Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Very low-density lipoprotein receptor (VLDL receptor) (VLDL-R)

 VLDLR_HUMAN             Reviewed;         873 AA.
P98155; B2RMZ7; D3DRH6; Q5VVF6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 183.
RecName: Full=Very low-density lipoprotein receptor;
Short=VLDL receptor;
Short=VLDL-R;
Flags: Precursor;
Name=VLDLR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=8128315; DOI=10.1007/BF01233382;
Gafvels M.E., Caird M., Britt D., Jackson C.L., Patterson D.,
Strauss J.F.;
"Cloning of a cDNA encoding a putative human very low density
lipoprotein/apolipoprotein E receptor and assignment of the gene to
chromosome 9pter-p23.";
Somat. Cell Mol. Genet. 19:557-569(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=8069294; DOI=10.1093/hmg/3.4.531;
Webb J.C., Patel D.D., Jones M.D., Knight B.L., Soutar A.K.;
"Characterization and tissue-specific expression of the human 'very
low density lipoprotein (VLDL) receptor' mRNA.";
Hum. Mol. Genet. 3:531-537(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8294473;
Sakai J., Hoshino A., Takahashi S., Miura Y., Ishii H., Suzuki H.,
Kawarabayasi Y., Yamamoto T.;
"Structure, chromosome location, and expression of the human very low
density lipoprotein receptor gene.";
J. Biol. Chem. 269:2173-2182(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=8020981; DOI=10.1006/geno.1994.1171;
Oka K., Tzung K.W., Sullivan M., Lindsay E., Baldini A., Chan L.;
"Human very-low-density lipoprotein receptor complementary DNA and
deduced amino acid sequence and localization of its gene (VLDLR) to
chromosome band 9p24 by fluorescence in situ hybridization.";
Genomics 20:298-300(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-59; HIS-262;
ILE-464; VAL-561; HIS-613 AND ILE-791.
SeattleSNPs variation discovery resource;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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).
[9]
INTERACTION WITH HRV VP1.
PubMed=12857919; DOI=10.1128/JVI.77.15.8504-8511.2003;
Neumann E., Moser R., Snyers L., Blaas D., Hewat E.A.;
"A cellular receptor of human rhinovirus type 2, the very-low-density
lipoprotein receptor, binds to two neighboring proteins of the viral
capsid.";
J. Virol. 77:8504-8511(2003).
[10]
INTERACTION WITH PCSK9.
PubMed=18039658; DOI=10.1074/jbc.M708098200;
Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J.,
Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G.;
"The proprotein convertase PCSK9 induces the degradation of low
density lipoprotein receptor (LDLR) and its closest family members
VLDLR and ApoER2.";
J. Biol. Chem. 283:2363-2372(2008).
[11]
UBIQUITINATION AT LYS-839 BY MYLIP, GLYCOSYLATION, AND MUTAGENESIS OF
LYS-825; LYS-828 AND LYS-839.
PubMed=20427281; DOI=10.1074/jbc.M110.123729;
Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,
Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D.,
Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.;
"The E3 ubiquitin ligase IDOL induces the degradation of the low
density lipoprotein receptor family members VLDLR and ApoER2.";
J. Biol. Chem. 285:19720-19726(2010).
[12]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 111-151 IN COMPLEX WITH HRV2.
PubMed=15064754; DOI=10.1038/nsmb753;
Verdaguer N., Fita I., Reithmayer M., Moser R., Blaas D.;
"X-ray structure of a minor group human rhinovirus bound to a fragment
of its cellular receptor protein.";
Nat. Struct. Mol. Biol. 11:429-434(2004).
[13]
VARIANTS ILE-59 AND LYS-379.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[14]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[15]
INVOLVEMENT IN CAMRQ1.
PubMed=16080122; DOI=10.1086/444400;
Boycott K.M., Flavelle S., Bureau A., Glass H.C., Fujiwara T.M.,
Wirrell E., Davey K., Chudley A.E., Scott J.N., McLeod D.R.,
Parboosingh J.S.;
"Homozygous deletion of the very low density lipoprotein receptor gene
causes autosomal recessive cerebellar hypoplasia with cerebral gyral
simplification.";
Am. J. Hum. Genet. 77:477-483(2005).
-!- FUNCTION: Binds VLDL and transports it into cells by endocytosis.
