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Protein

Very low-density lipoprotein receptor

Gene

VLDLR

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • lipoprotein particle receptor activity Source: BHF-UCL
  • very-low-density lipoprotein particle receptor activity Source: InterPro

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • lipid transport Source: UniProtKB-KW
  • ventral spinal cord development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cholesterol metabolism, Endocytosis, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Very low-density lipoprotein receptor
Short name:
VLDL receptor
Short name:
VLDL-R
Alternative name(s):
Vitellogenin receptor
Short name:
VTG receptor
Gene namesi
Name:VLDLR
Synonyms:VTGR
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini44 – 785742ExtracellularSequence analysisAdd
BLAST
Transmembranei786 – 80924HelicalSequence analysisAdd
BLAST
Topological domaini810 – 86354CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane, VLDL

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343Sequence analysisAdd
BLAST
Chaini44 – 863820Very low-density lipoprotein receptorPRO_0000017342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 63By similarity
Disulfide bondi58 ↔ 76By similarity
Disulfide bondi70 ↔ 85By similarity
Disulfide bondi90 ↔ 102By similarity
Disulfide bondi97 ↔ 115By similarity
Disulfide bondi109 ↔ 126By similarity
Disulfide bondi131 ↔ 145By similarity
Disulfide bondi138 ↔ 158By similarity
Disulfide bondi152 ↔ 167By similarity
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi172 ↔ 184By similarity
Disulfide bondi179 ↔ 197By similarity
Disulfide bondi191 ↔ 206By similarity
Disulfide bondi211 ↔ 223By similarity
Disulfide bondi218 ↔ 236By similarity
Disulfide bondi230 ↔ 247By similarity
Disulfide bondi257 ↔ 269By similarity
Disulfide bondi264 ↔ 282By similarity
Disulfide bondi276 ↔ 291By similarity
Disulfide bondi296 ↔ 308By similarity
Disulfide bondi303 ↔ 321By similarity
Disulfide bondi315 ↔ 330By similarity
Disulfide bondi336 ↔ 349By similarity
Disulfide bondi344 ↔ 362By similarity
Disulfide bondi356 ↔ 373By similarity
Disulfide bondi378 ↔ 389By similarity
Disulfide bondi385 ↔ 398By similarity
Disulfide bondi400 ↔ 412By similarity
Disulfide bondi418 ↔ 428By similarity
Disulfide bondi424 ↔ 437By similarity
Disulfide bondi439 ↔ 452By similarity
Disulfide bondi726 ↔ 739By similarity
Disulfide bondi735 ↔ 754By similarity
Disulfide bondi756 ↔ 769By similarity
Glycosylationi773 – 7731N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP98165.

Expressioni

Tissue specificityi

Abundant in oocytes; much less in heart and skeletal muscle.

Interactioni

Subunit structurei

Binds to the extracellular matrix protein Reelin. Interacts with LDLRAP1 (By similarity).By similarity

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi9031.ENSGALP00000016512.

Structurei

3D structure databases

ProteinModelPortaliP98165.
SMRiP98165. Positions 131-169, 295-332, 376-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 8739LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini88 – 12841LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini129 – 16941LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini170 – 20839LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini209 – 24941LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini255 – 29339LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini294 – 33239LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini334 – 37340LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini374 – 41340EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini414 – 45340EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati457 – 49842LDL-receptor class B 1Add
BLAST
Repeati499 – 54446LDL-receptor class B 2Add
BLAST
Repeati545 – 58743LDL-receptor class B 3Add
BLAST
Repeati588 – 63144LDL-receptor class B 4Add
BLAST
Repeati632 – 67443LDL-receptor class B 5Add
BLAST
Repeati675 – 71743LDL-receptor class B 6Add
BLAST
Domaini722 – 77049EGF-like 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi822 – 8276Endocytosis signalSequence analysis

