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Coronatine-insensitive protein 1 (COI-1) (F-box/LRR-repeat protein 2) (AtCOI1) (AtFBL2)

 COI1_ARATH              Reviewed;         592 AA.
O04197; B2BD84;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=Coronatine-insensitive protein 1;
AltName: Full=COI-1;
AltName: Full=F-box/LRR-repeat protein 2;
Short=AtCOI1;
Short=AtFBL2;
Name=COI1; Synonyms=FBL2; OrderedLocusNames=At2g39940;
ORFNames=T28M21.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=9582125; DOI=10.1126/science.280.5366.1091;
Xie D., Feys B.F., James S., Nieto-Rostro M., Turner J.G.;
"COI1: an Arabidopsis gene required for jasmonate-regulated defense
and fertility.";
Science 280:1091-1094(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Aa-0, cv. Ak-1, cv. Bay-0, cv. C24, cv. Columbia,
cv. Cvi-0, cv. Di-0, cv. Ei-2, cv. Gu-0, cv. HOG,
cv. Landsberg erecta, cv. Lz-0, cv. Nd-1, cv. Sha, cv. Sorbo,
cv. Tsu-0, cv. Wassilewskija, and cv. Wei-0;
Caldwell K.S., Michelmore R.W.;
"Genes encoding defense signaling proteins in plants show weaker
signatures of selection than those encoding recognition proteins.";
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION.
STRAIN=cv. Columbia;
PubMed=12244256; DOI=10.1105/tpc.6.5.751;
Feys B.J.F., Benedetti C.S., Penfold C.N., Turner J.G.;
"Arabidopsis mutants selected for resistance to the phytotoxin
coronatine are male sterile, insensitive to methyl jasmonate, and
resistant to a bacterial pathogen.";
Plant Cell 6:751-759(1994).
[7]
FUNCTION.
PubMed=10810145; DOI=10.1105/tpc.12.5.707;
Reymond P., Weber H., Damond M., Farmer E.E.;
"Differential gene expression in response to mechanical wounding and
insect feeding in Arabidopsis.";
Plant Cell 12:707-720(2000).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11077244; DOI=10.1016/S1360-1385(00)01769-6;
Xiao W., Jang J.-C.;
"F-box proteins in Arabidopsis.";
Trends Plant Sci. 5:454-457(2000).
[9]
FUNCTION, AND MUTAGENESIS OF LEU-245.
PubMed=12172836; DOI=10.1007/s00425-002-0787-4;
Ellis C., Turner J.G.;
"A conditionally fertile coi1 allele indicates cross-talk between
plant hormone signalling pathways in Arabidopsis thaliana seeds and
young seedlings.";
Planta 215:549-556(2002).
[10]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-22.
PubMed=12172031; DOI=10.1105/tpc.003368;
Xu L., Liu F., Lechner E., Genschik P., Crosby W.L., Ma H., Peng W.,
Huang D., Xie D.;
"The SCF(COI1) ubiquitin-ligase complexes are required for jasmonate
response in Arabidopsis.";
Plant Cell 14:1919-1935(2002).
[11]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-11; TRP-44 AND LEU-245.
PubMed=12445118; DOI=10.1046/j.1365-313X.2002.01432.x;
Devoto A., Nieto-Rostro M., Xie D., Ellis C., Harmston R., Patrick E.,
Davis J., Sherratt L., Coleman M., Turner J.G.;
"COI1 links jasmonate signalling and fertility to the SCF ubiquitin-
ligase complex in Arabidopsis.";
Plant J. 32:457-466(2002).
[12]
DOMAIN LEUCINE-RICH REPEATS.
PubMed=12008900; DOI=10.1023/A:1014440531842;
Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
"Cloning by pathway activation in yeast: identification of an
Arabidopsis thaliana F-box protein that can turn on glucose
repression.";
Plant Mol. Biol. 49:69-79(2002).
[13]
FUNCTION, AND SUBUNIT.
PubMed=12724535; DOI=10.1105/tpc.010207;
Feng S., Ma L., Wang X., Xie D., Dinesh-Kumar S.P., Wei N., Deng X.W.;
"The COP9 signalosome interacts physically with SCF COI1 and modulates
jasmonate responses.";
Plant Cell 15:1083-1094(2003).
[14]
FUNCTION.
