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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, A2mr
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.3 Publications
Functions as a receptor for Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.3 Publications

Sites

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

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. protein binding Source: IntAct

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:Lrp1
Synonyms:A2mr
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 44244405Extracellular Reviewed predictionAdd
BLAST
Transmembranei4425 – 444521Helical; Reviewed predictionAdd
BLAST
Topological domaini4446 – 4545100Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. clathrin-coated vesicle Source: Ensembl
  2. coated pit Source: UniProtKB-SubCell
  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-SubCell
  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 – 1919 Reviewed predictionAdd
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 ↔ 41 By similarityBy similarity
Disulfide bondi35 ↔ 54 By similarityBy similarity
Disulfide bondi48 ↔ 65 By similarityBy similarity
Disulfide bondi73 ↔ 86 By similarityBy similarity
Disulfide bondi80 ↔ 99 By similarityBy similarity
Disulfide bondi93 ↔ 109 By similarityBy similarity
Glycosylationi115 – 1151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi116 ↔ 125 By similarityBy similarity
Disulfide bondi121 ↔ 134 By similarityBy similarity
Disulfide bondi136 ↔ 149 By similarityBy similarity
Glycosylationi137 – 1371N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi155 ↔ 165 By similarityBy similarity
Disulfide bondi161 ↔ 174 By similarityBy similarity
Disulfide bondi176 ↔ 189 By similarityBy similarity
Glycosylationi186 – 1861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi240 – 2401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi275 – 2751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi358 – 3581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi447 – 4471N-linked (GlcNAc...)1 Publication
Disulfide bondi479 ↔ 494 By similarityBy similarity
Disulfide bondi490 ↔ 505 By similarityBy similarity
Disulfide bondi507 ↔ 520 By similarityBy similarity
Glycosylationi730 – 7301N-linked (GlcNAc...)1 Publication
Disulfide bondi808 ↔ 819 By similarityBy similarity
Disulfide bondi815 ↔ 828 By similarityBy similarity
Disulfide bondi830 ↔ 843 By similarityBy similarity
Disulfide bondi855 ↔ 867 By similarityBy similarity
Disulfide bondi862 ↔ 880 By similarityBy similarity
Disulfide bondi874 ↔ 891 By similarityBy similarity
Disulfide bondi896 ↔ 908 By similarityBy similarity
Disulfide bondi903 ↔ 921 By similarityBy similarity
Disulfide bondi915 ↔ 932 By similarityBy similarity
Glycosylationi929 – 9291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi937 ↔ 949 By similarityBy similarity
Disulfide bondi944 ↔ 962 By similarityBy similarity
Disulfide bondi956 ↔ 972 By similarityBy similarity
Disulfide bondi977 ↔ 990 By similarityBy similarity
Disulfide bondi985 ↔ 1003 By similarityBy similarity
Disulfide bondi997 ↔ 1012 By similarityBy similarity
Disulfide bondi1016 ↔ 1028 By similarityBy similarity
Disulfide bondi1023 ↔ 1041 By similarityBy similarity
Disulfide bondi1035 ↔ 1052 By similarityBy similarity
Glycosylationi1051 – 10511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1063 ↔ 1076 By similarityBy similarity
Disulfide bondi1070 ↔ 1089 By similarityBy similarity
Disulfide bondi1083 ↔ 1098 By similarityBy similarity
Disulfide bondi1105 ↔ 1119 By similarityBy similarity
Disulfide bondi1113 ↔ 1132 By similarityBy similarity
Disulfide bondi1126 ↔ 1141 By similarityBy similarity
Disulfide bondi1146 ↔ 1160 By similarityBy similarity
Disulfide bondi1153 ↔ 1173 By similarityBy similarity
Glycosylationi1155 – 11551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1156 – 11561N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1167 ↔ 1183 By similarityBy similarity
Disulfide bondi1186 ↔ 1197 By similarityBy similarity
Disulfide bondi1193 ↔ 1207 By similarityBy similarity
Glycosylationi1196 – 11961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1209 ↔ 1222 By similarityBy similarity
Glycosylationi1219 – 12191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1228 ↔ 1238 By similarityBy similarity
