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Q91ZX7

- LRP1_MOUSE

UniProt

Q91ZX7 - LRP1_MOUSE

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Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

Lrp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.
Functions as a receptor for Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi872 – 8721Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi875 – 8751Calcium 1By similarity
Metal bindingi877 – 8771Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi879 – 8791Calcium 1By similarity
Metal bindingi885 – 8851Calcium 1By similarity
Metal bindingi886 – 8861Calcium 1By similarity
Metal bindingi1033 – 10331Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi1036 – 10361Calcium 2By similarity
Metal bindingi1038 – 10381Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi1040 – 10401Calcium 2By similarity
Metal bindingi1046 – 10461Calcium 2By similarity
Metal bindingi1047 – 10471Calcium 2By similarity
Metal bindingi1081 – 10811Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1084 – 10841Calcium 3By similarity
Metal bindingi1086 – 10861Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1088 – 10881Calcium 3By similarity
Metal bindingi1094 – 10941Calcium 3By similarity
Metal bindingi1095 – 10951Calcium 3By similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. aorta morphogenesis Source: BHF-UCL
  3. apoptotic cell clearance Source: MGI
  4. beta-amyloid clearance Source: BHF-UCL
  5. cell proliferation Source: Ensembl
  6. cholesterol metabolic process Source: MGI
  7. lipoprotein metabolic process Source: Ensembl
  8. negative regulation of neuron apoptotic process Source: Ensembl
  9. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: BHF-UCL
  10. negative regulation of smooth muscle cell migration Source: BHF-UCL
  11. negative regulation of Wnt signaling pathway Source: MGI
  12. positive regulation of cholesterol efflux Source: BHF-UCL
  13. positive regulation of lipid transport Source: BHF-UCL
  14. positive regulation of protein transport Source: Ensembl
  15. protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
  16. receptor-mediated endocytosis Source: MGI
  17. regulation of actin cytoskeleton organization Source: BHF-UCL
  18. regulation of cholesterol transport Source: BHF-UCL
  19. regulation of phospholipase A2 activity Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196575. Scavenging of heme from plasma.
REACT_198569. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolow-density lipoprotein receptor-related protein 1
Short name:
LRP-1
Alternative name(s):
Alpha-2-macroglobulin receptor
Short name:
A2MR
CD_antigen: CD91
Cleaved into the following 3 chains:
Gene namesi
Name:Lrp1Imported
Synonyms:A2mrImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:96828. Lrp1.

Subcellular locationi

Chain Low-density lipoprotein receptor-related protein 1 intracellular domain : Cytoplasm By similarity. Nucleus By similarity
Note: After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.By similarity

