RCD1_ARATH
ID RCD1_ARATH Reviewed; 589 AA.
AC Q8RY59; Q93YR6; Q94KU0; Q9FT85; Q9FVR7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Inactive poly [ADP-ribose] polymerase RCD1;
DE AltName: Full=Protein RADICAL-INDUCED CELL DEATH 1;
GN Name=RCD1; Synonyms=ATP8, CEO1; OrderedLocusNames=At1g32230;
GN ORFNames=F3C3.1;
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] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=11018516; DOI=10.1016/s0014-5793(00)02016-0;
RA Belles-Boix E., Babiychuk E., Van Montagu M., Inze D., Kushnir S.;
RT "CEO1, a new protein from Arabidopsis thaliana, protects yeast against
RT oxidative damage.";
RL FEBS Lett. 482:19-24(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH TURNIP CRINKLE
RP VIRUS MOVEMENT PROTEIN P8.
RX PubMed=11297700; DOI=10.1099/0022-1317-82-5-1245;
RA Lin B., Heaton L.A.;
RT "An Arabidopsis thaliana protein interacts with a movement protein of
RT Turnip crinkle virus in yeast cells and in vitro.";
RL J. Gen. Virol. 82:1245-1251(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15208394; DOI=10.1105/tpc.021832;
RA Ahlfors R., Lang S., Overmyer K., Jaspers P., Brosche M., Tauriainen A.,
RA Kollist H., Tuominen H., Belles-Boix E., Piippo M., Inze D., Palva E.T.,
RA Kangasjarvi J.;
RT "Arabidopsis RADICAL-INDUCED CELL DEATH1 belongs to the WWE protein-protein
RT interaction domain protein family and modulates abscisic acid, ethylene,
RT and methyl jasmonate responses.";
RL Plant Cell 16:1925-1937(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY OZONE, AND DISRUPTION PHENOTYPE.
RX PubMed=11041881; DOI=10.2307/3871197;
RA Overmyer K., Tuominen H., Kettunen R., Betz C., Langebartels C.,
RA Sandermann H. Jr., Kangasjaervi J.;
RT "Ozone-sensitive arabidopsis rcd1 mutant reveals opposite roles for
RT ethylene and jasmonate signaling pathways in regulating superoxide-
RT dependent cell death.";
RL Plant Cell 12:1849-1862(2000).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14657410; DOI=10.1104/pp.103.033480;
RA Fujibe T., Saji H., Arakawa K., Yabe N., Takeuchi Y., Yamamoto K.T.;
RT "A methyl viologen-resistant mutant of Arabidopsis, which is allelic to
RT ozone-sensitive rcd1, is tolerant to supplemental ultraviolet-B
RT irradiation.";
RL Plant Physiol. 134:275-285(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15728341; DOI=10.1104/pp.104.055681;
RA Overmyer K., Brosche M., Pellinen R., Kuittinen T., Tuominen H.,
RA Ahlfors R., Keinaenen M., Saarma M., Scheel D., Kangasjaervi J.;
RT "Ozone-induced programmed cell death in the Arabidopsis radical-induced
RT cell death1 mutant.";
RL Plant Physiol. 137:1092-1104(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16926493; DOI=10.1271/bbb.50673;
RA Fujibe T., Saji H., Watahiki M.K., Yamamoto K.T.;
RT "Overexpression of the RADICAL-INDUCED CELL DEATH1 (RCD1) gene of
RT Arabidopsis causes weak rcd1 phenotype with compromised oxidative-stress
RT responses.";
RL Biosci. Biotechnol. Biochem. 70:1827-1831(2006).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19548978; DOI=10.1111/j.1365-313x.2009.03951.x;
RA Jaspers P., Blomster T., Brosche M., Salojaervi J., Ahlfors R.,
RA Vainonen J.P., Reddy R.A., Immink R., Angenent G., Turck F., Overmyer K.,
RA Kangasjaervi J.;
RT "Unequally redundant RCD1 and SRO1 mediate stress and developmental
RT responses and interact with transcription factors.";
RL Plant J. 60:268-279(2009).
RN [12]
RP FUNCTION.