Disulfide bondi1234 ↔ 1247 By similarityBy similarity
Disulfide bondi1249 ↔ 1262 By similarityBy similarity
Glycosylationi1512 – 15121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1541 ↔ 1554 By similarityBy similarity
Disulfide bondi1550 ↔ 1564 By similarityBy similarity
Glycosylationi1559 – 15591N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1566 ↔ 1579 By similarityBy similarity
Glycosylationi1576 – 15761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1617 – 16171N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1646 – 16461N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1724 – 17241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1734 – 17341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1764 – 17641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1826 – 18261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1851 ↔ 1862 By similarityBy similarity
Disulfide bondi1858 ↔ 1872 By similarityBy similarity
Disulfide bondi1874 ↔ 1887 By similarityBy similarity
Glycosylationi1934 – 19341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1996 – 19961N-linked (GlcNAc...) Reviewed prediction
Modified residuei2010 – 20101N6-acetyllysine1 Publication
Glycosylationi2049 – 20491N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2118 – 21181N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2128 – 21281N-linked (GlcNAc...)1 Publication
Disulfide bondi2160 ↔ 2171 By similarityBy similarity
Disulfide bondi2167 ↔ 2181 By similarityBy similarity
Disulfide bondi2183 ↔ 2195 By similarityBy similarity
Glycosylationi2473 – 24731N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2483 ↔ 2494 By similarityBy similarity
Disulfide bondi2490 ↔ 2504 By similarityBy similarity
Glycosylationi2503 – 25031N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2506 ↔ 2518 By similarityBy similarity
Glycosylationi2522 – 25221N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2525 ↔ 2538 By similarityBy similarity
Disulfide bondi2533 ↔ 2551 By similarityBy similarity
Disulfide bondi2545 ↔ 2562 By similarityBy similarity
Disulfide bondi2567 ↔ 2579 By similarityBy similarity
Disulfide bondi2574 ↔ 2592 By similarityBy similarity
Disulfide bondi2586 ↔ 2601 By similarityBy similarity
Glycosylationi2602 – 26021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2606 ↔ 2618 By similarityBy similarity
Disulfide bondi2613 ↔ 2631 By similarityBy similarity
Glycosylationi2621 – 26211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2625 ↔ 2640 By similarityBy similarity
Glycosylationi2639 – 26391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2645 ↔ 2667 By similarityBy similarity
Disulfide bondi2661 ↔ 2680 By similarityBy similarity
Disulfide bondi2674 ↔ 2689 By similarityBy similarity
Disulfide bondi2697 ↔ 2709 By similarityBy similarity
Disulfide bondi2704 ↔ 2722 By similarityBy similarity
Disulfide bondi2716 ↔ 2731 By similarityBy similarity
Disulfide bondi2735 ↔ 2747 By similarityBy similarity
Disulfide bondi2742 ↔ 2760 By similarityBy similarity
Disulfide bondi2754 ↔ 2770 By similarityBy similarity
Disulfide bondi2775 ↔ 2788 By similarityBy similarity
Disulfide bondi2782 ↔ 2801 By similarityBy similarity
Disulfide bondi2795 ↔ 2813 By similarityBy similarity
Glycosylationi2816 – 28161N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2819 ↔ 2831 By similarityBy similarity
Disulfide bondi2826 ↔ 2844 By similarityBy similarity
Disulfide bondi2838 ↔ 2854 By similarityBy similarity
Disulfide bondi2859 ↔ 2871 By similarityBy similarity
Disulfide bondi2866 ↔ 2885 By similarityBy similarity
Disulfide bondi2879 ↔ 2898 By similarityBy similarity
Disulfide bondi2905 ↔ 2918 By similarityBy similarity
Glycosylationi2906 – 29061N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2913 ↔ 2931 By similarityBy similarity
Disulfide bondi2925 ↔ 2940 By similarityBy similarity
Disulfide bondi2945 ↔ 2957 By similarityBy similarity
Disulfide bondi2953 ↔ 2966 By similarityBy similarity
Disulfide bondi2968 ↔ 2981 By similarityBy similarity
Disulfide bondi2987 ↔ 2997 By similarityBy similarity
Disulfide bondi2993 ↔ 3006 By similarityBy similarity
Disulfide bondi3008 ↔ 3022 By similarityBy similarity
Glycosylationi3049 – 30491N-linked (GlcNAc...)1 Publication
Glycosylationi3090 – 30901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3265 – 32651N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3295 ↔ 3306 By similarityBy similarity