In order to be internalized, the receptor-ligand complexes must
first cluster into clathrin-coated pits. Binding to Reelin induces
tyrosine phosphorylation of Dab1 and modulation of Tau
phosphorylation (By similarity). {ECO:0000250}.
-!- SUBUNIT: Binds to the extracellular matrix protein Reelin.
Interacts with VLDLR. Interacts with SNX17 (By similarity).
Interacts with DAB1. Receptor for the minor-group human
rhinoviruses (HRVs); binds protein VP1 through the second and
third LDL-receptor class A domains. Interacts with PCSK9.
{ECO:0000250, ECO:0000269|PubMed:12857919,
ECO:0000269|PubMed:15064754, ECO:0000269|PubMed:18039658}.
-!- INTERACTION:
P30533:LRPAP1; NbExp=4; IntAct=EBI-9004309, EBI-715927;
Q99068:Lrpap1 (xeno); NbExp=2; IntAct=EBI-9004309, EBI-919734;
Q60841:Reln (xeno); NbExp=4; IntAct=EBI-9004309, EBI-9248666;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Membrane, clathrin-coated pit; Single-pass type I
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P98155-1; Sequence=Displayed;
Name=Short;
IsoId=P98155-2; Sequence=VSP_004304;
-!- TISSUE SPECIFICITY: Abundant in heart and skeletal muscle; also
ovary and kidney; not in liver.
-!- PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation.
{ECO:0000269|PubMed:20427281}.
-!- DISEASE: Cerebellar ataxia, mental retardation, and dysequilibrium
syndrome 1 (CAMRQ1) [MIM:224050]: A congenital, non-progressive
cerebellar ataxia associated with disturbed equilibrium, delayed
ambulation, mental retardation, cerebellar hypoplasia and mild
cerebral gyral simplification. Additional features include short
stature, strabismus, pes planus and, rarely, seizures.
{ECO:0000269|PubMed:16080122}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/vldlr/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L20470; AAA53684.1; -; mRNA.
EMBL; S73849; AAB31735.1; -; mRNA.
EMBL; D16532; BAA03969.1; -; Genomic_DNA.
EMBL; D16493; BAA03945.1; -; mRNA.
EMBL; D16494; BAA03946.1; -; mRNA.
EMBL; L22431; AAA61344.1; -; mRNA.
EMBL; DQ067198; AAY46157.1; -; Genomic_DNA.
EMBL; AL450467; CAH72454.1; -; Genomic_DNA.
EMBL; CH471071; EAW58805.1; -; Genomic_DNA.
EMBL; CH471071; EAW58806.1; -; Genomic_DNA.
EMBL; BC136562; AAI36563.1; -; mRNA.
CCDS; CCDS34979.1; -. [P98155-2]
CCDS; CCDS6446.1; -. [P98155-1]
PIR; A49729; A49729.
RefSeq; NP_001018066.1; NM_001018056.2. [P98155-2]
RefSeq; NP_003374.3; NM_003383.4. [P98155-1]
UniGene; Hs.370422; -.
PDB; 1V9U; X-ray; 3.60 A; 5=111-151.
PDB; 3DPR; X-ray; 3.50 A; E=113-151.
PDBsum; 1V9U; -.
PDBsum; 3DPR; -.
ProteinModelPortal; P98155; -.
SMR; P98155; -.
BioGrid; 113277; 12.
DIP; DIP-40925N; -.
IntAct; P98155; 4.
MINT; MINT-111579; -.
STRING; 9606.ENSP00000371532; -.
DrugBank; DB03017; Lauric Acid.
iPTMnet; P98155; -.
PhosphoSitePlus; P98155; -.
BioMuta; VLDLR; -.
DMDM; 1730111; -.
EPD; P98155; -.
MaxQB; P98155; -.
PaxDb; P98155; -.
PeptideAtlas; P98155; -.
PRIDE; P98155; -.
Ensembl; ENST00000382099; ENSP00000371531; ENSG00000147852. [P98155-2]
Ensembl; ENST00000382100; ENSP00000371532; ENSG00000147852. [P98155-1]
GeneID; 7436; -.
KEGG; hsa:7436; -.
UCSC; uc003zhk.2; human. [P98155-1]
CTD; 7436; -.