RX PubMed=19625634; DOI=10.1104/pp.109.142786;
RA Teotia S., Lamb R.S.;
RT "The paralogous genes RADICAL-INDUCED CELL DEATH1 and SIMILAR TO RCD ONE1
RT have partially redundant functions during Arabidopsis development.";
RL Plant Physiol. 151:180-198(2009).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=20226034; DOI=10.1186/1471-2164-11-170;
RA Jaspers P., Overmyer K., Wrzaczek M., Vainonen J.P., Blomster T.,
RA Salojaervi J., Reddy R.A., Kangasjaervi J.;
RT "The RST and PARP-like domain containing SRO protein family: analysis of
RT protein structure, function and conservation in land plants.";
RL BMC Genomics 11:170-170(2010).
RN [14]
RP INDUCTION.
RX PubMed=19943170; DOI=10.1007/s00425-009-1070-8;
RA Xu J., Yin H., Liu X., Li X.;
RT "Salt affects plant Cd-stress responses by modulating growth and Cd
RT accumulation.";
RL Planta 231:449-459(2010).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=20009514; DOI=10.4161/psb.5.2.10400;
RA Teotia S., Muthuswamy S., Lamb R.S.;
RT "Radical-induced cell death1 and similar to RCD one1 and the stress-induced
RT morphogenetic response.";
RL Plant Signal. Behav. 5:143-145(2010).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21172813; DOI=10.1093/jxb/erq363;
RA Teotia S., Lamb R.S.;
RT "RCD1 and SRO1 are necessary to maintain meristematic fate in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 62:1271-1284(2011).
RN [17]
RP INTERACTION WITH NAC013 AND NAC046.
RX PubMed=25348421; DOI=10.1042/bj20141045;
RA O'Shea C., Kryger M., Stender E.G., Kragelund B.B., Willemoes M.,
RA Skriver K.;
RT "Protein intrinsic disorder in Arabidopsis NAC transcription factors:
RT transcriptional activation by ANAC013 and ANAC046 and their interactions
RT with RCD1.";
RL Biochem. J. 465:281-294(2015).
CC -!- FUNCTION: Inactive ADP-ribosyltransferase that functions with SRO1 to
CC regulate oxidative stress, hormonal and developmental responses.
CC Required for embryogenesis, vegetative and reproductive development,
CC and abiotic stress responses. May regulate several stress-responsive
CC genes. Seems to play a larger developmental role than SRO1. Does not
CC bind NAD in vitro. {ECO:0000269|PubMed:11018516,
CC ECO:0000269|PubMed:11041881, ECO:0000269|PubMed:14657410,
CC ECO:0000269|PubMed:15208394, ECO:0000269|PubMed:15728341,
CC ECO:0000269|PubMed:16926493, ECO:0000269|PubMed:19548978,
CC ECO:0000269|PubMed:19625634, ECO:0000269|PubMed:20226034,
CC ECO:0000269|PubMed:21172813}.
CC -!- SUBUNIT: Interacts with the transcription factors NAC013/NTL1 and
CC NAC046 (PubMed:25348421). Interacts with dehydration-responsive DREB2
CC proteins and a number of transcription factors belonging to several
CC protein families. Interacts with turnip crinkle virus (TCV) movement
CC protein P8. {ECO:0000269|PubMed:11018516, ECO:0000269|PubMed:11297700,
CC ECO:0000269|PubMed:19548978, ECO:0000269|PubMed:25348421}.
CC -!- INTERACTION:
CC Q8RY59; O80931: AS1; NbExp=2; IntAct=EBI-2118043, EBI-763232;
CC Q8RY59; Q96288: BBX24; NbExp=4; IntAct=EBI-2118043, EBI-631943;
CC Q8RY59; Q9LUA9: COL10; NbExp=3; IntAct=EBI-2118043, EBI-2434870;
CC Q8RY59; O82132: DREB2A; NbExp=3; IntAct=EBI-2118043, EBI-1786840;
CC Q8RY59; Q9LKW9: NHX7; NbExp=5; IntAct=EBI-2118043, EBI-2368285;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16926493,
CC ECO:0000269|PubMed:19548978}. Note=Speckle-like pattern.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RY59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RY59-2; Sequence=VSP_041441;
CC -!- TISSUE SPECIFICITY: Expressed in young developing tissues, such as
CC young leaves and flowers and root tips. In mature plants, expressed in
CC vasculature of leaves and roots, and guard cells.