Disulfide bondi3302 ↔ 3316 By similarityBy similarity
Disulfide bondi3318 ↔ 3331 By similarityBy similarity
Glycosylationi3334 – 33341N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3335 ↔ 3347 By similarityBy similarity
Disulfide bondi3342 ↔ 3360 By similarityBy similarity
Disulfide bondi3354 ↔ 3370 By similarityBy similarity
Disulfide bondi3375 ↔ 3387 By similarityBy similarity
Disulfide bondi3382 ↔ 3400 By similarityBy similarity
Disulfide bondi3394 ↔ 3409 By similarityBy similarity
Disulfide bondi3414 ↔ 3427 By similarityBy similarity
Disulfide bondi3421 ↔ 3440 By similarityBy similarity
Disulfide bondi3434 ↔ 3449 By similarityBy similarity
Disulfide bondi3454 ↔ 3467 By similarityBy similarity
Disulfide bondi3461 ↔ 3480 By similarityBy similarity
Disulfide bondi3474 ↔ 3490 By similarityBy similarity
Glycosylationi3489 – 34891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3495 ↔ 3508 By similarityBy similarity
Disulfide bondi3502 ↔ 3521 By similarityBy similarity
Disulfide bondi3515 ↔ 3532 By similarityBy similarity
Disulfide bondi3537 ↔ 3549 By similarityBy similarity
Disulfide bondi3544 ↔ 3562 By similarityBy similarity
Disulfide bondi3556 ↔ 3571 By similarityBy similarity
Disulfide bondi3576 ↔ 3588 By similarityBy similarity
Disulfide bondi3583 ↔ 3601 By similarityBy similarity
Disulfide bondi3595 ↔ 3610 By similarityBy similarity
Disulfide bondi3614 ↔ 3626 By similarityBy similarity
Disulfide bondi3621 ↔ 3639 By similarityBy similarity
Disulfide bondi3633 ↔ 3648 By similarityBy similarity
Disulfide bondi3655 ↔ 3667 By similarityBy similarity
Disulfide bondi3662 ↔ 3680 By similarityBy similarity
Glycosylationi3663 – 36631N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3674 ↔ 3691 By similarityBy similarity
Disulfide bondi3696 ↔ 3710 By similarityBy similarity
Disulfide bondi3704 ↔ 3723 By similarityBy similarity
Disulfide bondi3717 ↔ 3732 By similarityBy similarity
Disulfide bondi3742 ↔ 3755 By similarityBy similarity
Disulfide bondi3750 ↔ 3768 By similarityBy similarity
Disulfide bondi3762 ↔ 3777 By similarityBy similarity
Disulfide bondi3786 ↔ 3799 By similarityBy similarity
Glycosylationi3789 – 37891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3793 ↔ 3808 By similarityBy similarity
Disulfide bondi3810 ↔ 3823 By similarityBy similarity
Disulfide bondi3829 ↔ 3839 By similarityBy similarity
Disulfide bondi3835 ↔ 3848 By similarityBy similarity
Glycosylationi3840 – 38401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3850 ↔ 3861 By similarityBy similarity
Glycosylationi3954 – 39541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi4076 – 40761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi4126 – 41261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4152 ↔ 4161 By similarityBy similarity
Disulfide bondi4157 ↔ 4170 By similarityBy similarity
Disulfide bondi4172 ↔ 4183 By similarityBy similarity
Glycosylationi4180 – 41801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4201 ↔ 4211 By similarityBy similarity
Disulfide bondi4205 ↔ 4221 By similarityBy similarity
Disulfide bondi4223 ↔ 4232 By similarityBy similarity
Disulfide bondi4237 ↔ 4247 By similarityBy similarity
Disulfide bondi4241 ↔ 4257 By similarityBy similarity
Disulfide bondi4259 ↔ 4268 By similarityBy similarity
Disulfide bondi4273 ↔ 4283 By similarityBy similarity
Disulfide bondi4277 ↔ 4293 By similarityBy similarity
Glycosylationi4279 – 42791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi4280 – 42801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4295 ↔ 4304 By similarityBy similarity
Disulfide bondi4309 ↔ 4319 By similarityBy similarity
Disulfide bondi4313 ↔ 4329 By similarityBy similarity
Disulfide bondi4331 ↔ 4340 By similarityBy similarity
Disulfide bondi4345 ↔ 4353 By similarityBy similarity
Disulfide bondi4348 ↔ 4364 By similarityBy similarity
Glycosylationi4365 – 43651N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4366 ↔ 4375 By similarityBy similarity
Disulfide bondi4378 ↔ 4388 By similarityBy similarity
Disulfide bondi4382 ↔ 4398 By similarityBy similarity
Disulfide bondi4400 ↔ 4409 By similarityBy similarity
Modified residuei4508 – 45081Phosphotyrosine By 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.
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

