NCPR2_ARATH
ID NCPR2_ARATH Reviewed; 711 AA.
AC Q9SUM3; F4JPK2; Q39036;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=NADPH--cytochrome P450 reductase 2 {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=CPR 2 {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=P450R 2 {ECO:0000255|HAMAP-Rule:MF_03212};
DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
GN Name=ATR2; Synonyms=AR2; OrderedLocusNames=At4g30210; ORFNames=F9N11.60;
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] (ISOFORM 1), AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9235908; DOI=10.1074/jbc.272.31.19176;
RA Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.;
RT "Cloning, yeast expression, and characterization of the coupling of two
RT distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases
RT with P450 CYP73A5.";
RL J. Biol. Chem. 272:19176-19186(1997).
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] (ISOFORM 1).
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=9990323; DOI=10.1046/j.1432-1327.1998.2581040.x;
RA Louerat-Oriou B., Perret A., Pompon D.;
RT "Differential redox and electron-transfer properties of purified yeast,
RT plant and human NADPH-cytochrome P-450 reductases highly modulate
RT cytochrome P-450 activities.";
RL Eur. J. Biochem. 258:1040-1049(1998).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9449848; DOI=10.1104/pp.116.1.357;
RA Mizutani M., Ohta D.;
RT "Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana.
RT Gene structure, heterologous expression in insect cells, and differential
RT regulation.";
RL Plant Physiol. 116:357-367(1998).
RN [7]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9880378; DOI=10.1104/pp.119.1.353;
RA Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.;
RT "Microsomal electron transfer in higher plants: cloning and heterologous
RT expression of NADH-cytochrome b5 reductase from Arabidopsis.";
RL Plant Physiol. 119:353-361(1999).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10733884; DOI=10.1006/prep.1999.1195;
RA Hull A.K., Celenza J.L.;
RT "Bacterial expression and purification of the Arabidopsis NADPH-cytochrome
RT P450 reductase ATR2.";
RL Protein Expr. Purif. 18:310-315(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC cytochrome P450 in microsomes. It can also provide electron transfer to
CC heme oxygenase and cytochrome B5. Reduces a variety of substrates in
CC vitro, such as cytochrome c, feericyanide and dichloroindophenol.
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:10733884,
CC ECO:0000269|PubMed:9235908, ECO:0000269|PubMed:9449848,
CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03212};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9990323};
CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9990323};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for NADPH (at pH 7.7 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848,
CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323};
CC KM=2.0 uM for NADPH (at pH 7.25 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848,
CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323};
CC KM=15 uM for cytochrome c (at pH 7.7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848,
CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323};
CC KM=16 uM for cytochrome c (at pH 7.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848,
CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323};
CC KM=22.5 uM for cytochrome c (at pH 7.7 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848,
CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SUM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SUM3-2; Sequence=VSP_042906;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:9449848}.
CC -!- INDUCTION: By wounding and transition from dark to light.
CC {ECO:0000269|PubMed:9449848}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
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DR EMBL; X66017; CAA46815.1; -; mRNA.
DR EMBL; AL109796; CAB52465.1; -; Genomic_DNA.
DR EMBL; AL161576; CAB81014.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85737.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85738.1; -; Genomic_DNA.
DR EMBL; AF325101; AAK17169.1; -; mRNA.
DR PIR; S21531; S21531.
DR PIR; T14081; T14081.
DR RefSeq; NP_194750.1; NM_119167.4. [Q9SUM3-1]
DR RefSeq; NP_849472.2; NM_179141.2. [Q9SUM3-2]
DR PDB; 5GXU; X-ray; 2.30 A; A/B=73-711.
DR PDBsum; 5GXU; -.
DR AlphaFoldDB; Q9SUM3; -.
DR SMR; Q9SUM3; -.
DR STRING; 3702.AT4G30210.1; -.
DR iPTMnet; Q9SUM3; -.
DR PaxDb; Q9SUM3; -.
DR PRIDE; Q9SUM3; -.
DR ProteomicsDB; 251241; -. [Q9SUM3-1]
DR EnsemblPlants; AT4G30210.1; AT4G30210.1; AT4G30210. [Q9SUM3-2]
DR EnsemblPlants; AT4G30210.2; AT4G30210.2; AT4G30210. [Q9SUM3-1]
DR GeneID; 829144; -.