CC {ECO:0000269|PubMed:11018516, ECO:0000269|PubMed:11041881,
CC ECO:0000269|PubMed:19548978, ECO:0000269|PubMed:21172813}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo proper at the globular
CC stage. Expressed in the embryo until the torpedo stage, after which
CC expression within the procambial strands becomes pronounced.
CC {ECO:0000269|PubMed:21172813}.
CC -!- INDUCTION: By ozone, salt stress and cadmium.
CC {ECO:0000269|PubMed:11041881, ECO:0000269|PubMed:19943170,
CC ECO:0000269|PubMed:20226034}.
CC -!- DISRUPTION PHENOTYPE: Small plants, altered leaf shape and early
CC flowering. Plants lacking RCD1 show enhanced resistance to methyl
CC viologen, tolerance to freezing and supplementary UV-B irradiation,
CC reduced sensitivity to abscisic acid, ethylene and jasmonate, increased
CC sensitivity to ozone and up-regulation of reactive oxygen species
CC scavenging enzymes. {ECO:0000269|PubMed:11041881,
CC ECO:0000269|PubMed:14657410, ECO:0000269|PubMed:15208394,
CC ECO:0000269|PubMed:15728341, ECO:0000269|PubMed:19548978,
CC ECO:0000269|PubMed:20009514, ECO:0000269|PubMed:21172813}.
CC -!- MISCELLANEOUS: Plants overexpressing RCD1 show a weak rcd1 mutant
CC phenotype.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved catalytic triad His-Tyr-Glu of the active
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK54509.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AJ251578; CAC14428.1; -; mRNA.
DR EMBL; AF317898; AAK54509.1; ALT_SEQ; mRNA.
DR EMBL; AY578788; AAS91732.1; -; Genomic_DNA.
DR EMBL; AC084165; AAG23444.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31452.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31453.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57850.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57851.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57852.1; -; Genomic_DNA.
DR EMBL; AY059796; AAL24144.1; -; mRNA.
DR EMBL; AY075633; AAL91641.1; -; mRNA.
DR EMBL; AY142655; AAN13193.1; -; mRNA.
DR PIR; H86446; H86446.
DR RefSeq; NP_001320330.1; NM_001333000.1. [Q8RY59-2]
DR RefSeq; NP_001320331.1; NM_001332998.1. [Q8RY59-2]
DR RefSeq; NP_001320332.1; NM_001332999.1. [Q8RY59-2]
DR RefSeq; NP_564391.1; NM_102956.3. [Q8RY59-1]
DR RefSeq; NP_849739.1; NM_179408.3. [Q8RY59-2]
DR PDB; 5N9Q; NMR; -; A=468-589.
DR PDB; 5NGO; X-ray; 2.50 A; A/B/C/D/E/F/G/H=269-460.
DR PDB; 5OAO; NMR; -; A=500-572.
DR PDBsum; 5N9Q; -.
DR PDBsum; 5NGO; -.
DR PDBsum; 5OAO; -.
DR AlphaFoldDB; Q8RY59; -.
DR SMR; Q8RY59; -.
DR BioGRID; 25349; 34.
DR DIP; DIP-52884N; -.
DR IntAct; Q8RY59; 30.
DR STRING; 3702.AT1G32230.1; -.
DR PaxDb; Q8RY59; -.
DR PRIDE; Q8RY59; -.
DR ProteomicsDB; 236536; -. [Q8RY59-1]
DR EnsemblPlants; AT1G32230.1; AT1G32230.1; AT1G32230. [Q8RY59-1]
DR EnsemblPlants; AT1G32230.2; AT1G32230.2; AT1G32230. [Q8RY59-2]
DR EnsemblPlants; AT1G32230.4; AT1G32230.4; AT1G32230. [Q8RY59-2]
DR EnsemblPlants; AT1G32230.5; AT1G32230.5; AT1G32230. [Q8RY59-2]
DR EnsemblPlants; AT1G32230.6; AT1G32230.6; AT1G32230. [Q8RY59-2]
DR GeneID; 840115; -.
