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Ultraviolet-B receptor UVR8 (Protein UV-B RESISTANCE 8) (RCC1 domain-containing protein UVR8)

 UVR8_ARATH              Reviewed;         440 AA.
Q9FN03; Q9XHD7;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 111.
RecName: Full=Ultraviolet-B receptor UVR8;
AltName: Full=Protein UV-B RESISTANCE 8;
AltName: Full=RCC1 domain-containing protein UVR8;
Name=UVR8; OrderedLocusNames=At5g63860; ORFNames=MGI19.7;
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], DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
196-TRP--ARG-200.
STRAIN=cv. Landsberg erecta;
PubMed=12226503; DOI=10.1104/pp.005041;
Kliebenstein D.J., Lim J.E., Landry L.G., Last R.L.;
"Arabidopsis UVR8 regulates ultraviolet-B signal transduction and
tolerance and contains sequence similarity to human regulator of
chromatin condensation 1.";
Plant Physiol. 130:234-243(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16330762; DOI=10.1073/pnas.0507187102;
Brown B.A., Cloix C., Jiang G.H., Kaiserli E., Herzyk P.,
Kliebenstein D.J., Jenkins G.I.;
"A UV-B-specific signaling component orchestrates plant UV
protection.";
Proc. Natl. Acad. Sci. U.S.A. 102:18225-18230(2005).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17720867; DOI=10.1105/tpc.107.053330;
Kaiserli E., Jenkins G.I.;
"UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B
specific signaling component UVR8 and activates its function in the
nucleus.";
Plant Cell 19:2662-2673(2007).
[7]
FUNCTION.
PubMed=18055587; DOI=10.1104/pp.107.108456;
Brown B.A., Jenkins G.I.;
"UV-B signaling pathways with different fluence-rate response profiles
are distinguished in mature Arabidopsis leaf tissue by requirement for
UVR8, HY5, and HYH.";
Plant Physiol. 146:576-588(2008).
[8]
INTERACTION WITH HISTONE H2B.
PubMed=20031919; DOI=10.1093/mp/ssm012;
Cloix C., Jenkins G.I.;
"Interaction of the Arabidopsis UV-B-specific signaling component UVR8
with chromatin.";
Mol. Plant 1:118-128(2008).
[9]
FUNCTION, AND INTERACTION WITH COP1.
STRAIN=cv. Wassilewskija;
PubMed=19165148; DOI=10.1038/emboj.2009.4;
Favory J.J., Stec A., Gruber H., Rizzini L., Oravecz A., Funk M.,
Albert A., Cloix C., Jenkins G.I., Oakeley E.J., Seidlitz H.K.,
Nagy F., Ulm R.;
"Interaction of COP1 and UVR8 regulates UV-B-induced
photomorphogenesis and stress acclimation in Arabidopsis.";
EMBO J. 28:591-601(2009).
[10]
FUNCTION.
PubMed=19402876; DOI=10.1111/j.1469-8137.2009.02855.x;
Wargent J.J., Gegas V.C., Jenkins G.I., Doonan J.H., Paul N.D.;
"UVR8 in Arabidopsis thaliana regulates multiple aspects of cellular
differentiation during leaf development in response to ultraviolet B
radiation.";
New Phytol. 183:315-326(2009).
[11]
FUNCTION, AND INTERACTION WITH RUP1 AND RUP2.
PubMed=21041653; DOI=10.1073/pnas.0914532107;
Gruber H., Heijde M., Heller W., Albert A., Seidlitz H.K., Ulm R.;
"Negative feedback regulation of UV-B-induced photomorphogenesis and
stress acclimation in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 107:20132-20137(2010).
[12]
FUNCTION.
PubMed=21395889; DOI=10.1111/j.1365-313X.2011.04573.x;
Feher B., Kozma-Bognar L., Kevei E., Hajdu A., Binkert M., Davis S.J.,
Schaefer E., Ulm R., Nagy F.;
"Functional interaction of the circadian clock and UV RESISTANCE LOCUS
8-controlled UV-B signaling pathways in Arabidopsis thaliana.";
Plant J. 67:37-48(2011).