GO - Cellular componenti

  1. clathrin-coated vesicle Source: Ensembl
  2. coated pit Source: UniProtKB-KW
  3. dendrite Source: Ensembl
  4. endosome Source: Ensembl
  5. integral component of plasma membrane Source: UniProtKB
  6. lysosomal membrane Source: Ensembl
  7. membrane Source: MGI
  8. neuronal cell body Source: Ensembl
  9. nucleus Source: UniProtKB-KW
  10. perinuclear region of cytoplasm Source: MGI
  11. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death during early embryogenesis around 14 dpc.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 45454526Prolow-density lipoprotein receptor-related protein 1PRO_0000273273Add
BLAST
Chaini20 – ?39443925Low-density lipoprotein receptor-related protein 1 515 kDa subunitPRO_0000302753Add
BLAST
Chaini?3945 – 4545601Low-density lipoprotein receptor-related protein 1 85 kDa subunitPRO_0000302754Add
BLAST
Chaini?4442 – 4545104Low-density lipoprotein receptor-related protein 1 intracellular domainPRO_0000302755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 41By similarity
Disulfide bondi35 ↔ 54By similarity
Disulfide bondi48 ↔ 65By similarity
Disulfide bondi73 ↔ 86By similarity
Disulfide bondi80 ↔ 99By similarity
Disulfide bondi93 ↔ 109By similarity
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi116 ↔ 125By similarity
Disulfide bondi121 ↔ 134By similarity
Disulfide bondi136 ↔ 149By similarity
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi155 ↔ 165By similarity
Disulfide bondi161 ↔ 174By similarity
Disulfide bondi176 ↔ 189By similarity
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi447 – 4471N-linked (GlcNAc...)1 Publication
Disulfide bondi479 ↔ 494By similarity
Disulfide bondi490 ↔ 505By similarity
Disulfide bondi507 ↔ 520By similarity
Glycosylationi730 – 7301N-linked (GlcNAc...)1 Publication
Disulfide bondi808 ↔ 819By similarity
Disulfide bondi815 ↔ 828By similarity
Disulfide bondi830 ↔ 843By similarity
Disulfide bondi855 ↔ 867By similarity
Disulfide bondi862 ↔ 880By similarity
Disulfide bondi874 ↔ 891By similarity
Disulfide bondi896 ↔ 908By similarity
Disulfide bondi903 ↔ 921By similarity
Disulfide bondi915 ↔ 932By similarity
Glycosylationi929 – 9291N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi937 ↔ 949By similarity
Disulfide bondi944 ↔ 962By similarity
Disulfide bondi956 ↔ 972By similarity
Disulfide bondi977 ↔ 990By similarity
Disulfide bondi985 ↔ 1003By similarity
Disulfide bondi997 ↔ 1012By similarity
Disulfide bondi1016 ↔ 1028By similarity
Disulfide bondi1023 ↔ 1041By similarity
Disulfide bondi1035 ↔ 1052By similarity
Glycosylationi1051 – 10511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1063 ↔ 1076By similarity
Disulfide bondi1070 ↔ 1089By similarity
Disulfide bondi1083 ↔ 1098By similarity
Disulfide bondi1105 ↔ 1119By similarity
Disulfide bondi1113 ↔ 1132By similarity
Disulfide bondi1126 ↔ 1141By similarity
Disulfide bondi1146 ↔ 1160By similarity
Disulfide bondi1153 ↔ 1173By similarity
Glycosylationi1155 – 11551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1156 – 11561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1167 ↔ 1183By similarity
Disulfide bondi1186 ↔ 1197By similarity
Disulfide bondi1193 ↔ 1207By similarity
Glycosylationi1196 – 11961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1209 ↔ 1222By similarity
Glycosylationi1219 – 12191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1228 ↔ 1238By similarity
Disulfide bondi1234 ↔ 1247By similarity
Disulfide bondi1249 ↔ 1262By similarity
Glycosylationi1512 – 15121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1541 ↔ 1554By similarity
Disulfide bondi1550 ↔ 1564By similarity
Glycosylationi1559 – 15591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1566 ↔ 1579By similarity
Glycosylationi1576 – 15761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1617 – 16171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1646 – 16461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1724 – 17241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1734 – 17341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1764 – 17641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1826 – 18261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1851 ↔ 1862By similarity
Disulfide bondi1858 ↔ 1872By similarity
Disulfide bondi1874 ↔ 1887By similarity
Glycosylationi1934 – 19341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1996 – 19961N-linked (GlcNAc...)Sequence Analysis
Modified residuei2010 – 20101N6-acetyllysine1 Publication
Glycosylationi2049 – 20491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2118 – 21181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2128 – 21281N-linked (GlcNAc...)1 Publication
Disulfide bondi2160 ↔ 2171By similarity
Disulfide bondi2167 ↔ 2181By similarity
Disulfide bondi2183 ↔ 2195By similarity
Glycosylationi2473 – 24731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2483 ↔ 2494By similarity
Disulfide bondi2490 ↔ 2504By similarity
Glycosylationi2503 – 25031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2506 ↔ 2518By similarity
Glycosylationi2522 – 25221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2525 ↔ 2538By similarity
Disulfide bondi2533 ↔ 2551By similarity
Disulfide bondi2545 ↔ 2562By similarity
Disulfide bondi2567 ↔ 2579By similarity
Disulfide bondi2574 ↔ 2592By similarity
Disulfide bondi2586 ↔ 2601By similarity