DisGeNET; 7436; -.
EuPathDB; HostDB:ENSG00000147852.15; -.
GeneCards; VLDLR; -.
GeneReviews; VLDLR; -.
HGNC; HGNC:12698; VLDLR.
HPA; CAB032462; -.
HPA; HPA051312; -.
MalaCards; VLDLR; -.
MIM; 192977; gene.
MIM; 224050; phenotype.
neXtProt; NX_P98155; -.
OpenTargets; ENSG00000147852; -.
Orphanet; 1766; Dysequilibrium syndrome.
PharmGKB; PA37317; -.
eggNOG; ENOG410IPT5; Eukaryota.
eggNOG; ENOG410YQ6J; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000115656; -.
HOVERGEN; HBG006250; -.
InParanoid; P98155; -.
KO; K20053; -.
OMA; HTKCPAS; -.
OrthoDB; EOG091G01MX; -.
PhylomeDB; P98155; -.
TreeFam; TF351700; -.
Reactome; R-HSA-8866376; Reelin signalling pathway.
Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
Reactome; R-HSA-8964046; VLDL clearance.
SIGNOR; P98155; -.
EvolutionaryTrace; P98155; -.
GeneWiki; VLDL_receptor; -.
GenomeRNAi; 7436; -.
PRO; PR:P98155; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000147852; -.
CleanEx; HS_VLDLR; -.
ExpressionAtlas; P98155; baseline and differential.
Genevisible; P98155; HS.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0034185; F:apolipoprotein binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:BHF-UCL.
GO; GO:0034437; F:glycoprotein transporter activity; IDA:BHF-UCL.
GO; GO:0005041; F:low-density lipoprotein receptor activity; TAS:ProtInc.
GO; GO:0038025; F:reelin receptor activity; ISS:BHF-UCL.
GO; GO:0034189; F:very-low-density lipoprotein particle binding; IDA:BHF-UCL.
GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0034436; P:glycoprotein transport; IDA:BHF-UCL.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; TAS:Reactome.
GO; GO:0007613; P:memory; TAS:ProtInc.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:1900006; P:positive regulation of dendrite development; ISS:BHF-UCL.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0021517; P:ventral spinal cord development; IEA:Ensembl.
GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IDA:BHF-UCL.
Gene3D; 2.120.10.30; -; 2.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR032931; VLDLR.
PANTHER; PTHR10529:SF318; PTHR10529:SF318; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 8.
Pfam; PF00058; Ldl_recept_b; 5.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 6.
SMART; SM00179; EGF_CA; 2.
SMART; SM00192; LDLa; 8.
SMART; SM00135; LY; 5.
SUPFAM; SSF57424; SSF57424; 8.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 8.
PROSITE; PS50068; LDLRA_2; 8.
PROSITE; PS51120; LDLRB; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cholesterol metabolism;
Coated pit; Complete proteome; Disulfide bond; EGF-like domain;
Endocytosis; Glycoprotein; Isopeptide bond; Lipid metabolism;
Lipid transport; Membrane; Mental retardation; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Steroid metabolism;
Sterol metabolism; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; VLDL.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 873 Very low-density lipoprotein receptor.
/FTId=PRO_0000017343.
TOPO_DOM 28 797 Extracellular. {ECO:0000255}.
TRANSMEM 798 819 Helical. {ECO:0000255}.
TOPO_DOM 820 873 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 69 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 70 110 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 111 151 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 152 190 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 191 231 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 237 275 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 276 314 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 316 355 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 356 395 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 396 435 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 439 480 LDL-receptor class B 1.
REPEAT 481 524 LDL-receptor class B 2.
REPEAT 525 567 LDL-receptor class B 3.
REPEAT 568 611 LDL-receptor class B 4.
REPEAT 612 654 LDL-receptor class B 5.
REPEAT 655 697 LDL-receptor class B 6.
DOMAIN 702 750 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 751 790 Clustered O-linked oligosaccharides.
MOTIF 832 837 Endocytosis signal. {ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 765 765 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 781 781 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 45 {ECO:0000250}.
DISULFID 40 58 {ECO:0000250}.
DISULFID 52 67 {ECO:0000250}.
DISULFID 72 84 {ECO:0000250}.
DISULFID 79 97 {ECO:0000250}.