[13]
FUNCTION, SUBUNIT, INTERACTION WITH COP1, AND MUTAGENESIS OF GLY-145;
GLY-202 AND TRP-285.
PubMed=21454788; DOI=10.1126/science.1200660;
Rizzini L., Favory J.J., Cloix C., Faggionato D., O'Hara A.,
Kaiserli E., Baumeister R., Schaefer E., Nagy F., Jenkins G.I.,
Ulm R.;
"Perception of UV-B by the Arabidopsis UVR8 protein.";
Science 332:103-106(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
FUNCTION.
PubMed=22447155; DOI=10.1093/mp/sss025;
Demkura P.V., Ballare C.L.;
"UVR8 mediates UV-B-induced Arabidopsis defense responses against
Botrytis cinerea by controlling sinapate accumulation.";
Mol. Plant 5:642-652(2012).
[16]
FUNCTION.
PubMed=23161229; DOI=10.1007/s11120-012-9785-y;
Davey M.P., Susanti N.I., Wargent J.J., Findlay J.E., Paul Quick W.,
Paul N.D., Jenkins G.I.;
"The UV-B photoreceptor UVR8 promotes photosynthetic efficiency in
Arabidopsis thaliana exposed to elevated levels of UV-B.";
Photosyn. Res. 114:121-131(2012).
[17]
FUNCTION, SUBUNIT, INTERACTION WITH COP1, AND MUTAGENESIS OF TRP-39;
TRP-92; TRP-94; TRP-144; TRP-196; TRP-198; TRP-233; TRP-250; TRP-285;
TRP-300; TRP-302; TRP-337; TRP-352 AND TRP-400.
PubMed=23012433; DOI=10.1105/tpc.112.101451;
O'Hara A., Jenkins G.I.;
"In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor
UVR8.";
Plant Cell 24:3755-3766(2012).
[18]
FUNCTION, INTERACTION WITH COP1; RUP1 AND RUP2, AND MUTAGENESIS OF
GLY-283.
PubMed=22988111; DOI=10.1073/pnas.1210898109;
Cloix C., Kaiserli E., Heilmann M., Baxter K.J., Brown B.A.,
O'Hara A., Smith B.O., Christie J.M., Jenkins G.I.;
"C-terminal region of the UV-B photoreceptor UVR8 initiates signaling
through interaction with the COP1 protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:16366-16370(2012).
[19]
SUBUNIT.
PubMed=23129206; DOI=10.1104/pp.112.206805;
Heilmann M., Jenkins G.I.;
"Rapid reversion from monomer to dimer regenerates the ultraviolet-B
photoreceptor UV RESISTANCE LOCUS8 in intact Arabidopsis plants.";
Plant Physiol. 161:547-555(2013).
[20]
X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 10-381, SUBUNIT, AND
MUTAGENESIS OF TRP-233; TRP-285 AND TRP-337.
PubMed=22388820; DOI=10.1038/nature10931;
Wu D., Hu Q., Yan Z., Chen W., Yan C., Huang X., Zhang J., Yang P.,
Deng H., Wang J., Deng X., Shi Y.;
"Structural basis of ultraviolet-B perception by UVR8.";
Nature 484:214-219(2012).
[21]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-405, AND SUBUNIT.
PubMed=22323738; DOI=10.1126/science.1218091;
Christie J.M., Arvai A.S., Baxter K.J., Heilmann M., Pratt A.J.,
O'Hara A., Kelly S.M., Hothorn M., Smith B.O., Hitomi K.,
Jenkins G.I., Getzoff E.D.;
"Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated
disruption of cross-dimer salt bridges.";
Science 335:1492-1496(2012).