Glycosylationi2602 – 26021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2606 ↔ 2618By similarity
Disulfide bondi2613 ↔ 2631By similarity
Glycosylationi2621 – 26211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2625 ↔ 2640By similarity
Glycosylationi2639 – 26391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2645 ↔ 2667By similarity
Disulfide bondi2661 ↔ 2680By similarity
Disulfide bondi2674 ↔ 2689By similarity
Disulfide bondi2697 ↔ 2709By similarity
Disulfide bondi2704 ↔ 2722By similarity
Disulfide bondi2716 ↔ 2731By similarity
Disulfide bondi2735 ↔ 2747By similarity
Disulfide bondi2742 ↔ 2760By similarity
Disulfide bondi2754 ↔ 2770By similarity
Disulfide bondi2775 ↔ 2788By similarity
Disulfide bondi2782 ↔ 2801By similarity
Disulfide bondi2795 ↔ 2813By similarity
Glycosylationi2816 – 28161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2819 ↔ 2831By similarity
Disulfide bondi2826 ↔ 2844By similarity
Disulfide bondi2838 ↔ 2854By similarity
Disulfide bondi2859 ↔ 2871By similarity
Disulfide bondi2866 ↔ 2885By similarity
Disulfide bondi2879 ↔ 2898By similarity
Disulfide bondi2905 ↔ 2918By similarity
Glycosylationi2906 – 29061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2913 ↔ 2931By similarity
Disulfide bondi2925 ↔ 2940By similarity
Disulfide bondi2945 ↔ 2957By similarity
Disulfide bondi2953 ↔ 2966By similarity
Disulfide bondi2968 ↔ 2981By similarity
Disulfide bondi2987 ↔ 2997By similarity
Disulfide bondi2993 ↔ 3006By similarity
Disulfide bondi3008 ↔ 3022By similarity
Glycosylationi3049 – 30491N-linked (GlcNAc...)1 Publication
Glycosylationi3090 – 30901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3265 – 32651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3295 ↔ 3306By similarity
Disulfide bondi3302 ↔ 3316By similarity
Disulfide bondi3318 ↔ 3331By similarity
Glycosylationi3334 – 33341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3335 ↔ 3347By similarity
Disulfide bondi3342 ↔ 3360By similarity
Disulfide bondi3354 ↔ 3370By similarity
Disulfide bondi3375 ↔ 3387By similarity
Disulfide bondi3382 ↔ 3400By similarity
Disulfide bondi3394 ↔ 3409By similarity
Disulfide bondi3414 ↔ 3427By similarity
Disulfide bondi3421 ↔ 3440By similarity
Disulfide bondi3434 ↔ 3449By similarity
Disulfide bondi3454 ↔ 3467By similarity
Disulfide bondi3461 ↔ 3480By similarity
Disulfide bondi3474 ↔ 3490By similarity
Glycosylationi3489 – 34891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3495 ↔ 3508By similarity
Disulfide bondi3502 ↔ 3521By similarity
Disulfide bondi3515 ↔ 3532By similarity
Disulfide bondi3537 ↔ 3549By similarity
Disulfide bondi3544 ↔ 3562By similarity
Disulfide bondi3556 ↔ 3571By similarity
Disulfide bondi3576 ↔ 3588By similarity
Disulfide bondi3583 ↔ 3601By similarity
Disulfide bondi3595 ↔ 3610By similarity
Disulfide bondi3614 ↔ 3626By similarity
Disulfide bondi3621 ↔ 3639By similarity
Disulfide bondi3633 ↔ 3648By similarity
Disulfide bondi3655 ↔ 3667By similarity
Disulfide bondi3662 ↔ 3680By similarity
Glycosylationi3663 – 36631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3674 ↔ 3691By similarity
Disulfide bondi3696 ↔ 3710By similarity
Disulfide bondi3704 ↔ 3723By similarity
Disulfide bondi3717 ↔ 3732By similarity
Disulfide bondi3742 ↔ 3755By similarity
Disulfide bondi3750 ↔ 3768By similarity
Disulfide bondi3762 ↔ 3777By similarity
Disulfide bondi3786 ↔ 3799By similarity
Glycosylationi3789 – 37891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3793 ↔ 3808By similarity
Disulfide bondi3810 ↔ 3823By similarity
Disulfide bondi3829 ↔ 3839By similarity
Disulfide bondi3835 ↔ 3848By similarity
Glycosylationi3840 – 38401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3850 ↔ 3861By similarity
Glycosylationi3954 – 39541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4076 – 40761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4126 – 41261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4152 ↔ 4161By similarity
Disulfide bondi4157 ↔ 4170By similarity
Disulfide bondi4172 ↔ 4183By similarity
Glycosylationi4180 – 41801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4201 ↔ 4211By similarity
Disulfide bondi4205 ↔ 4221By similarity
Disulfide bondi4223 ↔ 4232By similarity
Disulfide bondi4237 ↔ 4247By similarity
Disulfide bondi4241 ↔ 4257By similarity
Disulfide bondi4259 ↔ 4268By similarity
Disulfide bondi4273 ↔ 4283By similarity
Disulfide bondi4277 ↔ 4293By similarity
Glycosylationi4279 – 42791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4280 – 42801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4295 ↔ 4304By similarity
Disulfide bondi4309 ↔ 4319By similarity
Disulfide bondi4313 ↔ 4329By similarity
Disulfide bondi4331 ↔ 4340By similarity
Disulfide bondi4345 ↔ 4353By similarity
Disulfide bondi4348 ↔ 4364By similarity
Glycosylationi4365 – 43651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4366 ↔ 4375By similarity
Disulfide bondi4378 ↔ 4388By similarity
Disulfide bondi4382 ↔ 4398By similarity
Disulfide bondi4400 ↔ 4409By similarity
Modified residuei4508 – 45081PhosphotyrosineBy similarity
Modified residuei4524 – 45241Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues.By similarity
Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1 (By similarity).By similarity
Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ91ZX7.
PaxDbiQ91ZX7.
PRIDEiQ91ZX7.