Sequence similaritiesi

Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 8 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 6 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPT5. Eukaryota.
ENOG410YQ6J. LUCA.
HOGENOMiHOG000115656.
HOVERGENiHBG006250.
InParanoidiP98165.
KOiK20053.
PhylomeDBiP98165.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 8 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR032931. VLDLR.
[Graphical view]
PANTHERiPTHR10529:SF101. PTHR10529:SF101. 1 hit.
PfamiPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 8 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 8 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 8 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSRQRGDR SAATGGGCGA RRWALPRCGA LCLLLALGCL RTATDGAKAK
60 70 80 90 100
CEESQFQCSN GRCIPLLWKC DGDEDCSDGS DESACVKKTC AESDFVCNSG
110 120 130 140 150
QCVPNRWQCD GDPDCEDGSD ESAELCHMRT CRVNEISCGP QSTQCIPVSW
160 170 180 190 200
KCDGEKDCDS GEDEENCGNV TCSAAEFTCS SGQCISKSFV CNGQDDCSDG
210 220 230 240 250
SDELECAPPT CGVHEFQCKS STCIPISWVC DDDADCSDHS DESLEQCGRQ
260 270 280 290 300
PAPPVKCSTS EVQCGSGECI HKKWRCDGDP DCKDGSDEIN CPSRTCRPDQ
310 320 330 340 350
FRCEDGNCIH GSRQCNGVRD CLDGTDEANC NNVIQCSGPG KFKCRSGECI
360 370 380 390 400
DINKVCNHHG DCKDWSDEPL KECNINECLV NNGGCSHICR DLVIGYECDC
410 420 430 440 450
PAGFELVDRR TCGDIDECQN PGICSQICIN LKGGYKCECS RGYQMDLATG
460 470 480 490 500
VCKAVGKEPC LIFTNRRDIR KIGLERKEYI QLVEQLRNTV ALDADIAEQK
510 520 530 540 550
LYWADFSQKA IFSASIDTRD KVGTHTRILD NIHSPAGIAV DWIYKNIYWT
560 570 580 590 600
DSSAKTISVA SLNGKKRKVL FLSELREPAS IAVDPLSGFM YWSDWGEPAK
610 620 630 640 650
IEKAGMNGFD RQQLVTTEIQ WPNGIALDLV KSRLYWLDSK LHMLSSVDLN
660 670 680 690 700
GQDRRLVLKS HMFLPHPLAL TIFEDRVFWI DGENEAVYGA NKFTGAELVT
710 720 730 740 750
LVNNLNDAQD IIVYHELVQP SGRNWCEENM VNGGCSYLCL PAPQINEHSP
760 770 780 790 800
KYTCTCPAGY FLQEDGLRCG GFNISSVVSE VAARGAAGAW AVLPILLLVT
810 820 830 840 850
AALAGYFMWR NWQHKNMKSM NFDNPVYLKT TEEDLTIDIG RHSGSVGHTY
860
PAISVVSTDD DML
Length:863
Mass (Da):94,905
Last modified:October 1, 1996 - v1
Checksum:i0672A8748F9A2245
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80207 mRNA. Translation: CAA56505.1.
PIRiS51789.
RefSeqiNP_990560.1. NM_205229.1.
UniGeneiGga.679.

Genome annotation databases

GeneIDi396154.
KEGGigga:396154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80207 mRNA. Translation: CAA56505.1.
PIRiS51789.
RefSeqiNP_990560.1. NM_205229.1.
UniGeneiGga.679.

3D structure databases

ProteinModelPortaliP98165.
SMRiP98165. Positions 131-169, 295-332, 376-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000016512.

Proteomic databases

PaxDbiP98165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396154.
KEGGigga:396154.

Organism-specific databases

CTDi7436.

Phylogenomic databases

eggNOGiENOG410IPT5. Eukaryota.
ENOG410YQ6J. LUCA.
HOGENOMiHOG000115656.
HOVERGENiHBG006250.
InParanoidiP98165.
KOiK20053.
PhylomeDBiP98165.

Miscellaneous databases

PROiP98165.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 8 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR032931. VLDLR.
[Graphical view]
PANTHERiPTHR10529:SF101. PTHR10529:SF101. 1 hit.
PfamiPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 8 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 8 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 8 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVLDLR_CHICK
AccessioniPrimary (citable) accession number: P98165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.