PubMed=12805591; DOI=10.1104/pp.103.022186;
van Wees S.C.M., Chang H.-S., Zhu T., Glazebrook J.;
"Characterization of the early response of Arabidopsis to Alternaria
brassicicola infection using expression profiling.";
Plant Physiol. 132:606-617(2003).
[15]
INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2; ASK11 AND ASK12.
PubMed=14749489; DOI=10.1093/pcp/pch009;
Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M.,
Shinozaki K., Shimada H., Matsui M.;
"Expression and interaction analysis of Arabidopsis Skp1-related
genes.";
Plant Cell Physiol. 45:83-91(2004).
[16]
FUNCTION.
PubMed=14756769; DOI=10.1111/j.1365-313X.2003.01986.x;
He P., Chintamanani S., Chen Z., Zhu L., Kunkel B.N., Alfano J.R.,
Tang X., Zhou J.-M.;
"Activation of a COI1-dependent pathway in Arabidopsis by Pseudomonas
syringae type III effectors and coronatine.";
Plant J. 37:589-602(2004).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS)1-592 IN COMPLEX WITH
JASMONOYL-ISOLEUCINE AND CORONATINE, INTERACTION WITH SKP1A AND
TIFY10A, AND MUTAGENESIS OF ARG-85; MET-88; PHE-89; ARG-121; LEU-301;
TYR-302; ARG-326; ARG-348; ARG-351; TYR-386; ARG-409; TYR-444; LEU-469
AND ARG-496.
PubMed=20927106; DOI=10.1038/nature09430;
Sheard L.B., Tan X., Mao H., Withers J., Ben-Nissan G., Hinds T.R.,
Kobayashi Y., Hsu F.F., Sharon M., Browse J., He S.Y., Rizo J.,
Howe G.A., Zheng N.;
"Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-
receptor.";
Nature 468:400-405(2010).
-!- FUNCTION: Required for jasmonate-regulated plant fertility and
defense processes, and for coronatine and/or other elicitors
perceptions/responses. Seems to not be required for meiosis.
Required for the regulation of some genes induced by wounding, but
not for all. Component of SCF(COI1) E3 ubiquitin ligase complexes,
which may mediate the ubiquitination and subsequent proteasomal
degradation of target proteins (probably including the ribulose
bisphosphate carboxylase small chain 1B RBCS-1B and the histone
deacetylase HDA6). These SCF complexes play crucial roles in
regulating response to jasmonate, and their interactions with the
COP9 signalosome (CSN) appear to be important for their activity.
Interacts with TIFY10A and inositol pentakisphosphate to form a
high-affinity jasmonates coreceptor. Involved in the regulation of
plant gene expression during plant-pathogen interactions with
Pseudomonas syringae and Alternaria brassicicola.
{ECO:0000269|PubMed:10810145, ECO:0000269|PubMed:12172031,
ECO:0000269|PubMed:12172836, ECO:0000269|PubMed:12244256,
ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:12724535,
ECO:0000269|PubMed:12805591, ECO:0000269|PubMed:14756769,
ECO:0000269|PubMed:9582125}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of SCF(COI1) E3 ubiquitin ligase complexes at
least composed of ASK1 or ASK2, CUL1, RBX1A or RBX1B and COI1.
Interacts with ASK1 and ASK2, but separately, Binds also to ASK11
and ASK12. Interacts with RBCS-1B and HDA6. SCF complexes interact
with the COP9 signalosome (CSN). Interacts with TIFY10A.
{ECO:0000269|PubMed:12172031, ECO:0000269|PubMed:12445118,
ECO:0000269|PubMed:12724535, ECO:0000269|PubMed:14749489,
ECO:0000269|PubMed:20927106}.
-!- INTERACTION:
Q94AH6:CUL1; NbExp=3; IntAct=EBI-401159, EBI-532411;
Q9FML2:HDA6; NbExp=3; IntAct=EBI-401159, EBI-639608;
Q39255:SKP1A; NbExp=11; IntAct=EBI-401159, EBI-532357;
Q9FHW7:SKP1B; NbExp=6; IntAct=EBI-401159, EBI-604076;
Q9LMA8:TIFY10A; NbExp=10; IntAct=EBI-401159, EBI-1388539;
Q9LVI4:TIFY6B; NbExp=6; IntAct=EBI-401159, EBI-1792431;
Q8W4J8:TIFY7; NbExp=7; IntAct=EBI-401159, EBI-1792583;
-!- DOMAIN: The F-box domain is essential for the formation of
SFC(COI1) complexes. {ECO:0000269|PubMed:12008900}.