-!- FUNCTION: UV-B specific signaling component that acts as UV-B
photoreceptor and plays a key role in establishing UV-protective
responses in plants. Upon UV-B irradiation, UVR8 undergoes an
immediate switch from homodimer to monomer, accumulates in the
nucleus, interacts with the photomorphogenic repressor COP1 and
regulates the expression of the transcription factor HY5 by
associating with chromatin (through histone H2B binding) in the
HY5 promoter region. UVR8 is involved in controlling aspects of
leaf growth and morphogenesis in response to UV-B, is required for
normal progression of endocycle and has a regulatory role in
stomatal differentiation. Is required for plant circadian clock
response to photomorphogenic UV-B light, partly through the
transcriptional activation of responsive clock genes. Promotes
photosynthetic efficiency at elevated levels of UV-B. Plays a role
in mediating the effects of UV-B radiation on pathogen resistance
by controlling the expression of the sinapate biosynthetic
pathway. The two tryptophans, Trp-285 and Trp-233, serve
collectively as the UV-B chromophore.
{ECO:0000269|PubMed:16330762, ECO:0000269|PubMed:17720867,
ECO:0000269|PubMed:18055587, ECO:0000269|PubMed:19165148,
ECO:0000269|PubMed:19402876, ECO:0000269|PubMed:21041653,
ECO:0000269|PubMed:21395889, ECO:0000269|PubMed:21454788,
ECO:0000269|PubMed:22447155, ECO:0000269|PubMed:22988111,
ECO:0000269|PubMed:23012433, ECO:0000269|PubMed:23161229}.
-!- SUBUNIT: Homodimer in the absence of UV-B, but absorption of UV-B
induces monomerization of UVR8 and interaction with COP1.
Interacts with RUP1, RUP2 and histone H2B.
{ECO:0000269|PubMed:19165148, ECO:0000269|PubMed:20031919,
ECO:0000269|PubMed:21041653, ECO:0000269|PubMed:21454788,
ECO:0000269|PubMed:22323738, ECO:0000269|PubMed:22388820,
ECO:0000269|PubMed:22988111, ECO:0000269|PubMed:23012433,
ECO:0000269|PubMed:23129206}.
-!- INTERACTION:
P43254:COP1; NbExp=3; IntAct=EBI-2407499, EBI-301649;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Note=UV-B
promotes rapid accumulation of UVR8 in the nucleus.
-!- DISRUPTION PHENOTYPE: Hypersensitivity to UV-B.
{ECO:0000269|PubMed:12226503}.
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EMBL; AF130441; AAD43920.1; -; mRNA.
EMBL; AB007646; BAB11034.1; -; Genomic_DNA.
EMBL; CP002688; AED97805.1; -; Genomic_DNA.
EMBL; AY125497; AAM78089.1; -; mRNA.
EMBL; BT000600; AAN18169.1; -; mRNA.
PIR; T50662; T50662.
RefSeq; NP_201191.1; NM_125781.4.
UniGene; At.49214; -.
PDB; 4D9S; X-ray; 1.70 A; A/B=1-405.
PDB; 4DNU; X-ray; 1.76 A; A=10-381.
PDB; 4DNV; X-ray; 2.00 A; A/B/C/D=12-381.
PDB; 4DNW; X-ray; 1.77 A; A/B=12-385.
PDB; 4NAA; X-ray; 1.67 A; A/B/C/D=13-381.
PDB; 4NBM; X-ray; 1.61 A; A/B/C/D=13-381.
PDB; 4NC4; X-ray; 1.75 A; A/B/C/D=13-381.
PDBsum; 4D9S; -.
PDBsum; 4DNU; -.
PDBsum; 4DNV; -.
PDBsum; 4DNW; -.
PDBsum; 4NAA; -.
PDBsum; 4NBM; -.
PDBsum; 4NC4; -.
ProteinModelPortal; Q9FN03; -.
SMR; Q9FN03; -.
BioGrid; 21748; 8.
DIP; DIP-59667N; -.
IntAct; Q9FN03; 1.
MINT; MINT-7033609; -.
STRING; 3702.AT5G63860.1; -.
iPTMnet; Q9FN03; -.
PaxDb; Q9FN03; -.
PRIDE; Q9FN03; -.
EnsemblPlants; AT5G63860.1; AT5G63860.1; AT5G63860.
GeneID; 836506; -.
Gramene; AT5G63860.1; AT5G63860.1; AT5G63860.
KEGG; ath:AT5G63860; -.
Araport; AT5G63860; -.
