P98155 (VLDLR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Very low-density lipoprotein receptor
Short name=VLDL receptor
Short name=VLDL-R

Gene names

Name:

VLDLR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	873 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	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. Ref.9 Ref.10
Subcellular location	Membrane; Single-pass type I membrane protein. Membrane › clathrin-coated pit; Single-pass type I membrane protein.
Tissue specificity	Abundant in heart and skeletal muscle; also ovary and kidney; not in liver.
Post-translational modification	Ubiquitinated at Lys-839 by MYLIP leading to degradation. Ref.11
Involvement in disease	Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 1 (CMARQ1) [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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15
Sequence similarities	Contains 3 EGF-like domains. Contains 8 LDL-receptor class A domains. Contains 6 LDL-receptor class B repeats.

Ontologies

Keywords
Biological process	Cholesterol metabolism Endocytosis Lipid metabolism Lipid transport Steroid metabolism Sterol metabolism Transport
Cellular component	Coated pit Membrane VLDL
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Mental retardation
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glycoprotein transport Inferred from direct assay PubMed 10571240. Source: BHF-UCL lipid transport Inferred from electronic annotation. Source: UniProtKB-KW memory Traceable author statement PubMed 7550352. Source: ProtInc negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of dendrite development Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of protein kinase activity Inferred from electronic annotation. Source: Compara ventral spinal cord development Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle clearance Inferred from direct assay PubMed 8083232. Source: BHF-UCL
Cellular_component	coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement PubMed 10380922. Source: ProtInc very-low-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	apolipoprotein binding Inferred from direct assay PubMed 10571240. Source: BHF-UCL calcium ion binding Inferred from electronic annotation. Source: InterPro glycoprotein transporter activity Inferred from direct assay PubMed 10571240. Source: BHF-UCL low-density lipoprotein receptor activity Traceable author statement PubMed 10380922. Source: ProtInc reelin receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL very-low-density lipoprotein particle binding Inferred from direct assay PubMed 10571240. Source: BHF-UCL very-low-density lipoprotein particle receptor activity Inferred from direct assay PubMed 8083232. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P98155-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P98155-2)

The sequence of this isoform differs from the canonical sequence as follows:
     751-779: STATTVTYSETKDTNTTEISATSGLVPGG → R