DISULFID 91 108 {ECO:0000250}.
DISULFID 113 127
DISULFID 120 140
DISULFID 134 149
DISULFID 154 166 {ECO:0000250}.
DISULFID 161 179 {ECO:0000250}.
DISULFID 173 188 {ECO:0000250}.
DISULFID 193 205 {ECO:0000250}.
DISULFID 200 218 {ECO:0000250}.
DISULFID 212 229 {ECO:0000250}.
DISULFID 239 251 {ECO:0000250}.
DISULFID 246 264 {ECO:0000250}.
DISULFID 258 273 {ECO:0000250}.
DISULFID 278 290 {ECO:0000250}.
DISULFID 285 303 {ECO:0000250}.
DISULFID 297 312 {ECO:0000250}.
DISULFID 318 331 {ECO:0000250}.
DISULFID 326 344 {ECO:0000250}.
DISULFID 338 355 {ECO:0000250}.
DISULFID 360 371 {ECO:0000250}.
DISULFID 367 380 {ECO:0000250}.
DISULFID 382 394 {ECO:0000250}.
DISULFID 400 410 {ECO:0000250}.
DISULFID 406 419 {ECO:0000250}.
DISULFID 421 434 {ECO:0000250}.
DISULFID 706 719 {ECO:0000250}.
DISULFID 715 734 {ECO:0000250}.
DISULFID 736 749 {ECO:0000250}.
CROSSLNK 839 839 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20427281}.
VAR_SEQ 751 779 STATTVTYSETKDTNTTEISATSGLVPGG -> R (in
isoform Short). {ECO:0000305}.
/FTId=VSP_004304.
VARIANT 59 59 V -> I (in dbSNP:rs6149).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.5}.
/FTId=VAR_011865.
VARIANT 262 262 P -> H (in dbSNP:rs34761707).
{ECO:0000269|Ref.5}.
/FTId=VAR_025063.
VARIANT 379 379 E -> K (in dbSNP:rs6146).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_011866.
VARIANT 464 464 L -> I (in dbSNP:rs34753566).
{ECO:0000269|Ref.5}.
/FTId=VAR_025064.
VARIANT 561 561 I -> V (in dbSNP:rs35724190).
{ECO:0000269|Ref.5}.
/FTId=VAR_025065.
VARIANT 613 613 R -> H (in dbSNP:rs35948251).
{ECO:0000269|Ref.5}.
/FTId=VAR_025066.
VARIANT 791 791 V -> I (in dbSNP:rs35334949).
{ECO:0000269|Ref.5}.
/FTId=VAR_025067.
MUTAGEN 825 825 K->R: Insensitive to MYLIP-triggered
degradation; when associated with R-828
and R-839. {ECO:0000269|PubMed:20427281}.
MUTAGEN 828 828 K->R: Insensitive to MYLIP-triggered
degradation; when associated with R-825
and R-839. {ECO:0000269|PubMed:20427281}.
MUTAGEN 839 839 K->R: Insensitive to MYLIP-triggered
degradation. Insensitive to MYLIP-
triggered degradation; when associated
with R-825 and R-828.
{ECO:0000269|PubMed:20427281}.
CONFLICT 9 9 L -> V (in Ref. 1; AAA53684).
{ECO:0000305}.
CONFLICT 13 13 L -> V (in Ref. 4; AAA61344).
{ECO:0000305}.
CONFLICT 424 424 G -> A (in Ref. 1; AAA53684).
{ECO:0000305}.
CONFLICT 678 678 L -> H (in Ref. 1; AAA53684).
{ECO:0000305}.
CONFLICT 766 766 T -> S (in Ref. 4; AAA61344).
{ECO:0000305}.
TURN 115 117 {ECO:0000244|PDB:3DPR}.
STRAND 121 125 {ECO:0000244|PDB:3DPR}.
STRAND 132 137 {ECO:0000244|PDB:3DPR}.
TURN 141 145 {ECO:0000244|PDB:3DPR}.