ArrayExpressiQ91ZX7.
BgeeiQ91ZX7.
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.2 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. 6 interactions.
DIPiDIP-47785N.
IntActiQ91ZX7. 13 interactions.
MINTiMINT-1848960.

Structurei

3D structure databases

ProteinModelPortaliQ91ZX7.
SMRiQ91ZX7. Positions 26-844, 851-1179, 1186-1567, 1585-2519, 2529-4412.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6742LDL-receptor class A 1Add
BLAST
Domaini71 – 11141LDL-receptor class A 2Add
BLAST
Domaini112 – 15039EGF-like 1Add
BLAST
Domaini151 – 19040EGF-like 2; calcium-binding Reviewed predictionAdd
BLAST
Repeati293 – 33543LDL-receptor class B 1Add
BLAST
Repeati336 – 37944LDL-receptor class B 2Add
BLAST
Repeati380 – 42344LDL-receptor class B 3Add
BLAST
Domaini475 – 52147EGF-like 3Add
BLAST
Repeati572 – 61443LDL-receptor class B 4Add
BLAST
Repeati615 – 66046LDL-receptor class B 5Add
BLAST
Repeati661 – 71151LDL-receptor class B 6Add
BLAST
Repeati712 – 75544LDL-receptor class B 7Add
BLAST
Domaini804 – 84441EGF-like 4Add
BLAST
Domaini853 – 89341LDL-receptor class A 3Add
BLAST
Domaini894 – 93441LDL-receptor class A 4Add
BLAST
Domaini935 – 97440LDL-receptor class A 5Add
BLAST
Domaini975 – 101440LDL-receptor class A 6Add
BLAST
Domaini1014 – 105441LDL-receptor class A 7Add
BLAST
Domaini1061 – 110040LDL-receptor class A 8Add
BLAST
Domaini1103 – 114341LDL-receptor class A 9Add
BLAST
Domaini1144 – 118340LDL-receptor class A 10Add
BLAST
Domaini1184 – 122340EGF-like 5Add
BLAST
Domaini1224 – 126340EGF-like 6Add
BLAST
Repeati1310 – 135647LDL-receptor class B 8Add
BLAST
Repeati1357 – 139943LDL-receptor class B 9Add
BLAST
Repeati1400 – 144647LDL-receptor class B 10Add
BLAST
Repeati1447 – 149145LDL-receptor class B 11Add
BLAST
Repeati1492 – 153241LDL-receptor class B 12Add
BLAST
Domaini1537 – 158044EGF-like 7Add
BLAST
Repeati1628 – 167043LDL-receptor class B 13Add
BLAST
Repeati1671 – 171444LDL-receptor class B 14Add
BLAST
Repeati1715 – 175440LDL-receptor class B 15Add
BLAST
Repeati1755 – 179945LDL-receptor class B 16Add
BLAST
Domaini1847 – 188842EGF-like 8Add
BLAST
Repeati1935 – 197743LDL-receptor class B 17Add
BLAST
Repeati1978 – 202043LDL-receptor class B 18Add
BLAST
Repeati2021 – 206444LDL-receptor class B 19Add
BLAST
Repeati2065 – 210844LDL-receptor class B 20Add
BLAST
Domaini2156 – 219641EGF-like 9Add
BLAST
Repeati2254 – 229542LDL-receptor class B 21Add
BLAST
Repeati2296 – 234449LDL-receptor class B 22Add
BLAST
Repeati2345 – 238945LDL-receptor class B 23Add
BLAST
Repeati2390 – 243243LDL-receptor class B 24Add
BLAST
Repeati2433 – 247442LDL-receptor class B 25Add
BLAST
Domaini2479 – 251941EGF-like 10Add
BLAST
Domaini2523 – 256442LDL-receptor class A 11Add
BLAST
Domaini2565 – 260339LDL-receptor class A 12Add
BLAST
Domaini2604 – 264239LDL-receptor class A 13Add
BLAST
Domaini2643 – 269149LDL-receptor class A 14Add
BLAST
Domaini2695 – 273339LDL-receptor class A 15Add
BLAST
Domaini2733 – 277240LDL-receptor class A 16Add
BLAST
Domaini2773 – 281543LDL-receptor class A 17Add
