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Low-density lipoprotein receptor-related protein 4 (LRP-4) (LDLR dan)

 LRP4_MOUSE              Reviewed;        1905 AA.
Q8VI56; A2AGT4; Q8BPX5; Q8CBB3; Q8CCP5;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
07-NOV-2018, entry version 153.
RecName: Full=Low-density lipoprotein receptor-related protein 4;
Short=LRP-4;
AltName: Full=LDLR dan;
Flags: Precursor;
Name=Lrp4; Synonyms=Kiaa0816;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
STRAIN=C57BL/6J;
PubMed=16517118; DOI=10.1016/j.ygeno.2006.01.007;
Simon-Chazottes D., Tutois S., Kuehn M., Evans M., Bourgade F.,
Cook S., Davisson M.T., Guenet J.L.;
"Mutations in the gene encoding the low-density lipoprotein receptor
LRP4 cause abnormal limb development in the mouse.";
Genomics 87:673-677(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-566 (ISOFORMS 1/2).
STRAIN=C57BL/6J; TISSUE=Bone, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1905 (ISOFORM 2).
TISSUE=Brain;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[6]
FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, FUNCTION AS RECEPTOR
FOR AGRIN, AND INTERACTION WITH AGRIN AND MUSK.
PubMed=18848351; DOI=10.1016/j.cell.2008.10.002;
Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M.,
Huang J.H., Hubbard S.R., Dustin M.L., Burden S.J.;
"Lrp4 is a receptor for Agrin and forms a complex with MuSK.";
Cell 135:334-342(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION.
PubMed=21471202; DOI=10.1074/jbc.M110.190330;
Leupin O., Piters E., Halleux C., Hu S., Kramer I., Morvan F.,
Bouwmeester T., Schirle M., Bueno-Lozano M., Fuentes F.J., Itin P.H.,
Boudin E., de Freitas F., Jennes K., Brannetti B., Charara N.,
Ebersbach H., Geisse S., Lu C.X., Bauer A., Van Hul W., Kneissel M.;
"Bone overgrowth-associated mutations in the LRP4 gene impair
sclerostin facilitator function.";
J. Biol. Chem. 286:19489-19500(2011).
[9]
INTERACTION WITH MESD, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=24140340; DOI=10.1016/j.febslet.2013.10.001;
Hoshi T., Tezuka T., Yokoyama K., Iemura S., Natsume T., Yamanashi Y.;
"Mesdc2 plays a key role in cell-surface expression of Lrp4 and
postsynaptic specialization in myotubes.";
FEBS Lett. 587:3749-3754(2013).
-!- FUNCTION: Mediates SOST-dependent inhibition of bone formation.
Functions as a specific facilitator of SOST-mediated inhibition of
Wnt signaling. Plays a key role in the formation and the
maintenance of the neuromuscular junction (NMJ), the synapse
between motor neuron and skeletal muscle. Directly binds AGRIN and
recruits it to the MUSK signaling complex. Mediates the AGRIN-
induced phosphorylation of MUSK, the kinase of the complex. The
activation of MUSK in myotubes induces the formation of NMJ by
regulating different processes including the transcription of
specific genes and the clustering of AChR in the postsynaptic
membrane. Alternatively, may be involved in the negative
regulation of the canonical Wnt signaling pathway, being able to
antagonize the LRP6-mediated activation of this pathway. More
generally, has been proposed to function as a cell surface
endocytic receptor binding and internalizing extracellular ligands
for degradation by lysosomes. Plays an essential role in the
process of digit differentiation (PubMed:16517118).
{ECO:0000269|PubMed:16517118, ECO:0000269|PubMed:18848351,
ECO:0000269|PubMed:21471202}.
-!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms
an AGRIN receptor complex that binds AGRIN resulting in activation
of MUSK. Interacts (via the extracellular domain) with SOST; the
interaction facilitates the inhibition of Wnt signaling (By
similarity). Interacts with MESD; the interaction promotes
glycosylation of LRP4 and its cell-surface expression
(PubMed:24140340). {ECO:0000250, ECO:0000269|PubMed:24140340}.
-!- INTERACTION:
P25304:Agrn (xeno); NbExp=3; IntAct=EBI-2106160, EBI-2106099;
Q9ERE7:Mesd; NbExp=2; IntAct=EBI-2106160, EBI-6662606;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24140340};
Single-pass type I membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8VI56-1; Sequence=Displayed;
Name=2;
IsoId=Q8VI56-2; Sequence=VSP_010034;
-!- PTM: N-glycosylation is required for cell surface location.