DR Gramene; AT1G32230.1; AT1G32230.1; AT1G32230. [Q8RY59-1]
DR Gramene; AT1G32230.2; AT1G32230.2; AT1G32230. [Q8RY59-2]
DR Gramene; AT1G32230.4; AT1G32230.4; AT1G32230. [Q8RY59-2]
DR Gramene; AT1G32230.5; AT1G32230.5; AT1G32230. [Q8RY59-2]
DR Gramene; AT1G32230.6; AT1G32230.6; AT1G32230. [Q8RY59-2]
DR KEGG; ath:AT1G32230; -.
DR Araport; AT1G32230; -.
DR TAIR; locus:2031700; AT1G32230.
DR eggNOG; ENOG502QZEX; Eukaryota.
DR InParanoid; Q8RY59; -.
DR PhylomeDB; Q8RY59; -.
DR PRO; PR:Q8RY59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY59; baseline and differential.
DR Genevisible; Q8RY59; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010102; P:lateral root morphogenesis; IMP:TAIR.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:TAIR.
DR GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0010193; P:response to ozone; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0000303; P:response to superoxide; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR DisProt; DP01180; -.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR044964; RCD1/SRO1-5.
DR InterPro; IPR022003; RST.
DR InterPro; IPR004170; WWE-dom.
DR PANTHER; PTHR32263; PTHR32263; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF12174; RST; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51879; RST; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein;
KW Host-virus interaction; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..589
FT /note="Inactive poly [ADP-ribose] polymerase RCD1"
FT /id="PRO_0000410418"
FT DOMAIN 64..153
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 248..469
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DOMAIN 501..572
FT /note="RST"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01227"
FT REGION 464..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 485
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11297700,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_041441"
FT CONFLICT 522
FT /note="A -> V (in Ref. 1; CAC14428)"
FT /evidence="ECO:0000305"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 303..323
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5NGO"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:5NGO"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5NGO"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 439..448
FT /evidence="ECO:0007829|PDB:5NGO"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:5N9Q"
FT HELIX 510..517
FT /evidence="ECO:0007829|PDB:5N9Q"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:5N9Q"
FT HELIX 523..537
FT /evidence="ECO:0007829|PDB:5N9Q"
FT HELIX 543..550
FT /evidence="ECO:0007829|PDB:5N9Q"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:5N9Q"
FT HELIX 556..566
FT /evidence="ECO:0007829|PDB:5N9Q"
SQ SEQUENCE 589 AA; 65697 MW; 1803D75683524CDC CRC64;
MEAKIVKVLD SSRCEDGFGK KRKRAASYAA YVTGVSCAKL QNVPPPNGQC QIPDKRRRLE
GENKLSAYEN RSGKALVRYY TYFKKTGIAK RVMMYENGEW NDLPEHVICA IQNELEEKSA
AIEFKLCGHS FILDFLHMQR LDMETGAKTP LAWIDNAGKC FFPEIYESDE RTNYCHHKCV
EDPKQNAPHD IKLRLEIDVN GGETPRLNLE ECSDESGDNM MDDVPLAQRS SNEHYDEATE
DSCSRKLEAA VSKWDETDAI VVSGAKLTGS EVLDKDAVKK MFAVGTASLG HVPVLDVGRF
SSEIAEARLA LFQKQVEITK KHRGDANVRY AWLPAKREVL SAVMMQGLGV GGAFIRKSIY
GVGIHLTAAD CPYFSARYCD VDENGVRYMV LCRVIMGNME LLRGDKAQFF SGGEEYDNGV
DDIESPKNYI VWNINMNTHI FPEFVVRFKL SNLPNAEGNL IAKRDNSGVT LEGPKDLPPQ
LESNQGARGS GSANSVGSST TRPKSPWMPF PTLFAAISHK VAENDMLLIN ADYQQLRDKK
MTRAEFVRKL RVIVGDDLLR STITTLQNQP KSKEIPGSIR DHEEGAGGL