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 873

846

Very low-density lipoprotein receptor

PRO_0000017343

Regions

Topological domain

28 – 797

770

Extracellular Potential

Transmembrane

798 – 819

22

Helical; Potential

Topological domain

820 – 873

54

Cytoplasmic Potential

Domain

31 – 69

39

LDL-receptor class A 1

Domain

70 – 110

41

LDL-receptor class A 2

Domain

111 – 151

41

LDL-receptor class A 3

Domain

152 – 190

39

LDL-receptor class A 4

Domain

191 – 231

41

LDL-receptor class A 5

Domain

237 – 275

39

LDL-receptor class A 6

Domain

276 – 314

39

LDL-receptor class A 7

Domain

316 – 355

40

LDL-receptor class A 8

Domain

356 – 395

40

EGF-like 1

Domain

396 – 435

40

EGF-like 2; calcium-binding Potential

Repeat

439 – 480

42

LDL-receptor class B 1

Repeat

481 – 524

44

LDL-receptor class B 2

Repeat

525 – 567

43

LDL-receptor class B 3

Repeat

568 – 611

44

LDL-receptor class B 4

Repeat

612 – 654

43

LDL-receptor class B 5

Repeat

655 – 697

43

LDL-receptor class B 6

Domain

702 – 750

49

EGF-like 3

Region

751 – 790

40

Clustered O-linked oligosaccharides

Motif

832 – 837

6

Endocytosis signal Potential

Amino acid modifications

Glycosylation

151

1

N-linked (GlcNAc...) Potential

Glycosylation

765

1

N-linked (GlcNAc...) Potential

Glycosylation

781

1

N-linked (GlcNAc...) Potential

Disulfide bond

33 ↔ 45

By similarity

Disulfide bond

40 ↔ 58

By similarity

Disulfide bond

52 ↔ 67

By similarity

Disulfide bond

72 ↔ 84

By similarity

Disulfide bond

79 ↔ 97

By similarity

Disulfide bond

91 ↔ 108

By similarity

Disulfide bond

113 ↔ 127

Disulfide bond

120 ↔ 140

Disulfide bond

134 ↔ 149

Disulfide bond

154 ↔ 166

By similarity

Disulfide bond

161 ↔ 179

By similarity

Disulfide bond

173 ↔ 188

By similarity

Disulfide bond

193 ↔ 205

By similarity

Disulfide bond

200 ↔ 218

By similarity

Disulfide bond

212 ↔ 229

By similarity

Disulfide bond

239 ↔ 251

By similarity

Disulfide bond

246 ↔ 264

By similarity

Disulfide bond

258 ↔ 273

By similarity

Disulfide bond

278 ↔ 290

By similarity

Disulfide bond

285 ↔ 303

By similarity

Disulfide bond

297 ↔ 312

By similarity

Disulfide bond

318 ↔ 331

By similarity

Disulfide bond

326 ↔ 344

By similarity

Disulfide bond

338 ↔ 355

By similarity

Disulfide bond

360 ↔ 371

By similarity

Disulfide bond

367 ↔ 380

By similarity

Disulfide bond

382 ↔ 394

By similarity

Disulfide bond

400 ↔ 410

By similarity

Disulfide bond

406 ↔ 419

By similarity

Disulfide bond

421 ↔ 434

By similarity

Disulfide bond

706 ↔ 719

By similarity

Disulfide bond

715 ↔ 734

By similarity

Disulfide bond

736 ↔ 749

By similarity

Cross-link

839

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Natural variations

Alternative sequence

751 – 779

29

STATT…LVPGG → R in isoform Short.

VSP_004304

Natural variant

59

1

V → I. Ref.5 Ref.13
Corresponds to variant rs6149 [ dbSNP | Ensembl ].

VAR_011865

Natural variant

262

1

P → H. Ref.5
Corresponds to variant rs34761707 [ dbSNP | Ensembl ].

VAR_025063

Natural variant

379

1

E → K. Ref.13
Corresponds to variant rs6146 [ dbSNP | Ensembl ].

VAR_011866

Natural variant

464

1

L → I. Ref.5
Corresponds to variant rs34753566 [ dbSNP | Ensembl ].

VAR_025064

Natural variant

561

1

I → V. Ref.5
Corresponds to variant rs35724190 [ dbSNP | Ensembl ].

VAR_025065

Natural variant

613

1

R → H. Ref.5
Corresponds to variant rs35948251 [ dbSNP | Ensembl ].

VAR_025066

Natural variant

791

1

V → I. Ref.5
Corresponds to variant rs35334949 [ dbSNP | Ensembl ].

VAR_025067

Experimental info

Mutagenesis

825

1

K → R: Insensitive to MYLIP-triggered degradation; when associated with R-828 and R-839. Ref.11

Mutagenesis

828

1

K → R: Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-839. Ref.11

Mutagenesis

839

1

K → R: Insensitive to MYLIP-triggered degradation. Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-828. Ref.11

Sequence conflict

9

1

L → V in AAA53684. Ref.1

Sequence conflict

13

1

L → V in AAA61344. Ref.4

Sequence conflict

424

1

G → A in AAA53684. Ref.1

Sequence conflict

678

1

L → H in AAA53684. Ref.1

Sequence conflict

766

1

T → S in AAA61344. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

873

Helix Strand Turn

Details...