{ECO:0000269|PubMed:24140340}.
-!- DISEASE: Note=Defects in Lrp4 are the cause of digitation anormale
(dan) phenotype, this mutation is the consequence of a retroviral
insertion. Dan mice shown growth retardation in 10-day-old mice
dan/dan and polysyndactyly (PubMed:16517118). Defects in Lrp4 are
the cause of malformed digits (mdig) phenotype. It is a
spontaneous, autosomal recessive mutation resulting in
polysyndactyly (PubMed:16517118). {ECO:0000269|PubMed:16517118}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC27835.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAC29416.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AF247637; AAL36970.1; -; mRNA.
EMBL; AL732478; CAM24075.1; -; Genomic_DNA.
EMBL; AL691489; CAM24075.1; JOINED; Genomic_DNA.
EMBL; BC132240; AAI32241.1; -; mRNA.
EMBL; AK032360; BAC27835.1; ALT_TERM; mRNA.
EMBL; AK036406; BAC29416.1; ALT_SEQ; mRNA.
EMBL; AK129224; BAC98034.1; -; Transcribed_RNA.
CCDS; CCDS16432.1; -. [Q8VI56-1]
RefSeq; NP_001139329.1; NM_001145857.1.
RefSeq; NP_766256.3; NM_172668.3. [Q8VI56-1]
UniGene; Mm.275149; -.
UniGene; Mm.469960; -.
ProteinModelPortal; Q8VI56; -.
SMR; Q8VI56; -.
IntAct; Q8VI56; 14.
MINT; Q8VI56; -.
STRING; 10090.ENSMUSP00000028689; -.
iPTMnet; Q8VI56; -.
PhosphoSitePlus; Q8VI56; -.
PaxDb; Q8VI56; -.
PeptideAtlas; Q8VI56; -.
PRIDE; Q8VI56; -.
Ensembl; ENSMUST00000028689; ENSMUSP00000028689; ENSMUSG00000027253. [Q8VI56-1]
GeneID; 228357; -.
KEGG; mmu:228357; -.
UCSC; uc008kvx.2; mouse. [Q8VI56-1]
CTD; 4038; -.
MGI; MGI:2442252; Lrp4.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XPR2; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000047507; -.
HOVERGEN; HBG049163; -.
InParanoid; Q8VI56; -.
KO; K20051; -.
OMA; CGRNHFT; -.
OrthoDB; EOG091G0178; -.
PhylomeDB; Q8VI56; -.
TreeFam; TF315253; -.
ChiTaRS; Lrp4; mouse.
PRO; PR:Q8VI56; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027253; Expressed in 237 organ(s), highest expression level in testis.
Genevisible; Q8VI56; MM.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; ISS:UniProtKB.
GO; GO:0048856; P:anatomical structure development; IMP:MGI.
GO; GO:0030509; P:BMP signaling pathway; IEA:InterPro.
GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0060173; P:limb development; ISO:MGI.
GO; GO:0050771; P:negative regulation of axonogenesis; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
GO; GO:1901631; P:positive regulation of presynaptic membrane organization; IDA:UniProtKB.
GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
GO; GO:0097104; P:postsynaptic membrane assembly; IMP:UniProtKB.
GO; GO:0097105; P:presynaptic membrane assembly; IMP:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
GO; GO:0043113; P:receptor clustering; IMP:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IDA:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
CDD; cd00112; LDLa; 7.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR030799; LRP4.
PANTHER; PTHR44017:SF4; PTHR44017:SF4; 1.
Pfam; PF12662; cEGF; 1.
Pfam; PF00057; Ldl_recept_a; 8.
Pfam; PF00058; Ldl_recept_b; 16.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 7.
SMART; SM00179; EGF_CA; 3.
SMART; SM00192; LDLa; 8.
SMART; SM00135; LY; 20.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57424; SSF57424; 8.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 8.
PROSITE; PS50068; LDLRA_2; 8.
PROSITE; PS51120; LDLRB; 20.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
EGF-like domain; Endocytosis; Glycoprotein; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1905 Low-density lipoprotein receptor-related
protein 4.
/FTId=PRO_0000017326.
TOPO_DOM 21 1725 Extracellular. {ECO:0000255}.
TRANSMEM 1726 1746 Helical. {ECO:0000255}.
TOPO_DOM 1747 1905 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 67 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 70 106 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 109 144 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 147 183 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 190 226 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 230 266 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 269 305 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 311 350 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 354 394 EGF-like 1; atypical.
