508};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15266056, ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC in cotyledons. {ECO:0000269|PubMed:14977588,
CC ECO:0000269|PubMed:15266056, ECO:0000269|PubMed:7948903}.
CC -!- DISRUPTION PHENOTYPE: Strong growth retardation and severe chlorosis in
CC leaves; white leaves, but green cotyledons. Leaves missing the palisade
CC mesophyll layer, due to reduced cell number and size. Abnormal
CC thylakoid membrane in chloroplasts, probably due to photo-oxidative
CC damage. Defective in protein import into chloroplasts.
CC {ECO:0000269|PubMed:14977588, ECO:0000269|PubMed:15266056}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; AY842241; AAW28080.1; -; Genomic_DNA.
DR EMBL; AL023094; CAA18853.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80191.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86417.1; -; Genomic_DNA.
DR EMBL; AY065123; AAL38299.1; -; mRNA.
DR EMBL; AY081611; AAM10173.1; -; mRNA.
DR EMBL; D28869; BAA06024.1; -; mRNA.
DR PIR; T05294; T05294.
DR RefSeq; NP_195200.1; NM_119640.3.
DR PDB; 6LBP; X-ray; 3.06 A; A/B=75-561.
DR PDBsum; 6LBP; -.
DR AlphaFoldDB; Q9STG9; -.
DR SMR; Q9STG9; -.
DR BioGRID; 14908; 5.
DR IntAct; Q9STG9; 4.
DR STRING; 3702.AT4G34740.1; -.
DR MEROPS; C44.A01; -.
DR MEROPS; C44.A03; -.
DR SwissPalm; Q9STG9; -.
DR PaxDb; Q9STG9; -.
DR PRIDE; Q9STG9; -.
DR ProteomicsDB; 246850; -.
DR EnsemblPlants; AT4G34740.1; AT4G34740.1; AT4G34740.
DR GeneID; 829626; -.
DR Gramene; AT4G34740.1; AT4G34740.1; AT4G34740.
DR KEGG; ath:AT4G34740; -.
DR Araport; AT4G34740; -.
DR TAIR; locus:2139549; AT4G34740.
DR eggNOG; KOG0572; Eukaryota.
DR HOGENOM; CLU_022389_3_3_1; -.
DR InParanoid; Q9STG9; -.
DR OMA; CTHCFDG; -.
DR OrthoDB; 400911at2759; -.
DR PhylomeDB; Q9STG9; -.
DR BioCyc; ARA:AT4G34740-MON; -.
DR BRENDA; 2.4.2.14; 399.
DR UniPathway; UPA00074; UER00124.
DR PRO; PR:Q9STG9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STG9; baseline and differential.
DR Genevisible; Q9STG9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IMP:TAIR.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:TAIR.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR Pfam; PF13537; GATase_7; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Glutamine amidotransferase; Glycosyltransferase;
KW Iron; Iron-sulfur; Magnesium; Metal-binding; Plastid; Purine biosynthesis;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..561
FT /note="Amidophosphoribosyltransferase 2, chloroplastic"
FT /id="PRO_0000420282"
FT DOMAIN 87..307
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 323
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MUTAGEN 187
FT /note="H->T: In cia1-2; small plants with white leaves
FT showing an irregular mosaic of green sectors."
FT /evidence="ECO:0000269|PubMed:15266056"
FT MUTAGEN 264
FT /note="R->K: Strong resistance to the bleaching herbicides
FT DAS073 and DAS734."
FT /evidence="ECO:0000269|PubMed:17616508"
FT MUTAGEN 265
FT /note="P->S: Low resistance to the bleaching herbicides
FT DAS073 and DAS734; when associated with F-494."
FT /evidence="ECO:0000269|PubMed:17616508"
FT MUTAGEN 371
FT /note="G->S: Low resistance to the bleaching herbicides
FT DAS073 and DAS734."
FT /evidence="ECO:0000269|PubMed:17616508"
FT MUTAGEN 476
FT /note="P->S: Resistance to the bleaching herbicides DAS073
FT and DAS734."
FT /evidence="ECO:0000269|PubMed:17616508"
FT MUTAGEN 494
FT /note="Y->F: Low resistance to the bleaching herbicides
FT DAS073 and DAS734; when associated with S-265."
FT /evidence="ECO:0000269|PubMed:17616508"
FT CONFLICT 5
FT /note="S -> C (in Ref. 1; AAW28080)"
FT /evidence="ECO:0000305"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:6LBP"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6LBP"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 439..450
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 454..462
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 505..512
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 513..518
FT /evidence="ECO:0007829|PDB:6LBP"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:6LBP"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:6LBP"
SQ SEQUENCE 561 AA; 61030 MW; AE52BD02CE304796 CRC64;
MAATSSISSS LSLNAKPNKL SNNNNNNKPH RFLRNPFLNP SSSSFSPLPA SISSSSSSPS
FPLRVSNPLT LLAADNDDYD EKPREECGVV GIYGDSEASR LCYLALHALQ HRGQEGAGIV
TVSKDKVLQT ITGVGLVSEV FSESKLDQLP GDIAIGHVRY STAGSSMLKN VQPFVAGYRF
GSVGVAHNGN LVNYTKLRAD LEENGSIFNT SSDTEVVLHL IAISKARPFF MRIVDACEKL
QGAYSMVFVT EDKLVAVRDP HGFRPLVMGR RSNGAVVFAS ETCALDLIEA TYEREVYPGE
VLVVDKDGVK CQCLMPHPEP KQCIFEHIYF SLPNSIVFGR SVYESRHVFG EILATESPVD
CDVVIAVPDS GVVAALGYAA KAGVAFQQGL IRSHYVGRTF IEPSQKIRDF GVKLKLSPVR
GVLEGKRVVV VDDSIVRGTT SSKIVRLLRE AGAKEVHMRI ASPPIIASCY YGVDTPSSNE
LISNRMSVDE IRDYIGCDSL AFLSFETLKK HLGEDSRSFC YACFTGDYPV KPTEDKVKRG
GDFIDDGLVG GIHNIEGGWV R