PTM databases

PhosphoSiteiQ91ZX7.

Expressioni

Gene expression databases

BgeeiQ91ZX7.
ExpressionAtlasiQ91ZX7. baseline and differential.
GenevestigatoriQ91ZX7.

Interactioni

Subunit structurei

Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-terminal subunit. Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1. Interacts with LRPAP1 (By similarity). Intracellular domain interacts with MAFB. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with bacterial exotoxins.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab1P973182EBI-300955,EBI-81680
Dlg4Q621083EBI-300955,EBI-300895
Mapk8ip1Q9WVI92EBI-300955,EBI-74515
Mapk8ip2Q9ERE92EBI-300955,EBI-74576

Protein-protein interaction databases

BioGridi201201. 7 interactions.
DIPiDIP-47785N.
IntActiQ91ZX7. 13 interactions.
MINTiMINT-1848960.

Structurei

3D structure databases

ProteinModelPortaliQ91ZX7.
SMRiQ91ZX7. Positions 26-844, 851-1179, 1186-1567, 1585-2519, 2529-4410.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 44244405ExtracellularSequence AnalysisAdd
BLAST
Topological domaini4446 – 4545100CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4425 – 444521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6742LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini71 – 11141LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 15039EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 19040EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati293 – 33543LDL-receptor class B 1Sequence AnalysisAdd
BLAST
Repeati336 – 37944LDL-receptor class B 2Sequence AnalysisAdd
BLAST
Repeati380 – 42344LDL-receptor class B 3Sequence AnalysisAdd
BLAST
Domaini475 – 52147EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Repeati572 – 61443LDL-receptor class B 4Sequence AnalysisAdd
BLAST
Repeati615 – 66046LDL-receptor class B 5Sequence AnalysisAdd
BLAST
Repeati661 – 71151LDL-receptor class B 6Sequence AnalysisAdd
BLAST
Repeati712 – 75544LDL-receptor class B 7Sequence AnalysisAdd
BLAST
Domaini804 – 84441EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini853 – 89341LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini894 – 93441LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini935 – 97440LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini975 – 101440LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini1014 – 105441LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini1061 – 110040LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini1103 – 114341LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini1144 – 118340LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini1184 – 122340EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini1224 – 126340EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Repeati1310 – 135647LDL-receptor class B 8Sequence AnalysisAdd
BLAST
Repeati1357 – 139943LDL-receptor class B 9Sequence AnalysisAdd
BLAST
Repeati1400 – 144647LDL-receptor class B 10Sequence AnalysisAdd
BLAST
Repeati1447 – 149145LDL-receptor class B 11Sequence AnalysisAdd
BLAST
Repeati1492 – 153241LDL-receptor class B 12Sequence AnalysisAdd
BLAST
Domaini1537 – 158044EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Repeati1628 – 167043LDL-receptor class B 13Sequence AnalysisAdd
BLAST
Repeati1671 – 171444LDL-receptor class B 14Sequence AnalysisAdd
BLAST
Repeati1715 – 175440LDL-receptor class B 15Sequence AnalysisAdd
BLAST
Repeati1755 – 179945LDL-receptor class B 16Sequence AnalysisAdd
BLAST
Domaini1847 – 188842EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati1935 – 197743LDL-receptor class B 17Sequence AnalysisAdd
BLAST
Repeati1978 – 202043LDL-receptor class B 18Sequence AnalysisAdd
BLAST
Repeati2021 – 206444LDL-receptor class B 19Sequence AnalysisAdd
BLAST
Repeati2065 – 210844LDL-receptor class B 20Sequence AnalysisAdd
BLAST