TAIR; locus:2163986; AT5G63860.
eggNOG; KOG1426; Eukaryota.
eggNOG; COG5184; LUCA.
HOGENOM; HOG000240817; -.
InParanoid; Q9FN03; -.
OMA; RHTMAAD; -.
OrthoDB; EOG0936083F; -.
PhylomeDB; Q9FN03; -.
PRO; PR:Q9FN03; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FN03; baseline and differential.
Genevisible; Q9FN03; AT.
GO; GO:0000785; C:chromatin; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003682; F:chromatin binding; IDA:TAIR.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:TAIR.
GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
GO; GO:0009649; P:entrainment of circadian clock; IMP:TAIR.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0009411; P:response to UV; IMP:TAIR.
GO; GO:0010224; P:response to UV-B; IGI:TAIR.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
InterPro; IPR032996; UVR8.
PANTHER; PTHR22870:SF297; PTHR22870:SF297; 1.
Pfam; PF00415; RCC1; 7.
PRINTS; PR00633; RCCNDNSATION.
SUPFAM; SSF50985; SSF50985; 1.
PROSITE; PS00626; RCC1_2; 5.
PROSITE; PS50012; RCC1_3; 7.
1: Evidence at protein level;
3D-structure; Acetylation; Chromophore; Complete proteome; Cytoplasm;
Nucleus; Photoreceptor protein; Receptor; Reference proteome; Repeat;
Sensory transduction.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 440 Ultraviolet-B receptor UVR8.
/FTId=PRO_0000421722.
REPEAT 32 84 RCC1 1.
REPEAT 86 137 RCC1 2.
REPEAT 139 189 RCC1 3.
REPEAT 190 241 RCC1 4.
REPEAT 243 293 RCC1 5.
REPEAT 294 345 RCC1 6.
REPEAT 347 399 RCC1 7.
REGION 397 423 Required for interaction with COP1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 39 39 W->A: Loss of function, homodimerization
and interaction with COP1.
{ECO:0000269|PubMed:23012433}.
MUTAGEN 39 39 W->F: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 39 39 W->Y: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 92 92 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 94 94 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 144 144 W->A: Cannot interact with COP1.
{ECO:0000269|PubMed:23012433}.
MUTAGEN 144 144 W->F: No effect on the interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 144 144 W->Y: No effect on the interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 145 145 G->S: In uvr8-15; loss of function and
interaction with COP1.
{ECO:0000269|PubMed:21454788}.
MUTAGEN 196 200 Missing: In uvr8-1; loss of function.
{ECO:0000269|PubMed:12226503}.
MUTAGEN 196 196 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 198 198 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 202 202 G->R: In uvr8-9; loss of function and
interaction with COP1.
{ECO:0000269|PubMed:21454788}.
MUTAGEN 233 233 W->A: Reduces response to UV-B.
{ECO:0000269|PubMed:22388820,
ECO:0000269|PubMed:23012433}.
MUTAGEN 250 250 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 283 283 G->E: In uvr8-5; loss of response to UV-
B. {ECO:0000269|PubMed:22988111}.
MUTAGEN 285 285 W->A: Loss of function. Constitutive
monomer. {ECO:0000269|PubMed:21454788,
ECO:0000269|PubMed:22388820,
ECO:0000269|PubMed:23012433}.
MUTAGEN 285 285 W->F: Loss of function. Constitutive
homodimer and no interaction with COP1.
{ECO:0000269|PubMed:21454788,
ECO:0000269|PubMed:22388820,
ECO:0000269|PubMed:23012433}.
MUTAGEN 300 300 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 302 302 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 337 337 W->A: Reduces response to UV-B.
{ECO:0000269|PubMed:22388820,
ECO:0000269|PubMed:23012433}.
MUTAGEN 352 352 W->A: Cannot interact with COP1.
{ECO:0000269|PubMed:23012433}.
MUTAGEN 352 352 W->F: No effect on the interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 352 352 W->Y: No effect on the interaction with
COP1. {ECO:0000269|PubMed:23012433}.
MUTAGEN 400 400 W->A: No effect on function,
homodimerization and interaction with
COP1. {ECO:0000269|PubMed:23012433}.