Turn

115 – 117

3

Beta strand

121 – 125

5

Beta strand

132 – 137

6

Turn

141 – 145

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8BAC29438A78C2B8	FASTA	873	96,098
	10 20 30 40 50 60 MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD 70 80 90 100 110 120 GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG SDESPEQCHM RTCRIHEISC 130 140 150 160 170 180 GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS 190 200 210 220 230 240 DGSDELDCAP PTCGAHEFQC STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP 250 260 270 280 290 300 ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI 310 320 330 340 350 360 RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE PLKECHINEC 370 380 390 400 410 420 LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE 430 440 450 460 470 480 CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA 490 500 510 520 530 540 QKLFWADLSQ KAIFSASIDD KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA 550 560 570 580 590 600 TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ 610 620 630 640 650 660 WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI 670 680 690 700 710 720 DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDM ENGGCEYLCL 730 740 750 760 770 780 PAPQINDHSP KYTCSCPSGY NVEENGRDCQ STATTVTYSE TKDTNTTEIS ATSGLVPGGI 790 800 810 820 830 840 NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT 850 860 870 TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA
	Isoform Short [UniParc]. Checksum: 588311D7C6B2C1FD	FASTA	845	93,383
	10 20 30 40 50 60 MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD 70 80 90 100 110 120 GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG SDESPEQCHM RTCRIHEISC 130 140 150 160 170 180 GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS 190 200 210 220 230 240 DGSDELDCAP PTCGAHEFQC STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP 250 260 270 280 290 300 ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI 310 320 330 340 350 360 RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE PLKECHINEC 370 380 390 400 410 420 LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE 430 440 450 460 470 480 CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA 490 500 510 520 530 540 QKLFWADLSQ KAIFSASIDD KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA 550 560 570 580 590 600 TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ 610 620 630 640 650 660 WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI 670 680 690 700 710 720 DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDM ENGGCEYLCL 730 740 750 760 770 780 PAPQINDHSP KYTCSCPSGY NVEENGRDCQ RINVTTAVSE VSVPPKGTSA AWAILPLLLL 790 800 810 820 830 840 VMAAVGGYLM WRNWQHKNMK SMNFDNPVYL KTTEEDLSID IGRHSASVGH TYPAISVVST DDDLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a cDNA encoding a putative human very low density lipoprotein/apolipoprotein E receptor and assignment of the gene to chromosome 9pter-p23." Gafvels M.E., Caird M., Britt D., Jackson C.L., Patterson D., Strauss J.F. Somat. Cell Mol. Genet. 19:557-569(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"Characterization and tissue-specific expression of the human 'very low density lipoprotein (VLDL) receptor' mRNA." Webb J.C., Patel D.D., Jones M.D., Knight B.L., Soutar A.K. Hum. Mol. Genet. 3:531-537(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	"Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene." Sakai J., Hoshino A., Takahashi S., Miura Y., Ishii H., Suzuki H., Kawarabayasi Y., Yamamoto T. J. Biol. Chem. 269:2173-2182(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	"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." Oka K., Tzung K.W., Sullivan M., Lindsay E., Baldini A., Chan L. Genomics 20:298-300(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[5]	SeattleSNPs variation discovery resource Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-59; HIS-262; ILE-464; VAL-561; HIS-613 AND ILE-791.
[6]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[9]	"A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid." Neumann E., Moser R., Snyers L., Blaas D., Hewat E.A. J. Virol. 77:8504-8511(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRV VP1.
[10]	"The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2." Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J., Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G. J. Biol. Chem. 283:2363-2372(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCSK9.
[11]	"The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2." 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. J. Biol. Chem. 285:19720-19726(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-839 BY MYLIP, GLYCOSYLATION, MUTAGENESIS OF LYS-825; LYS-828 AND LYS-839.
[12]	"X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein." Verdaguer N., Fita I., Reithmayer M., Moser R., Blaas D. Nat. Struct. Mol. Biol. 11:429-434(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 111-151 IN COMPLEX WITH HRV2.
[13]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." 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. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ILE-59 AND LYS-379.
[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]	"Homozygous deletion of the very low density lipoprotein receptor gene causes autosomal recessive cerebellar hypoplasia with cerebral gyral simplification." 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. Am. J. Hum. Genet. 77:477-483(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CMARQ1.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L20470 mRNA. Translation: AAA53684.1.
S73849 mRNA. Translation: AAB31735.1.
D16532 Genomic DNA. Translation: BAA03969.1.
D16493 mRNA. Translation: BAA03945.1.
D16494 mRNA. Translation: BAA03946.1.
L22431 mRNA. Translation: AAA61344.1.
DQ067198 Genomic DNA. Translation: AAY46157.1.
AL450467 Genomic DNA. Translation: CAH72454.1.
CH471071 Genomic DNA. Translation: EAW58805.1.
CH471071 Genomic DNA. Translation: EAW58806.1.
BC136562 mRNA. Translation: AAI36563.1.

IPI

IPI00024273.
IPI00219353.

PIR

A49729.

RefSeq

NP_001018066.1. NM_001018056.1.
NP_003374.3. NM_003383.3.

UniGene

Hs.370422.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V9U	X-ray	3.60	5	111-151	[»]
3DPR	X-ray	3.50	E	113-151	[»]

ProteinModelPortal

P98155.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40925N.

STRING

9606.ENSP00000371532.

PTM databases

PhosphoSite

P98155.

Polymorphism databases

DMDM

1730111.

Proteomic databases

PaxDb

P98155.

PRIDE

P98155.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000382099; ENSP00000371531; ENSG00000147852.
ENST00000382100; ENSP00000371532; ENSG00000147852.

GeneID

7436.

KEGG

hsa:7436.

UCSC

uc003zhk.1. human.

Organism-specific databases

CTD

7436.

GeneCards

GC09P002611.

HGNC

HGNC:12698. VLDLR.

HPA

CAB032462.

MIM

192977. gene.
224050. phenotype.

neXtProt

NX_P98155.

Orphanet

1766. Dysequilibrium syndrome.

PharmGKB

PA37317.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG255913.

HOGENOM

HOG000115656.

HOVERGEN

HBG006250.

InParanoid

P98155.

OMA

SIDIGRH.

OrthoDB

EOG4V6ZFX.

PhylomeDB

P98155.

Enzyme and pathway databases

Pathway_Interaction_DB

lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
reelinpathway. Reelin signaling pathway.

Gene expression databases

ArrayExpress

P98155.

Bgee

P98155.

CleanEx

HS_VLDLR.

Genevestigator

P98155.

GermOnline

ENSG00000147852. Homo sapiens.

Family and domain databases

Gene3D

2.120.10.30. 1 hit.
4.10.400.10. 8 hits.

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]

Pfam

PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]

SMART

SM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 8 hits.
SM00135. LY. 5 hits.
[Graphical view]

SUPFAM

SSF57184. Grow_fac_recept. 1 hit.
SSF57424. LDL_rcpt_classA_cys-rich. 8 hits.

PROSITE

PS00010. ASX_HYDROXYL. 2 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 8 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P98155.

GenomeRNAi

7436.

NextBio

29124.

SOURCE

Search...

Entry information

Entry name

VLDLR_HUMAN

Accession

Primary (citable) accession number: P98155
Secondary accession number(s): B2RMZ7, D3DRH6, Q5VVF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 143 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.