Domaini2156 – 219641EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Repeati2254 – 229542LDL-receptor class B 21Sequence AnalysisAdd
BLAST
Repeati2296 – 234449LDL-receptor class B 22Sequence AnalysisAdd
BLAST
Repeati2345 – 238945LDL-receptor class B 23Sequence AnalysisAdd
BLAST
Repeati2390 – 243243LDL-receptor class B 24Sequence AnalysisAdd
BLAST
Repeati2433 – 247442LDL-receptor class B 25Sequence AnalysisAdd
BLAST
Domaini2479 – 251941EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini2523 – 256442LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST
Domaini2565 – 260339LDL-receptor class A 12PROSITE-ProRule annotationAdd
BLAST
Domaini2604 – 264239LDL-receptor class A 13PROSITE-ProRule annotationAdd
BLAST
Domaini2643 – 269149LDL-receptor class A 14PROSITE-ProRule annotationAdd
BLAST
Domaini2695 – 273339LDL-receptor class A 15PROSITE-ProRule annotationAdd
BLAST
Domaini2733 – 277240LDL-receptor class A 16PROSITE-ProRule annotationAdd
BLAST
Domaini2773 – 281543LDL-receptor class A 17PROSITE-ProRule annotationAdd
BLAST
Domaini2817 – 285640LDL-receptor class A 18PROSITE-ProRule annotationAdd
BLAST
Domaini2857 – 290044LDL-receptor class A 19PROSITE-ProRule annotationAdd
BLAST
Domaini2903 – 294139LDL-receptor class A 20PROSITE-ProRule annotationAdd
BLAST
Domaini2942 – 298241EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini2983 – 302341EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati3070 – 311445LDL-receptor class B 26Sequence AnalysisAdd
BLAST
Repeati3115 – 315743LDL-receptor class B 27Sequence AnalysisAdd
BLAST
Repeati3158 – 320144LDL-receptor class B 28Sequence AnalysisAdd
BLAST
Repeati3202 – 324443LDL-receptor class B 29Sequence AnalysisAdd
BLAST
Repeati3245 – 328541LDL-receptor class B 30Sequence AnalysisAdd
BLAST
Domaini3291 – 333242EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini3333 – 337240LDL-receptor class A 21PROSITE-ProRule annotationAdd
BLAST
Domaini3373 – 341139LDL-receptor class A 22PROSITE-ProRule annotationAdd
BLAST
Domaini3412 – 345140LDL-receptor class A 23PROSITE-ProRule annotationAdd
BLAST
Domaini3452 – 349241LDL-receptor class A 24PROSITE-ProRule annotationAdd
BLAST
Domaini3493 – 353442LDL-receptor class A 25PROSITE-ProRule annotationAdd
BLAST
Domaini3535 – 357339LDL-receptor class A 26PROSITE-ProRule annotationAdd
BLAST
Domaini3574 – 361239LDL-receptor class A 27PROSITE-ProRule annotationAdd
BLAST
Domaini3612 – 365039LDL-receptor class A 28PROSITE-ProRule annotationAdd
BLAST
Domaini3653 – 369341LDL-receptor class A 29PROSITE-ProRule annotationAdd
BLAST
Domaini3694 – 373441LDL-receptor class A 30PROSITE-ProRule annotationAdd
BLAST
Domaini3740 – 377940LDL-receptor class A 31PROSITE-ProRule annotationAdd
BLAST
Domaini3782 – 382443EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini3825 – 386238EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Repeati3913 – 395543LDL-receptor class B 31Sequence AnalysisAdd
BLAST
Repeati3971 – 401343LDL-receptor class B 32Sequence AnalysisAdd
BLAST
Repeati4014 – 405744LDL-receptor class B 33Sequence AnalysisAdd
BLAST
Repeati4058 – 410245LDL-receptor class B 34Sequence AnalysisAdd
BLAST
Domaini4148 – 418437EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini4197 – 423337EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini4233 – 426937EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini4269 – 430537EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini4305 – 434137EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini4341 – 437636EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini4374 – 441037EGF-like 22PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4446 – 4545100Interaction with MAFB1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3941 – 39444Recognition site for proteolytical processingSequence Analysis
Motifi4503 – 45086NPXY motif