DOMAIN 395 434 EGF-like 2; calcium-binding.
REPEAT 480 522 LDL-receptor class B 1.
REPEAT 523 565 LDL-receptor class B 2.
REPEAT 566 609 LDL-receptor class B 3.
REPEAT 610 652 LDL-receptor class B 4.
REPEAT 653 693 LDL-receptor class B 5.
DOMAIN 698 737 EGF-like 3.
REPEAT 785 827 LDL-receptor class B 6.
REPEAT 828 870 LDL-receptor class B 7.
REPEAT 871 914 LDL-receptor class B 8.
REPEAT 915 956 LDL-receptor class B 9.
REPEAT 957 998 LDL-receptor class B 10.
REPEAT 1093 1135 LDL-receptor class B 11.
REPEAT 1136 1178 LDL-receptor class B 12.
REPEAT 1179 1222 LDL-receptor class B 13.
REPEAT 1223 1263 LDL-receptor class B 14.
REPEAT 1264 1306 LDL-receptor class B 15.
REPEAT 1397 1439 LDL-receptor class B 16.
REPEAT 1440 1482 LDL-receptor class B 17.
REPEAT 1483 1526 LDL-receptor class B 18.
REPEAT 1527 1568 LDL-receptor class B 19.
REPEAT 1569 1610 LDL-receptor class B 20.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 719 719 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 901 901 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1077 1077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1415 1415 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1467 1467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 44 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 34 57 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 51 66 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 71 83 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 78 96 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 90 105 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 110 122 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 117 135 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 129 143 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 148 160 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 155 173 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 167 182 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 191 203 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 198 216 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 210 225 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 231 243 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 238 256 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 250 265 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 270 282 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 277 295 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 289 304 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 312 324 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 319 337 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 331 349 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 358 369 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 365 378 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 380 393 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 399 409 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 405 418 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 420 433 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 702 713 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 709 722 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 724 736 {ECO:0000255|PROSITE-ProRule:PRU00124}.
VAR_SEQ 1564 1620 Missing (in isoform 2).
{ECO:0000303|PubMed:14621295}.
/FTId=VSP_010034.
CONFLICT 196 196 F -> L (in Ref. 4; BAC27835).
{ECO:0000305}.
CONFLICT 325 325 I -> L (in Ref. 4; BAC29416).
{ECO:0000305}.
CONFLICT 380 380 C -> R (in Ref. 1; AAL36970).
{ECO:0000305}.
CONFLICT 682 685 HFPM -> LHTP (in Ref. 5). {ECO:0000305}.
CONFLICT 1330 1330 G -> S (in Ref. 1; AAL36970).
{ECO:0000305}.
SEQUENCE 1905 AA; 211954 MW; 282CA859B76D9BAD CRC64;
MRRWWGALLL GALLCAHGIA SSLECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH
SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG
YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE
SCPSAVPSPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS
GLCINSGWRC DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGINDCGDS SDESPQQNCR PRTGEENCNV
NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG RTCQDVNECA EEGYCSQGCT NTEGAFQCWC
EAGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE
LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL
DGAHRKVLLW QSLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP
NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT
KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY
TCACPTGFRK INSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW
DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI
EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASSRQVIISS
NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGQRIYW
TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP PVTTLCAVEN GGCSHLCLRS
PNPSGFSCTC PTGINLLRDG KTCSPGMNSF LIFARRIDVR MVSLDIPYFA DVVVPINMTM
KNTIAIGVDP LEGKVYWSDS TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW
TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS PVQHPYGLTL
LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ AVDRAQPLGF NKCGSRNGGC
SHLCLPRPSG FSCACPTGIQ LKGDRKTCDP SPETYLLFSS RGSIRRISLD TDDHTDVHVP
VPGLNNVISL DYDSVHGKVY YTDVFLDVIR RADLNGSNME TVIGHGLKTT DGLAVDWVAR
NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN
LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF
ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN
NGGCTHLCFA RASDFVCACP DEPDGHPCSL VPGLVPPAPR ATSMNEKSPV LPNTLPTTLH
SSTTKTRTSL EGAGGRCSER DAQLGLCAHS NEAVPAAPGE GLHVSYAIGG LLSILLILLV
IAALMLYRHR KSKFTDPGMG NLTYSNPSYR TSTQEVKLEA APKPAVYNQL CYKKEGGPDH
SYTKEKIKIV EGIRLLAGDD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT
ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV


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