-!- DOMAIN: The Leu-rich domain is involved in the interactions with
RBCS-1B and RPD3B. {ECO:0000269|PubMed:12008900}.
-!- DISRUPTION PHENOTYPE: Mutants coi1-1 to coi1-14 are male sterile,
insensitive to MeJA and coronatine, and exhibit enhanced
resistance to Pseudomonas syringae atropurpurea (coronatine
producing strain). Mutant coi1-16 has reduced sensitivity to
jasmonate, but is male fertile when grown below 22 degrees Celsius
and male sterile otherwise. {ECO:0000269|PubMed:9582125}.
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EMBL; AF036340; AAC17498.1; -; mRNA.
EMBL; EF470606; ABR45936.1; -; Genomic_DNA.
EMBL; EF470607; ABR45937.1; -; Genomic_DNA.
EMBL; EF470608; ABR45938.1; -; Genomic_DNA.
EMBL; EF470609; ABR45939.1; -; Genomic_DNA.
EMBL; EF470610; ABR45940.1; -; Genomic_DNA.
EMBL; EF470611; ABR45941.1; -; Genomic_DNA.
EMBL; EF470612; ABR45942.1; -; Genomic_DNA.
EMBL; EF470613; ABR45943.1; -; Genomic_DNA.
EMBL; EF470614; ABR45944.1; -; Genomic_DNA.
EMBL; EF470615; ABR45945.1; -; Genomic_DNA.
EMBL; EF470616; ABR45946.1; -; Genomic_DNA.
EMBL; EF470617; ABR45947.1; -; Genomic_DNA.
EMBL; EF470619; ABR45949.1; -; Genomic_DNA.
EMBL; EF470620; ABR45950.1; -; Genomic_DNA.
EMBL; EF470621; ABR45951.1; -; Genomic_DNA.
EMBL; EF470622; ABR45952.1; -; Genomic_DNA.
EMBL; EF470623; ABR45953.1; -; Genomic_DNA.
EMBL; EF470624; ABR45954.1; -; Genomic_DNA.
EMBL; AF002109; AAB95279.1; -; Genomic_DNA.
EMBL; CP002685; AEC09753.1; -; Genomic_DNA.
EMBL; AY045625; AAK73983.1; -; mRNA.
EMBL; AY133556; AAM91386.1; -; mRNA.
PIR; T52139; T52139.
RefSeq; NP_565919.1; NM_129552.4.
UniGene; At.20831; -.
UniGene; At.71018; -.
PDB; 3OGK; X-ray; 2.80 A; B/D/F/H/J/L/N/P=1-592.
PDB; 3OGL; X-ray; 3.18 A; B/D/F/H/J/L/N/P=1-592.
PDB; 3OGM; X-ray; 3.34 A; B/D/F/H/J/L/N/P=1-592.
PDBsum; 3OGK; -.
PDBsum; 3OGL; -.
PDBsum; 3OGM; -.
ProteinModelPortal; O04197; -.
SMR; O04197; -.
BioGrid; 3919; 21.
DIP; DIP-31324N; -.
IntAct; O04197; 13.
STRING; 3702.AT2G39940.1; -.
PaxDb; O04197; -.
EnsemblPlants; AT2G39940.1; AT2G39940.1; AT2G39940.
GeneID; 818581; -.
Gramene; AT2G39940.1; AT2G39940.1; AT2G39940.
KEGG; ath:AT2G39940; -.
Araport; AT2G39940; -.
TAIR; locus:2061136; AT2G39940.
eggNOG; KOG1947; Eukaryota.
eggNOG; ENOG410XQ54; LUCA.
HOGENOM; HOG000238474; -.
InParanoid; O04197; -.
KO; K13463; -.
OMA; IEHPAHI; -.
OrthoDB; EOG093604QH; -.
PhylomeDB; O04197; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; O04197; -.
PRO; PR:O04197; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O04197; baseline and differential.
Genevisible; O04197; AT.
GO; GO:0009901; P:anther dehiscence; IMP:CACAO.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; TAS:TAIR.
GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IGI:TAIR.
GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
GO; GO:0010218; P:response to far red light; IMP:TAIR.
GO; GO:0009625; P:response to insect; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
GO; GO:0009611; P:response to wounding; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:TAIR.
GO; GO:0009641; P:shade avoidance; IMP:TAIR.
GO; GO:0048443; P:stamen development; IMP:TAIR.