Sequence similaritiesi

Belongs to the LDLR family.Sequence Analysis
Contains 22 EGF-like domains.PROSITE-ProRule annotation
Contains 31 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG235850.
GeneTreeiENSGT00760000119194.
HOGENOMiHOG000230574.
HOVERGENiHBG006292.
InParanoidiQ91ZX7.
KOiK04550.
OrthoDBiEOG790FZT.
PhylomeDBiQ91ZX7.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR006150. Cys_repeat_1.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 17 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
SM00289. WR1. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91ZX7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG
60 70 80 90 100
ERDCPDGSDE APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM
110 120 130 140 150
DGSDEGAHCR ELRANCSRMG CQHHCVPTPS GPTCYCNSSF QLQADGKTCK
160 170 180 190 200
DFDECSVYGT CSQLCTNTDG SFTCGCVEGY LLQPDNRSCK AKNEPVDRPP
210 220 230 240 250
VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN ETVCWVHVGD
260 270 280 290 300
SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD
310 320 330 340 350
IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE
360 370 380 390 400
RCDMDGQNRT KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK
410 420 430 440 450
GRQTIIQGIL IEHLYGLTVF ENYLYATNSD NANTQQKTSV IRVNRFNSTE
460 470 480 490 500
YQVVTRVDKG GALHIYHQRR QPRVRSHACE NDQYGKPGGC SDICLLANSH
510 520 530 540 550
KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR GMDMGAKVPD
560 570 580 590 600
EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD
610 620 630 640 650
GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH
660 670 680 690 700
PRAIVVDPLN GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL
710 720 730 740 750
WPNGLSLDIP AGRLYWVDAF YDRIETILLN GTDRKIVYEG PELNHAFGLC
760 770 780 790 800
HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV TLLRSERPPI FEIRMYDAQQ
810 820 830 840 850
QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG VTCLANPSYV
860 870 880 890 900
PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR
910 920 930 940 950
FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI
960 970 980 990 1000
PISWTCDLDD DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND
1010 1020 1030 1040 1050
NDCGDNSDEA GCSHSCSSTQ FKCNSGRCIP EHWTCDGDND CGDYSDETHA
1060 1070 1080 1090 1100
NCTNQATRPP GGCHSDEFQC RLDGLCIPLR WRCDGDTDCM DSSDEKSCEG
1110 1120 1130 1140 1150
VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN CEALACRPPS
1160 1170 1180 1190 1200
HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA
1210 1220 1230 1240 1250
PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY
1260 1270 1280 1290 1300
EGWVLEPDGE SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT
1310 1320 1330 1340 1350
IALDFHLSQS ALYWTDVVED KIYRGKLLDN GALTSFEVVI QYGLATPEGL
1360 1370 1380 1390 1400
AVDWIAGNIY WVESNLDQIE VAKLDGTLRT TLLAGDIEHP RAIALDPRDG
1410 1420 1430 1440 1450
ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL TVDYLEKRIL
1460 1470 1480 1490 1500
WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN
1510 1520 1530 1540 1550
TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC
1560 1570 1580 1590 1600
SHLCLINYNR TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD
1610 1620 1630 1640 1650
APYYNYIISF TVPDIDNVTV LDYDAREQRV YWSDVRTQAI KRAFINGTGV
1660 1670 1680 1690 1700
ETVVSADLPN AHGLAVDWVS RNLFWTSYDT NKKQINVARL DGSFKNAVVQ
1710 1720 1730 1740 1750
GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS GQKGPVGLAI
1760 1770 1780 1790 1800
DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL
1810 1820 1830 1840 1850
WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP
1860 1870 1880 1890 1900
CSVNNGDCSQ LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE
1910 1920 1930 1940 1950
GIRGIPLDPN DKSDALVPVS GTSLAVGIDF HAENDTIYWV DMGLSTISRA
1960 1970 1980 1990 2000
KRDQTWREDV VTNGIGRVEG IAVDWIAGNI YWTDQGFDVI EVARLNGSFR
2010 2020 2030 2040 2050
YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD GTERVVLVNV
2060 2070 2080 2090 2100
SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF
2110 2120 2130 2140 2150
SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN
2160 2170 2180 2190 2200
RDRQKGTNVC AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG
2210 2220 2230 2240 2250
YLLYSERTIL KSIHLSDERN LNAPVQPFED PEHMKNVIAL AFDYRAGTSP
2260 2270 2280 2290 2300
GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV ENVGSVEGLA YHRGWDTLYW
2310 2320 2330 2340 2350
TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL DECQNLMFWT
2360 2370 2380 2390 2400
NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD
2410 2420 2430 2440 2450
KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV
2460 2470 2480 2490 2500
GSDMKLLRVD IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG
2510 2520 2530 2540 2550
HVNCSCRGGR ILQEDFTCRA VNSSCRAQDE FECANGECIS FSLTCDGVSH