DR Gramene; AT4G30210.1; AT4G30210.1; AT4G30210. [Q9SUM3-2]
DR Gramene; AT4G30210.2; AT4G30210.2; AT4G30210. [Q9SUM3-1]
DR KEGG; ath:AT4G30210; -.
DR Araport; AT4G30210; -.
DR TAIR; locus:2128951; AT4G30210.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; Q9SUM3; -.
DR PhylomeDB; Q9SUM3; -.
DR BioCyc; ARA:AT4G30210-MON; -.
DR BioCyc; MetaCyc:AT4G30210-MON; -.
DR SABIO-RK; Q9SUM3; -.
DR PRO; PR:Q9SUM3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUM3; baseline and differential.
DR Genevisible; Q9SUM3; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:UniProtKB.
DR DisProt; DP02644; -.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_03212; NCPR; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR023208; P450R.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000208; P450R; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; FAD;
KW Flavoprotein; FMN; Membrane; NADP; Oxidoreductase;
KW Phenylpropanoid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..711
FT /note="NADPH--cytochrome P450 reductase 2"
FT /id="PRO_0000416840"
FT TOPO_DOM 1..51
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TOPO_DOM 73..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 105..255
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 310..556
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 111..116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 166..169
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 204..213
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 330
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 489..492
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 507..509
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 523..526
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 570
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 631..632
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 637..641
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 673
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 711
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT VAR_SEQ 447
FT /note="K -> KV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042906"
FT CONFLICT 297..298
FT /note="NM -> TL (in Ref. 1; CAA46815)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..348
FT /note="YET -> MKL (in Ref. 1; CAA46815)"
FT /evidence="ECO:0000305"
FT CONFLICT 540..544
FT /note="NCSSA -> KLFLGR (in Ref. 1; CAA46815)"
FT /evidence="ECO:0000305"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 447..453
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 454..458
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 461..467
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 479..482
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 524..531
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 543..549
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 573..586
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 595..602
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 611..619
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 624..635
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 640..646
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 648..656
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:5GXU"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 670..686
FT /evidence="ECO:0007829|PDB:5GXU"
FT HELIX 690..703
FT /evidence="ECO:0007829|PDB:5GXU"
FT STRAND 705..710
FT /evidence="ECO:0007829|PDB:5GXU"
SQ SEQUENCE 711 AA; 78927 MW; F0503108EB7F508F CRC64;
MSSSSSSSTS MIDLMAAIIK GEPVIVSDPA NASAYESVAA ELSSMLIENR QFAMIVTTSI
AVLIGCIVML VWRRSGSGNS KRVEPLKPLV IKPREEEIDD GRKKVTIFFG TQTGTAEGFA
KALGEEAKAR YEKTRFKIVD LDDYAADDDE YEEKLKKEDV AFFFLATYGD GEPTDNAARF
YKWFTEGNDR GEWLKNLKYG VFGLGNRQYE HFNKVAKVVD DILVEQGAQR LVQVGLGDDD
QCIEDDFTAW REALWPELDT ILREEGDTAV ATPYTAAVLE YRVSIHDSED AKFNDINMAN
GNGYTVFDAQ HPYKANVAVK RELHTPESDR SCIHLEFDIA GSGLTYETGD HVGVLCDNLS
ETVDEALRLL DMSPDTYFSL HAEKEDGTPI SSSLPPPFPP CNLRTALTRY ACLLSSPKKS
ALVALAAHAS DPTEAERLKH LASPAGKDEY SKWVVESQRS LLEVMAEFPS AKPPLGVFFA
GVAPRLQPRF YSISSSPKIA ETRIHVTCAL VYEKMPTGRI HKGVCSTWMK NAVPYEKSEN
CSSAPIFVRQ SNFKLPSDSK VPIIMIGPGT GLAPFRGFLQ ERLALVESGV ELGPSVLFFG
CRNRRMDFIY EEELQRFVES GALAELSVAF SREGPTKEYV QHKMMDKASD IWNMISQGAY
LYVCGDAKGM ARDVHRSLHT IAQEQGSMDS TKAEGFVKNL QTSGRYLRDV W