SEQUENCE 873 AA; 96098 MW; 8BAC29438A78C2B8 CRC64;
MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD
GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG SDESPEQCHM RTCRIHEISC
GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS
DGSDELDCAP PTCGAHEFQC STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP
ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE PLKECHINEC
LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
QKLFWADLSQ KAIFSASIDD KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ
WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDM ENGGCEYLCL
PAPQINDHSP KYTCSCPSGY NVEENGRDCQ STATTVTYSE TKDTNTTEIS ATSGLVPGGI
NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT
TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA


Related products :

Catalog number Product name Quantity
U1009Rb CLIA Oryctolagus cuniculus,Rabbit,Very low-density lipoprotein receptor,VLDL receptor,VLDLR,VLDL-R 96T
E1009h ELISA kit Homo sapiens,Human,Very low-density lipoprotein receptor,VLDL receptor,VLDLR,VLDL-R 96T
E1009Rb ELISA kit Oryctolagus cuniculus,Rabbit,Very low-density lipoprotein receptor,VLDL receptor,VLDLR,VLDL-R 96T
U1009h CLIA Homo sapiens,Human,Very low-density lipoprotein receptor,VLDL receptor,VLDLR,VLDL-R 96T
E1009Rb ELISA Oryctolagus cuniculus,Rabbit,Very low-density lipoprotein receptor,VLDL receptor,VLDLR,VLDL-R 96T
E1009h ELISA Homo sapiens,Human,Very low-density lipoprotein receptor,VLDL receptor,VLDLR,VLDL-R 96T
U1009m CLIA Mouse,Mus musculus,Very low-density lipoprotein receptor,VLDL receptor,Vldlr,VLDL-R 96T
E1009m ELISA Mouse,Mus musculus,Very low-density lipoprotein receptor,VLDL receptor,Vldlr,VLDL-R 96T
E1009r ELISA kit Rat,Rattus norvegicus,Very low-density lipoprotein receptor,VLDL receptor,Vldlr,VLDL-R 96T
E1009r ELISA Rat,Rattus norvegicus,Very low-density lipoprotein receptor,VLDL receptor,Vldlr,VLDL-R 96T
U1009r CLIA Rat,Rattus norvegicus,Very low-density lipoprotein receptor,VLDL receptor,Vldlr,VLDL-R 96T
E1009m ELISA kit Mouse,Mus musculus,Very low-density lipoprotein receptor,VLDL receptor,Vldlr,VLDL-R 96T
U1009c CLIA Chicken,Gallus gallus,Very low-density lipoprotein receptor,Vitellogenin receptor,VLDL receptor,VLDLR,VLDL-R,VTG receptor,VTGR 96T
E1009c ELISA Chicken,Gallus gallus,Very low-density lipoprotein receptor,Vitellogenin receptor,VLDL receptor,VLDLR,VLDL-R,VTG receptor,VTGR 96T
E1009c ELISA kit Chicken,Gallus gallus,Very low-density lipoprotein receptor,Vitellogenin receptor,VLDL receptor,VLDLR,VLDL-R,VTG receptor,VTGR 96T
orb24628 VLDL Receptor antibody Monoclonal Lipoprotein, Very Low Density (VLDL) Receptor, C-terminal is a mouse monoclonal antibody to lipoprotein. 0.2 mg
orb24627 VLDL Receptor antibody Monoclonal Lipoprotein, Very Low Density (VLDL) Receptor, C-terminal is a mouse monoclonal antibody to lipoprotein. 0.2 mg
orb24629 VLDL Receptor antibody Monoclonal Lipoprotein, Very Low Density (VLDL) Receptor is a mouse monoclonal antibody to lipoprotein. 0.2 mg
orb82146 Human VLDL protein Lipoprotein, Very Low Density (VLDL) is a purified lipoprotein. For research use only. 1 mg
orb81992 Human VLDL protein Lipoprotein, Very Low Density (VLDL) is a purified lipoprotein. For research use only. 1 mg
DL-VLDL-Mu Mouse Very Low Density Lipoprotein (VLDL) ELISA Kit 96T
DL-VLDL-Hu Human Very Low Density Lipoprotein (VLDL) ELISA Kit 96T
H01241M Lipoprotein, Very Low Density (VLDL) Receptor host: Mouse 0.2mg
H01240M Lipoprotein, Very Low Density (VLDL) Receptor, C-terminal host: Mouse 0.2mg
H01239M Lipoprotein, Very Low Density (VLDL) Receptor, C-terminal host: Mouse 0.2mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur