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Embryonic polarity protein dorsal

 DORS_DROME              Reviewed;         999 AA.
P15330; O77088; Q0E8P9; Q6AWP3; Q9VJD9; Q9VJE0;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
18-JUL-2018, entry version 207.
RecName: Full=Embryonic polarity protein dorsal;
Name=dl; ORFNames=CG6667;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=3118464; DOI=10.1126/science.3118464;
Steward R.;
"Dorsal, an embryonic polarity gene in Drosophila, is homologous to
the vertebrate proto-oncogene, c-rel.";
Science 238:692-694(1987).
[2]
SEQUENCE REVISION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=2598266; DOI=10.1016/0092-8674(89)90773-3;
Steward R.;
"Relocalization of the dorsal protein from the cytoplasm to the
nucleus correlates with its function.";
Cell 59:1179-1188(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
STRAIN=Oregon-R;
PubMed=10072776; DOI=10.1016/S0378-1119(98)00595-2;
Gross I., Georgel P., Oertel-Buchheit P., Schnarr M., Reichhart J.-M.;
"Dorsal-B, a splice variant of the Drosophila factor Dorsal, is a
novel Rel/NF-kappaB transcriptional activator.";
Gene 228:233-242(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]
INTERACTION WITH TAMO, AND SUBCELLULAR LOCATION.
PubMed=12653959; DOI=10.1046/j.1365-2443.2002.00634.x;
Minakhina S., Yang J., Steward R.;
"Tamo selectively modulates nuclear import in Drosophila.";
Genes Cells 8:299-310(2003).
[8]
INTERACTION WITH EMB, AND SUBCELLULAR LOCATION.
PubMed=14638854; DOI=10.1083/jcb.200304046;
Roth P., Xylourgidis N., Sabri N., Uv A.E., Fornerod M.,
Samakovlis C.;
"The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the
nuclear envelope and attenuates NES-mediated nuclear export.";
J. Cell Biol. 163:701-706(2003).
[9]
FUNCTION.
PubMed=18000549; DOI=10.1371/journal.pone.0001178;
Ayyar S., Pistillo D., Calleja M., Brookfield A., Gittins K.,
Goldstone C., Simpson P.;
"NF-kappaB/Rel-mediated regulation of the neural fate in Drosophila.";
PLoS ONE 2:E1178-E1178(2007).
[10]
FUNCTION.
PubMed=25477468; DOI=10.1126/science.1258236;
Meyer S.N., Amoyel M., Bergantinos C., de la Cova C., Schertel C.,
Basler K., Johnston L.A.;
"An ancient defense system eliminates unfit cells from developing
tissues during cell competition.";
Science 346:1258236-1258236(2014).
-!- FUNCTION: Embryonic developmental protein (PubMed:2598266,
PubMed:10072776). The lateral or ventral identity of a cell
depends upon the concentration of this protein in its nucleus
during the blastoderm stage (PubMed:2598266). A morphogenetic
protein that specifically binds to the kappa B-related consensus
sequence 5'-GRGAAAANCC-3', located in the enhancer region of
zygotic genes such as Zen, Twist, Snail and Decapentaplegic.
Mediates an immune response in larvae (PubMed:10072776). Part of a
signaling pathway involving NF-kappa-B and Toll-related receptors,
that functions in the apoptosis of unfit cells during cell
competition (PubMed:25477468). May be part of a NF-kappa-B and
Tollo signaling cascade that regulates development of the
peripheral nervous system (PubMed:18000549).
{ECO:0000269|PubMed:10072776, ECO:0000269|PubMed:18000549,
ECO:0000269|PubMed:25477468, ECO:0000269|PubMed:2598266}.
-!- SUBUNIT: Interacts with tamo via the nuclear localization signal.
Interacts with emb, a component of the nuclear pore complex.
{ECO:0000269|PubMed:12653959, ECO:0000269|PubMed:14638854}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-198375, EBI-198375;
Q03017:cact; NbExp=5; IntAct=EBI-198375, EBI-200600;
P98149:Dif; NbExp=2; IntAct=EBI-198375, EBI-188843;
Q05652:pll; NbExp=3; IntAct=EBI-198375, EBI-115059;
Q94527-1:Rel; NbExp=2; IntAct=EBI-198375, EBI-15786027;
Q9W1A4:tamo; NbExp=4; IntAct=EBI-198375, EBI-91385;
P22812:tub; NbExp=4; IntAct=EBI-198375, EBI-93181;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In ventral regions
it is first cytoplasmic, then the protein is relocalized in the
nucleus. Its nuclear localization is essential to its function as
a morphogen. In dorsal regions it remains cytoplasmic. Tamo
negatively regulates nuclear import of dl. Emb in the nuclear pore
complex is responsible for export of dl from the nucleus.
-!- SUBCELLULAR LOCATION: Isoform A: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=C;
IsoId=P15330-1; Sequence=Displayed;
Name=A; Synonyms=B;
IsoId=P15330-2; Sequence=VSP_005581, VSP_005582;
Note=Nuclear localization signal at positions 335-340. Ref.1
(AAA28479) sequence is in conflict in position: 506:Q->QQ.
{ECO:0000305};
-!- TISSUE SPECIFICITY: In unchallenged larvae, expression of both
isoforms is seen in fat body and gut (isoform A is more abundant).
After immune challenge levels of both isoforms are enhanced.
{ECO:0000269|PubMed:10072776}.
-!- DEVELOPMENTAL STAGE: Isoform A is expressed maternally and both
isoforms are expressed zygotically from 6-9 hours embryos through
to adulthood. {ECO:0000269|PubMed:10072776}.
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EMBL; M23702; AAA28479.1; -; mRNA.
EMBL; AF053614; AAC35296.1; -; mRNA.
EMBL; AE014134; AAF53611.1; -; Genomic_DNA.
EMBL; AE014134; AAF53612.1; -; Genomic_DNA.
EMBL; BT015205; AAT94434.1; -; mRNA.
PIR; A30350; A30350.
RefSeq; NP_001163000.1; NM_001169529.1. [P15330-2]
RefSeq; NP_001163001.1; NM_001169530.1. [P15330-2]
RefSeq; NP_001286014.1; NM_001299085.1. [P15330-1]
RefSeq; NP_724052.1; NM_165217.3. [P15330-2]
RefSeq; NP_724053.1; NM_165218.3. [P15330-2]
RefSeq; NP_724054.1; NM_165219.2. [P15330-1]
UniGene; Dm.3233; -.
ProteinModelPortal; P15330; -.
SMR; P15330; -.
BioGrid; 61043; 70.
DIP; DIP-17423N; -.
IntAct; P15330; 56.
STRING; 7227.FBpp0080560; -.
iPTMnet; P15330; -.
PaxDb; P15330; -.
PRIDE; P15330; -.
EnsemblMetazoa; FBtr0081005; FBpp0080558; FBgn0260632. [P15330-2]
EnsemblMetazoa; FBtr0081006; FBpp0080559; FBgn0260632. [P15330-2]
EnsemblMetazoa; FBtr0081007; FBpp0080560; FBgn0260632. [P15330-1]
EnsemblMetazoa; FBtr0301383; FBpp0290597; FBgn0260632. [P15330-2]
EnsemblMetazoa; FBtr0301384; FBpp0290598; FBgn0260632. [P15330-2]
EnsemblMetazoa; FBtr0340250; FBpp0309222; FBgn0260632. [P15330-1]
GeneID; 35047; -.
KEGG; dme:Dmel_CG6667; -.
UCSC; CG6667-RA; d. melanogaster. [P15330-1]
CTD; 35047; -.
FlyBase; FBgn0260632; dl.
eggNOG; ENOG410IG8F; Eukaryota.
eggNOG; ENOG410XT64; LUCA.
GeneTree; ENSGT00500000044765; -.
InParanoid; P15330; -.
KO; K09254; -.
OMA; FNTLPRQ; -.
OrthoDB; EOG091G07RW; -.
PhylomeDB; P15330; -.
Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
Reactome; R-DME-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-DME-202424; Downstream TCR signaling.
Reactome; R-DME-209400; Transcriptional activtion by phosphorylated DL/DIF dimer.
Reactome; R-DME-209406; Degradation of NF-kappa-B inhibitor, CACT.
Reactome; R-DME-209560; NF-kB is activated and signals survival.
Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
Reactome; R-DME-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-DME-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-DME-9020702; Interleukin-1 signaling.
Reactome; R-DME-933542; TRAF6 mediated NF-kB activation.
SignaLink; P15330; -.
ChiTaRS; Dl; fly.
GenomeRNAi; 35047; -.
PRO; PR:P15330; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0260632; -.
ExpressionAtlas; P15330; baseline and differential.
Genevisible; P15330; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0070379; F:high mobility group box 1 binding; IPI:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070491; F:repressing transcription factor binding; IPI:FlyBase.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0009952; P:anterior/posterior pattern specification; TAS:FlyBase.
GO; GO:0006952; P:defense response; TAS:FlyBase.
GO; GO:0009950; P:dorsal/ventral axis specification; TAS:FlyBase.
GO; GO:0009953; P:dorsal/ventral pattern formation; NAS:FlyBase.
GO; GO:0007398; P:ectoderm development; NAS:FlyBase.
GO; GO:0001715; P:ectodermal cell fate specification; TAS:FlyBase.
GO; GO:0007369; P:gastrulation; NAS:FlyBase.
GO; GO:0010004; P:gastrulation involving germ band extension; TAS:FlyBase.
GO; GO:0008354; P:germ cell migration; TAS:FlyBase.
GO; GO:0007507; P:heart development; NAS:FlyBase.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0006955; P:immune response; IEP:FlyBase.
GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
GO; GO:0007498; P:mesoderm development; NAS:FlyBase.
GO; GO:0007501; P:mesodermal cell fate specification; TAS:FlyBase.
GO; GO:0010629; P:negative regulation of gene expression; IDA:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:FlyBase.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:FlyBase.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
GO; GO:0042387; P:plasmatocyte differentiation; IMP:FlyBase.
GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
GO; GO:0035206; P:regulation of hemocyte proliferation; IDA:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:FlyBase.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0008063; P:Toll signaling pathway; TAS:FlyBase.
GO; GO:0007419; P:ventral cord development; NAS:FlyBase.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR24169; PTHR24169; 2.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 999 Embryonic polarity protein dorsal.
/FTId=PRO_0000205164.
DOMAIN 47 342 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
MOTIF 756 773 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 395 464 Gln-rich.
COMPBIAS 635 705 Pro-rich.
MOD_RES 312 312 Phosphoserine; by PKA. {ECO:0000255}.
VAR_SEQ 330 677 GKHTFWNLHRHLKRKPDEDLFQQILRLDAKREVQPPTIEVI
DLDTPKIDVQREIPSEMEFNHEESQQSEPALEQEQSVQQEQ
YTQEQSLQQEQYTQEQSLQQEQYLQQLEQQQSFQLEEPMQQ
DQELPAQQSFDQAIDHLPDHTSDHIPEDMEAADAHAEAEAH
RLRSEQEKEIDTIIDEKVRELEQLDLGQQLEPRPLTANDKI
TEWMKSSEIEQQVHEPSPTAEADVLDSALEISKADKTLDEL
LETVAELDEIYTDFKVQRDTYKNTIQNELAGLQGRAPLQVE
DSFDDAATYTSLQIAFKNPVLIPMDDIMPPTPPMSQCAPED
AHQHYDPVEVNSQARKPETP -> DPAHLRRKRQKTGGDPM
HLLLQQQQKQQLQNDHQDGRQTNMNCWNTQNIPPIKTEPRD
TSPQPFGLSYRAPPELTPSPQPLSPSSNYNHNSTPSPYNMA
SAVTPTNGQQQLMSPNHPQQQQQQQQYGATDLGSNYNPFAQ
QVLAQQQQHQQQQQQHQHQHQQQHQQQQQQQQQQQQQSLQF
HANPFGNPGGNSWESKFSAAAVAAAAATATGAAPANGNSNN
LSNLNNPFTMHNLLTSGGGPGNANNLQWNLTTNHLHNQHTL
HQQQQLQQQQQQQYDNTAPTNNNANLNNNNNNNNTAGNQAD
NNGPTLSNLLSFDSGQLVHINSEDQQILRLNSEDLQISNLS
IST (in isoform A).
{ECO:0000303|PubMed:10072776,
ECO:0000303|PubMed:3118464,
ECO:0000303|Ref.6}.
/FTId=VSP_005581.
VAR_SEQ 678 999 Missing (in isoform A).
{ECO:0000303|PubMed:10072776,
ECO:0000303|PubMed:3118464,
ECO:0000303|Ref.6}.
/FTId=VSP_005582.
CONFLICT 236 236 T -> S (in Ref. 6; AAT94434).
{ECO:0000305}.
CONFLICT 391 391 H -> Q (in Ref. 3; AAC35296).
{ECO:0000305}.
CONFLICT 401 401 L -> F (in Ref. 3; AAC35296).
{ECO:0000305}.
CONFLICT 407 407 V -> SQQEQYTQEQSL (in Ref. 3; AAC35296).
{ECO:0000305}.
CONFLICT 698 699 DK -> EQ (in Ref. 3; AAC35296).
{ECO:0000305}.
CONFLICT 965 999 ASEFDETSAYYAPVDAGEILTPDEVAKRLAAANGI -> PV
NLTRPPPTMLPWMLARF (in Ref. 3; AAC35296).
{ECO:0000305}.
SEQUENCE 999 AA; 111551 MW; E29C6594AC07D662 CRC64;
MFPNQNNGAA PGQGPAVDGQ QSLNYNGLPA QQQQQLAQST KNVRKKPYVK ITEQPAGKAL
RFRYECEGRS AGSIPGVNST PENKTYPTIE IVGYKGRAVV VVSCVTKDTP YRPHPHNLVG
KEGCKKGVCT LEINSETMRA VFSNLGIQCV KKKDIEAALK AREEIRVDPF KTGFSHRFQP
SSIDLNSVRL CFQVFMESEQ KGRFTSPLPP VVSEPIFDKK AMSDLVICRL CSCSATVFGN
TQIILLCEKV AKEDISVRFF EEKNGQSVWE AFGDFQHTDV HKQTAITFKT PRYHTLDITE
PAKVFIQLRR PSDGVTSEAL PFEYVPMDSG KHTFWNLHRH LKRKPDEDLF QQILRLDAKR
EVQPPTIEVI DLDTPKIDVQ REIPSEMEFN HEESQQSEPA LEQEQSVQQE QYTQEQSLQQ
EQYTQEQSLQ QEQYLQQLEQ QQSFQLEEPM QQDQELPAQQ SFDQAIDHLP DHTSDHIPED
MEAADAHAEA EAHRLRSEQE KEIDTIIDEK VRELEQLDLG QQLEPRPLTA NDKITEWMKS
SEIEQQVHEP SPTAEADVLD SALEISKADK TLDELLETVA ELDEIYTDFK VQRDTYKNTI
QNELAGLQGR APLQVEDSFD DAATYTSLQI AFKNPVLIPM DDIMPPTPPM SQCAPEDAHQ
HYDPVEVNSQ ARKPETPMRP VPPVPPAILT IQYPPEEDKL PPLPPKRIRK QDSNAENRSI
EANTVQTKPS TGESPLNKRL PPAPKNPNFN TLPRQKKPGF FSKLFSRRKS KPDLAQGQEN
SSILDSKANS REPSIGHFNM QDPMRASLRS SKSAAPFISN PAPAKSSPVK AKKPGSKLTK
PVGRSVSSVS GKRPAYLNAD VVHIPLKGDS VNSLPQQQRT EGYSQSSTIS VGAGLDRRTA
SALQLADIPI SEGGMELVAI ADRQSLHNLV SSIEGHFNVQ LDPNLDLTEA EHFALYTSIP
PLAAASEFDE TSAYYAPVDA GEILTPDEVA KRLAAANGI


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Catalog number Product name Quantity
30-327 Prd is a pair-rule protein expressed in a segmentally repeating pattern to define the polarity of embryonic segments. 0.05 mg
EIAAB42181 Dorsal prostate transglutaminase,Dorsal protein 1,DP1,Dp1,Protein-glutamine gamma-glutamyltransferase 4,Rat,Rattus norvegicus,TGase-4,Tgm4,Transglutaminase-4
EIAAB11928 Dorsal root ganglia homeobox protein,Dorsal root ganglion 11,Drg11,Drgx,Homeobox protein DRG11,Mouse,Mus musculus,Paired-related homeobox protein-like 1,Prrxl1