2560 2570 2580 2590 2600
CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV SNMLWCNGVD DCGDGSDEIP
2610 2620 2630 2640 2650
CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC SATDCSSYFR
2660 2670 2680 2690 2700
LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN
2710 2720 2730 2740 2750
YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK
2760 2770 2780 2790 2800
QWLCDGSDDC GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD
2810 2820 2830 2840 2850
CTDGADESVT AGCLYNSTCD DREFMCQNRL CIPKHFVCDH DRDCADGSDE
2860 2870 2880 2890 2900
SPECEYPTCG PNEFRCANGR CLSSRQWECD GENDCHDHSD EAPKNPHCTS
2910 2920 2930 2940 2950
PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC HVNECLSRKL
2960 2970 2980 2990 3000
SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT
3010 3020 3030 3040 3050
HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY
3060 3070 3080 3090 3100
TLLKQGLNNA VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT
3110 3120 3130 3140 3150
GLSNPDGLAV DWVGGNLYWC DKGRDTIEVS KLNGAYRTVL VSSGLREPRA
3160 3170 3180 3190 3200
LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG RSIIVDTKIT WPNGLTVDYV
3210 3220 3230 3240 3250
TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL FEDYVYWTDW
3260 3270 3280 3290 3300
ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG
3310 3320 3330 3340 3350
GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF
3360 3370 3380 3390 3400
WWKCDTEDDC GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC
3410 3420 3430 3440 3450
QDNSDEANCD IHVCLPSQFK CTNTNRCIPG IFRCNGQDNC GDGEDERDCP
3460 3470 3480 3490 3500
EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC VDGSDEPANC TQMTCGVDEF
3510 3520 3530 3540 3550
RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY QFRCKNNRCV
3560 3570 3580 3590 3600
PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD
3610 3620 3630 3640 3650
CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT
3660 3670 3680 3690 3700
GVRTCPLDEF QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR
3710 3720 3730 3740 3750
PFRCKNDRVC LWIGRQCDGV DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC
3760 3770 3780 3790 3800
RNQRCLSSSL RCNMFDDCGD GSDEEDCSID PKLTSCATNA SMCGDEARCV
3810 3820 3830 3840 3850
RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN NTKGGHLCSC
3860 3870 3880 3890 3900
ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES
3910 3920 3930 3940 3950
VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV
3960 3970 3980 3990 4000
THLNISGLKM PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM
4010 4020 4030 4040 4050
IDEPHAIVVD PLRGTMYWSD WGNHPKIETA AMDGTLRETL VQDNIQWPTG
4060 4070 4080 4090 4100
LAVDYHNERL YWADAKLSVI GSIRLNGTDP IVAADSKRGL SHPFSIDVFE
4110 4120 4130 4140 4150
DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY HQHKQPEVTN
4160 4170 4180 4190 4200
PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT
4210 4220 4230 4240 4250
CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS
4260 4270 4280 4290 4300
PSGMPTCRCP TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL
4310 4320 4330 4340 4350
GDRCQYRQCS GFCENFGTCQ MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ
4360 4370 4380 4390 4400
GACVVNKQTG DVTCNCTDGR VAPSCLTCID HCSNGGSCTM NSKMMPECQC
4410 4420 4430 4440 4450
PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG VVFWYKRRVR
4460 4470 4480 4490 4500
GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP
4510 4520 4530 4540
TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA
Length:4,545
Mass (Da):504,742
Last modified:December 1, 2001 - v1
Checksum:i9904CF5DF5EE333E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2642 – 26421A → T in AAL09567. (PubMed:12151109)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67469 mRNA. Translation: CAA47817.1. Sequence problems.
AF367720 mRNA. Translation: AAL09566.1.
AF369477
, AF369389, AF369390, AF369391, AF369392, AF369393, AF369394, AF369395, AF369396, AF369397, AF369398, AF369399, AF369400, AF369401, AF369402, AF369403, AF369404, AF369405, AF369406, AF369407, AF369408, AF369409, AF369410, AF369411, AF369412, AF369413, AF369414, AF369415, AF369416, AF369417, AF369418, AF369419, AF369420, AF369421, AF369422, AF369423, AF369424, AF369425, AF369426, AF369427, AF369428, AF369429, AF369430, AF369431, AF369432, AF369433, AF369434, AF369435, AF369436, AF369437, AF369438, AF369439, AF369440, AF369441, AF369442, AF369443, AF369444, AF369445, AF369446, AF369447, AF369448, AF369449, AF369450, AF369451, AF369452, AF369453, AF369454, AF369455, AF369456, AF369457, AF369458, AF369459, AF369460, AF369461, AF369462, AF369463, AF369464, AF369465, AF369466, AF369467, AF369468, AF369469, AF369470, AF369471, AF369472, AF369473, AF369474, AF369475, AF369476 Genomic DNA. Translation: AAL09567.1.
CCDSiCCDS24245.1.
PIRiS25111.
RefSeqiNP_032538.2. NM_008512.2.
UniGeneiMm.271854.