CONFLICT 173 173 R -> P (in Ref. 1; AAD43920).
{ECO:0000305}.
STRAND 17 22 {ECO:0000244|PDB:4NBM}.
STRAND 24 31 {ECO:0000244|PDB:4NBM}.
TURN 32 34 {ECO:0000244|PDB:4NBM}.
STRAND 35 40 {ECO:0000244|PDB:4NBM}.
STRAND 49 51 {ECO:0000244|PDB:4NBM}.
STRAND 55 60 {ECO:0000244|PDB:4NBM}.
HELIX 62 64 {ECO:0000244|PDB:4NBM}.
STRAND 69 74 {ECO:0000244|PDB:4NBM}.
STRAND 76 83 {ECO:0000244|PDB:4NBM}.
TURN 84 87 {ECO:0000244|PDB:4NBM}.
STRAND 88 93 {ECO:0000244|PDB:4NBM}.
HELIX 96 98 {ECO:0000244|PDB:4NBM}.
STRAND 102 104 {ECO:0000244|PDB:4NBM}.
STRAND 108 113 {ECO:0000244|PDB:4NBM}.
HELIX 115 117 {ECO:0000244|PDB:4NBM}.
STRAND 122 127 {ECO:0000244|PDB:4NBM}.
STRAND 129 136 {ECO:0000244|PDB:4NBM}.
STRAND 141 145 {ECO:0000244|PDB:4NBM}.
STRAND 154 156 {ECO:0000244|PDB:4NBM}.
STRAND 160 165 {ECO:0000244|PDB:4NBM}.
HELIX 167 169 {ECO:0000244|PDB:4NBM}.
STRAND 174 179 {ECO:0000244|PDB:4NBM}.
STRAND 181 188 {ECO:0000244|PDB:4NBM}.
STRAND 193 197 {ECO:0000244|PDB:4NBM}.
STRAND 205 209 {ECO:0000244|PDB:4NBM}.
STRAND 212 217 {ECO:0000244|PDB:4NBM}.
STRAND 226 231 {ECO:0000244|PDB:4NBM}.
STRAND 233 240 {ECO:0000244|PDB:4NBM}.
STRAND 245 249 {ECO:0000244|PDB:4NBM}.
STRAND 258 260 {ECO:0000244|PDB:4NBM}.
STRAND 264 269 {ECO:0000244|PDB:4NBM}.
HELIX 271 273 {ECO:0000244|PDB:4NBM}.
STRAND 278 283 {ECO:0000244|PDB:4NBM}.
STRAND 285 292 {ECO:0000244|PDB:4NBM}.
STRAND 297 301 {ECO:0000244|PDB:4NBM}.
STRAND 310 312 {ECO:0000244|PDB:4NBM}.
STRAND 316 322 {ECO:0000244|PDB:4NBM}.
HELIX 325 327 {ECO:0000244|PDB:4NBM}.
STRAND 330 335 {ECO:0000244|PDB:4NBM}.
STRAND 337 344 {ECO:0000244|PDB:4NBM}.
STRAND 349 353 {ECO:0000244|PDB:4NBM}.
STRAND 361 364 {ECO:0000244|PDB:4NBM}.
STRAND 368 373 {ECO:0000244|PDB:4NBM}.
HELIX 375 377 {ECO:0000244|PDB:4NBM}.