GO; GO:0010118; P:stomatal movement; IMP:TAIR.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR032675; LRR_dom_sf.
1: Evidence at protein level;
3D-structure; Complete proteome; Jasmonic acid signaling pathway;
Leucine-rich repeat; Plant defense; Reference proteome; Repeat;
Ubl conjugation pathway.
CHAIN 1 592 Coronatine-insensitive protein 1.
/FTId=PRO_0000119960.
DOMAIN 16 57 F-box.
REPEAT 58 82 LRR 1.
REPEAT 83 102 LRR 2.
REPEAT 103 120 LRR 3.
REPEAT 121 154 LRR 4.
REPEAT 155 182 LRR 5.
REPEAT 183 210 LRR 6.
REPEAT 211 236 LRR 7.
REPEAT 237 264 LRR 8.
REPEAT 265 283 LRR 8.
REPEAT 284 308 LRR 10.
REPEAT 309 332 LRR 11.
REPEAT 333 368 LRR 12.
REPEAT 369 393 LRR 13.
REPEAT 394 426 LRR 14.
REPEAT 427 456 LRR 15.
REPEAT 457 478 LRR 16.
REPEAT 479 500 LRR 17.
REPEAT 501 524 LRR 18.
COMPBIAS 102 517 Leu-rich.
BINDING 85 85 Jasmonate. {ECO:0000244|PDB:3OGK,
ECO:0000244|PDB:3OGL,
ECO:0000244|PDB:3OGM,
ECO:0000269|PubMed:20927106}.
BINDING 348 348 Jasmonate. {ECO:0000244|PDB:3OGK,
ECO:0000244|PDB:3OGL,
ECO:0000244|PDB:3OGM,
ECO:0000269|PubMed:20927106}.
BINDING 386 386 Jasmonate. {ECO:0000244|PDB:3OGK,
ECO:0000244|PDB:3OGM,
ECO:0000269|PubMed:20927106}.
BINDING 409 409 Jasmonate. {ECO:0000244|PDB:3OGK,
ECO:0000244|PDB:3OGL,
ECO:0000244|PDB:3OGM,
ECO:0000269|PubMed:20927106}.
BINDING 496 496 Jasmonate. {ECO:0000244|PDB:3OGL,
ECO:0000244|PDB:3OGM,
ECO:0000269|PubMed:20927106}.
MUTAGEN 11 11 L->A: No effects on interactions.
{ECO:0000269|PubMed:12445118}.
MUTAGEN 22 22 E->A: Abrogates SFC(COI1) complexes
formation, loss of response to jasmonate.
{ECO:0000269|PubMed:12172031}.
MUTAGEN 44 44 W->A: Abrogates SFC(COI1) complexes
formation and of interactions with RBCS-
1B and RPD3B, loss of response to
jasmonate. {ECO:0000269|PubMed:12445118}.
MUTAGEN 85 85 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 88 88 M->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 89 89 F->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 121 121 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 245 245 L->F: In coi1-16; abrogates interactions
with RBCS-1B and RPD3B (coi1-16).
{ECO:0000269|PubMed:12172836,
ECO:0000269|PubMed:12445118}.
MUTAGEN 301 301 L->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 302 302 Y->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 326 326 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 348 348 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 351 351 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 386 386 Y->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 409 409 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 444 444 Y->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 469 469 L->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
MUTAGEN 496 496 R->A: Loss of interaction with TIFY10A.
{ECO:0000269|PubMed:20927106}.
HELIX 17 19 {ECO:0000244|PDB:3OGK}.
HELIX 21 25 {ECO:0000244|PDB:3OGK}.
HELIX 31 37 {ECO:0000244|PDB:3OGK}.
HELIX 42 51 {ECO:0000244|PDB:3OGK}.
STRAND 54 58 {ECO:0000244|PDB:3OGK}.
HELIX 60 62 {ECO:0000244|PDB:3OGK}.
HELIX 65 71 {ECO:0000244|PDB:3OGK}.
STRAND 76 81 {ECO:0000244|PDB:3OGK}.
HELIX 85 89 {ECO:0000244|PDB:3OGK}.
HELIX 94 96 {ECO:0000244|PDB:3OGL}.
HELIX 101 110 {ECO:0000244|PDB:3OGK}.
STRAND 116 121 {ECO:0000244|PDB:3OGK}.
HELIX 126 136 {ECO:0000244|PDB:3OGK}.