Genome annotation databases

EnsembliENSMUST00000049149; ENSMUSP00000044004; ENSMUSG00000040249.
GeneIDi16971.
KEGGimmu:16971.
UCSCiuc007hjx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67469 mRNA. Translation: CAA47817.1 . Sequence problems.
AF367720 mRNA. Translation: AAL09566.1 .
AF369477
, AF369389 , AF369390 , AF369391 , AF369392 , AF369393 , AF369394 , AF369395 , AF369396 , AF369397 , AF369398 , AF369399 , AF369400 , AF369401 , AF369402 , AF369403 , AF369404 , AF369405 , AF369406 , AF369407 , AF369408 , AF369409 , AF369410 , AF369411 , AF369412 , AF369413 , AF369414 , AF369415 , AF369416 , AF369417 , AF369418 , AF369419 , AF369420 , AF369421 , AF369422 , AF369423 , AF369424 , AF369425 , AF369426 , AF369427 , AF369428 , AF369429 , AF369430 , AF369431 , AF369432 , AF369433 , AF369434 , AF369435 , AF369436 , AF369437 , AF369438 , AF369439 , AF369440 , AF369441 , AF369442 , AF369443 , AF369444 , AF369445 , AF369446 , AF369447 , AF369448 , AF369449 , AF369450 , AF369451 , AF369452 , AF369453 , AF369454 , AF369455 , AF369456 , AF369457 , AF369458 , AF369459 , AF369460 , AF369461 , AF369462 , AF369463 , AF369464 , AF369465 , AF369466 , AF369467 , AF369468 , AF369469 , AF369470 , AF369471 , AF369472 , AF369473 , AF369474 , AF369475 , AF369476 Genomic DNA. Translation: AAL09567.1 .
CCDSi CCDS24245.1.
PIRi S25111.
RefSeqi NP_032538.2. NM_008512.2.
UniGenei Mm.271854.

3D structure databases

ProteinModelPortali Q91ZX7.
SMRi Q91ZX7. Positions 26-844, 851-1179, 1186-1567, 1585-2519, 2529-4410.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201201. 7 interactions.
DIPi DIP-47785N.
IntActi Q91ZX7. 13 interactions.
MINTi MINT-1848960.

PTM databases

PhosphoSitei Q91ZX7.

Proteomic databases

MaxQBi Q91ZX7.
PaxDbi Q91ZX7.
PRIDEi Q91ZX7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049149 ; ENSMUSP00000044004 ; ENSMUSG00000040249 .
GeneIDi 16971.
KEGGi mmu:16971.
UCSCi uc007hjx.1. mouse.

Organism-specific databases

CTDi 4035.
MGIi MGI:96828. Lrp1.

Phylogenomic databases

eggNOGi NOG235850.
GeneTreei ENSGT00760000119194.
HOGENOMi HOG000230574.
HOVERGENi HBG006292.
InParanoidi Q91ZX7.
KOi K04550.
OrthoDBi EOG790FZT.
PhylomeDBi Q91ZX7.
TreeFami TF315253.

Enzyme and pathway databases

Reactomei REACT_196575. Scavenging of heme from plasma.
REACT_198569. Retinoid metabolism and transport.

Miscellaneous databases

NextBioi 291026.
PROi Q91ZX7.
SOURCEi Search...

Gene expression databases

Bgeei Q91ZX7.
ExpressionAtlasi Q91ZX7. baseline and differential.
Genevestigatori Q91ZX7.

Family and domain databases

Gene3Di 2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR006150. Cys_repeat_1.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view ]
Pfami PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 16 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00181. EGF. 17 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 35 hits.
SM00289. WR1. 4 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 9 hits.
SSF57424. SSF57424. 30 hits.
PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: LiverImported.
  2. "Functional expression of murine LRP1 requires correction of Lrp1 cDNA sequences."
    Smeijers L., Willems S., Lauwers A., Thiry E., van Leuven F., Roebroek A.J.M.
    Biochim. Biophys. Acta 1577:155-158(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/JImported and CBAImported.
  3. "The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A."
    Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K., Saelinger C.B.
    J. Biol. Chem. 267:12420-12423(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
  4. "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."
    Morris S.M., Cooper J.A.
    Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  5. "Low-density lipoprotein receptor-related protein interacts with MafB, a regulator of hindbrain development."
    Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M., Willnow T.E.
    FEBS Lett. 565:23-27(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAFB.
  6. "LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation."
    Herz J., Clouthier D.E., Hammer R.E.
    Cell 71:411-421(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730; ASN-2128 AND ASN-3049.
    Tissue: Myoblast.
  9. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447.
  10. Cited for: FUNCTION AS A RECEPTOR FOR CHOLIX TOXIN.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2010, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiLRP1_MOUSE
AccessioniPrimary (citable) accession number: Q91ZX7
Secondary accession number(s): Q61291, Q920Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 108 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3