SEQUENCE 440 AA; 47118 MW; D2EA103CCFC92E98 CRC64;
MAEDMAADEV TAPPRKVLII SAGASHSVAL LSGDIVCSWG RGEDGQLGHG DAEDRPSPTQ
LSALDGHQIV SVTCGADHTV AYSQSGMEVY SWGWGDFGRL GHGNSSDLFT PLPIKALHGI
RIKQIACGDS HCLAVTMEGE VQSWGRNQNG QLGLGDTEDS LVPQKIQAFE GIRIKMVAAG
AEHTAAVTED GDLYGWGWGR YGNLGLGDRT DRLVPERVTS TGGEKMSMVA CGWRHTISVS
YSGALYTYGW SKYGQLGHGD LEDHLIPHKL EALSNSFISQ ISGGWRHTMA LTSDGKLYGW
GWNKFGQVGV GNNLDQCSPV QVRFPDDQKV VQVSCGWRHT LAVTERNNVF AWGRGTNGQL
GIGESVDRNF PKIIEALSVD GASGQHIESS NIDPSSGKSW VSPAERYAVV PDETGLTDGS
SKGNGGDISV PQTDVKRVRI


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Catalog number Product name Quantity
EIAAB25874 Influenza resistance protein,Interferon-induced GTP-binding protein Mx1,Mouse,Mus musculus,Mx1,Myxoma resistance protein 1,Myxovirus resistance protein 1
EIAAB34101 CHC1L,CHC1-L,Chromosome condensation 1-like,Homo sapiens,Human,RCBTB2,RCC1 and BTB domain-containing protein 2,RCC1-like G exchanging factor,Regulator of chromosome condensation and BTB domain-contain
EIAAB34098 Mouse,Mus musculus,Rcbtb1,RCC1 and BTB domain-containing protein 1,Regulator of chromosome condensation and BTB domain-containing protein 1
20-783-74648 MOUSE ANTI HUMAN BREAST CANCER RESISTANCE PROTEIN - Placenta-specific ATP-binding cassette transporter; Breast cancer resistance protein; Mitoxantrone resistance-associated protein; CD338 antigen; CDw 1 ml
E2370h Human Hect Domain And RCC1 Like Domain Protein 1 E 96T
E2371h Human Hect Domain And RCC1 Like Domain Protein 2 E 96T
E5786h Human Hect Domain And RCC1 Like Domain Protein 3 E 96T
E4116h Human Hect Domain And RCC1 Like Domain Protein 6 E 96T
E4284h Human Hect Domain And RCC1 Like Domain Protein 4 E 96T
EIAAB25877 Bos taurus,Bovine,Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1
EIAAB25876 Interferon-induced GTP-binding protein Mx1,Mx1,Myxoma resistance protein 1,Myxovirus resistance protein 1,Rat,Rattus norvegicus
EIAAB25875 Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1,Pig,Sus scrofa
EIAAB05298 C1q domain-containing protein 1,C1QDC1,CAPRIN2,Caprin-2,Cytoplasmic activation_proliferation-associated protein 2,EEG1,Gastric cancer multidrug resistance-associated protein,Homo sapiens,Human,KIAA187
EIAAB34100 Chc1l,Chromosome condensation 1-like,Rat,Rattus norvegicus,Rcbtb2,RCC1 and BTB domain-containing protein 2,Regulator of chromosome condensation and BTB domain-containing protein 2
EIAAB34099 Chc1l,Chromosome condensation 1-like,Mouse,Mus musculus,Rcbtb2,RCC1 and BTB domain-containing protein 2,Regulator of chromosome condensation and BTB domain-containing protein 2
E3234h Human RCC1 And BTB Domain Containing Protein 1 ELI 96T
E3235h Human RCC1 And BTB Domain Containing Protein 2 ELI 96T
RCBT2_MOUSE Mouse ELISA Kit FOR RCC1 and BTB domain-containing protein 2 96T
E1622h Mouse ELISA Kit FOR RCC1 domain-containing protein 1 96T
G6765 RCC1 and BTB domain-containing protein 2 (RCBTB2), Rat, ELISA Kit 96T
CSB-EL019504RA Rat RCC1 and BTB domain-containing protein 2(RCBTB2) ELISA kit 96T
EIAAB25880 Homo sapiens,Human,Interferon-induced GTP-binding protein Mx2,Interferon-regulated resistance GTP-binding protein MxB,MX2,Myxovirus resistance protein 2,p78-related protein
G6761 RCC1 and BTB domain-containing protein 1 (RCBTB1), Human, ELISA Kit 96T
CSB-EL019503HU Human RCC1 and BTB domain-containing protein 1(RCBTB1) ELISA kit 96T
CSB-EL019507MO Mouse RCC1 domain-containing protein 1(RCCD1) ELISA kit 96T


 

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