HELIX 137 139 {ECO:0000244|PDB:3OGK}.
STRAND 142 147 {ECO:0000244|PDB:3OGK}.
STRAND 149 152 {ECO:0000244|PDB:3OGK}.
HELIX 153 162 {ECO:0000244|PDB:3OGK}.
STRAND 167 170 {ECO:0000244|PDB:3OGK}.
STRAND 175 177 {ECO:0000244|PDB:3OGK}.
HELIX 182 190 {ECO:0000244|PDB:3OGK}.
STRAND 196 198 {ECO:0000244|PDB:3OGK}.
HELIX 209 218 {ECO:0000244|PDB:3OGK}.
STRAND 224 226 {ECO:0000244|PDB:3OGK}.
HELIX 232 235 {ECO:0000244|PDB:3OGK}.
HELIX 236 241 {ECO:0000244|PDB:3OGK}.
STRAND 247 250 {ECO:0000244|PDB:3OGK}.
STRAND 262 264 {ECO:0000244|PDB:3OGK}.
STRAND 274 277 {ECO:0000244|PDB:3OGK}.
TURN 282 284 {ECO:0000244|PDB:3OGK}.
HELIX 285 294 {ECO:0000244|PDB:3OGK}.
STRAND 297 300 {ECO:0000244|PDB:3OGK}.
HELIX 307 314 {ECO:0000244|PDB:3OGK}.
STRAND 322 326 {ECO:0000244|PDB:3OGK}.
HELIX 327 329 {ECO:0000244|PDB:3OGK}.
HELIX 330 340 {ECO:0000244|PDB:3OGK}.
STRAND 346 350 {ECO:0000244|PDB:3OGK}.
STRAND 355 362 {ECO:0000244|PDB:3OGL}.
HELIX 367 376 {ECO:0000244|PDB:3OGK}.
STRAND 381 388 {ECO:0000244|PDB:3OGK}.
HELIX 392 401 {ECO:0000244|PDB:3OGK}.
STRAND 407 412 {ECO:0000244|PDB:3OGK}.
HELIX 425 434 {ECO:0000244|PDB:3OGK}.
STRAND 440 444 {ECO:0000244|PDB:3OGK}.
HELIX 447 449 {ECO:0000244|PDB:3OGK}.
HELIX 452 460 {ECO:0000244|PDB:3OGK}.
STRAND 467 470 {ECO:0000244|PDB:3OGK}.
HELIX 477 484 {ECO:0000244|PDB:3OGK}.
STRAND 492 497 {ECO:0000244|PDB:3OGK}.
HELIX 502 511 {ECO:0000244|PDB:3OGK}.
STRAND 517 522 {ECO:0000244|PDB:3OGK}.
HELIX 532 535 {ECO:0000244|PDB:3OGK}.
STRAND 540 545 {ECO:0000244|PDB:3OGK}.
STRAND 567 572 {ECO:0000244|PDB:3OGK}.
SEQUENCE 592 AA; 67665 MW; 1DDCF04990144C06 CRC64;
MEDPDIKRCK LSCVATVDDV IEQVMTYITD PKDRDSASLV CRRWFKIDSE TREHVTMALC
YTATPDRLSR RFPNLRSLKL KGKPRAAMFN LIPENWGGYV TPWVTEISNN LRQLKSVHFR
RMIVSDLDLD RLAKARADDL ETLKLDKCSG FTTDGLLSIV THCRKIKTLL MEESSFSEKD
GKWLHELAQH NTSLEVLNFY MTEFAKISPK DLETIARNCR SLVSVKVGDF EILELVGFFK
AAANLEEFCG GSLNEDIGMP EKYMNLVFPR KLCRLGLSYM GPNEMPILFP FAAQIRKLDL
LYALLETEDH CTLIQKCPNL EVLETRNVIG DRGLEVLAQY CKQLKRLRIE RGADEQGMED
EEGLVSQRGL IALAQGCQEL EYMAVYVSDI TNESLESIGT YLKNLCDFRL VLLDREERIT
DLPLDNGVRS LLIGCKKLRR FAFYLRQGGL TDLGLSYIGQ YSPNVRWMLL GYVGESDEGL
MEFSRGCPNL QKLEMRGCCF SERAIAAAVT KLPSLRYLWV QGYRASMTGQ DLMQMARPYW
NIELIPSRRV PEVNQQGEIR EMEHPAHILA YYSLAGQRTD CPTTVRVLKE PI


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