EIAAB11926 Dorsal root ganglia homeobox protein,Dorsal root ganglion 11,Drg11,Drgx,Homeobox protein DRG11,Paired-related homeobox protein-like 1,Prrxl1,Rat,Rattus norvegicus
EIAAB13056 Embryonic poly(A)-binding protein 2,Embryonic poly(A)-binding protein type II,Embryonic polyadenylate-binding protein 2,ePABP2,EPABP2,ePABP-2,Homo sapiens,Human,PABPN1L,PABPNL1,Poly(A)-binding protein
EIAAB13057 Embryonic poly(A)-binding protein 2,Embryonic poly(A)-binding protein type II,Embryonic polyadenylate-binding protein 2,ePABP2,Epabp2,ePABP-2,Gm1108,Mouse,Mus musculus,Pabpn1l,Pabpnl1,Poly(A)-binding
EIAAB13055 Embryonic poly(A)-binding protein 2,Embryonic poly(A)-binding protein type II,Embryonic polyadenylate-binding protein 2,ePABP2,Epabp2,ePABP-2,Pabpn1l,Pabpnl1,Poly(A)-binding protein nuclear-like 1,Rat
EIAAB26912 Jac,Jacob protein,Juxtasynaptic attractor of caldendrin on dendritic boutons protein,Nasal embryonic LHRH factor,Nasal embryonic luteinizing hormone-releasing hormone factor,Nelf,Rat,Rattus norvegicus
EIAAB26911 Jac,Jacob protein,Juxtasynaptic attractor of caldendrin on dendritic boutons protein,Mouse,Mus musculus,Nasal embryonic LHRH factor,Nasal embryonic luteinizing hormone-releasing hormone factor,Nelf
BT-240 Bovine Total Protein Dorsal Root Ganglia 0.5mg
BT-240 Bovine Dorsal Root Ganglia Total Protein 0.5mg
EH1769 Segment polarity protein dishevelled homolog DVL-1 Elisa Kit 96T
DRGX_RAT Rat ELISA Kit FOR Dorsal root ganglia homeobox protein 96T
DVL2_HUMAN Human ELISA Kit FOR Segment polarity protein dishevelled homolog DVL-2 96T
G9365 Segment polarity protein dishevelled homolog DVL-1 (DVL1), Rat, ELISA Kit 96T
CSB-EL007284RA Rat Segment polarity protein dishevelled homolog DVL-1(DVL1) ELISA kit 96T
E14442h Human Dorsal Root Ganglia Homeobox Protein ELISA K 96T
CSB-EL007187RA Rat Dorsal root ganglia homeobox protein(DRGX) ELISA kit 96T
E4217h Human Dorsal Repulsive Axon Guidance Protein ELISA 96T
E7847h Human Dorsal Neural Tube Nuclear Protein ELISA Kit 96T
CSB-EL007287HU Human Segment polarity protein dishevelled homolog DVL-3(DVL3) ELISA kit 96T
CSB-EL007284RA Rat Segment polarity protein dishevelled homolog DVL-1(DVL1) ELISA kit SpeciesRat 96T
G9369 Segment polarity protein dishevelled homolog DVL-3 (DVL3), Human, ELISA Kit 96T
G9370 Segment polarity protein dishevelled homolog DVL-3 (DVL3), Mouse, ELISA Kit 96T
G9368 Segment polarity protein dishevelled homolog DVL-2 (DVL2), Mouse, ELISA Kit 96T


 

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