BLAST
Domaini2817 – 285640LDL-receptor class A 18Add
BLAST
Domaini2857 – 290044LDL-receptor class A 19Add
BLAST
Domaini2903 – 294139LDL-receptor class A 20Add
BLAST
Domaini2942 – 298241EGF-like 11Add
BLAST
Domaini2983 – 302341EGF-like 12; calcium-binding Reviewed predictionAdd
BLAST
Repeati3070 – 311445LDL-receptor class B 26Add
BLAST
Repeati3115 – 315743LDL-receptor class B 27Add
BLAST
Repeati3158 – 320144LDL-receptor class B 28Add
BLAST
Repeati3202 – 324443LDL-receptor class B 29Add
BLAST
Repeati3245 – 328541LDL-receptor class B 30Add
BLAST
Domaini3291 – 333242EGF-like 13Add
BLAST
Domaini3333 – 337240LDL-receptor class A 21Add
BLAST
Domaini3373 – 341139LDL-receptor class A 22Add
BLAST
Domaini3412 – 345140LDL-receptor class A 23Add
BLAST
Domaini3452 – 349241LDL-receptor class A 24Add
BLAST
Domaini3493 – 353442LDL-receptor class A 25Add
BLAST
Domaini3535 – 357339LDL-receptor class A 26Add
BLAST
Domaini3574 – 361239LDL-receptor class A 27Add
BLAST
Domaini3612 – 365039LDL-receptor class A 28Add
BLAST
Domaini3653 – 369341LDL-receptor class A 29Add
BLAST
Domaini3694 – 373441LDL-receptor class A 30Add
BLAST
Domaini3740 – 377940LDL-receptor class A 31Add
BLAST
Domaini3782 – 382443EGF-like 14Add
BLAST
Domaini3825 – 386238EGF-like 15Add
BLAST
Repeati3913 – 395543LDL-receptor class B 31Add
BLAST
Repeati3971 – 401343LDL-receptor class B 32Add
BLAST
Repeati4014 – 405744LDL-receptor class B 33Add
BLAST
Repeati4058 – 410245LDL-receptor class B 34Add
BLAST
Domaini4148 – 418437EGF-like 16Add
BLAST
Domaini4197 – 423337EGF-like 17Add
BLAST
Domaini4233 – 426937EGF-like 18Add
BLAST
Domaini4269 – 430537EGF-like 19Add
BLAST
Domaini4305 – 434137EGF-like 20Add
BLAST
Domaini4341 – 437636EGF-like 21Add
BLAST
Domaini4374 – 441037EGF-like 22Add
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 processing Reviewed prediction
Motifi4503 – 45086NPXY motif

Sequence similaritiesi

Belongs to the LDLR family.
Contains 22 EGF-like domains.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG235850.
GeneTreeiENSGT00750000117273.
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

MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG     50
ERDCPDGSDE APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM 100
DGSDEGAHCR ELRANCSRMG CQHHCVPTPS GPTCYCNSSF QLQADGKTCK 150
DFDECSVYGT CSQLCTNTDG SFTCGCVEGY LLQPDNRSCK AKNEPVDRPP 200
VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN ETVCWVHVGD 250
SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD 300
IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE 350
RCDMDGQNRT KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK 400
GRQTIIQGIL IEHLYGLTVF ENYLYATNSD NANTQQKTSV IRVNRFNSTE 450
YQVVTRVDKG GALHIYHQRR QPRVRSHACE NDQYGKPGGC SDICLLANSH 500
KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR GMDMGAKVPD 550
EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD 600
GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH 650
PRAIVVDPLN GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL 700
WPNGLSLDIP AGRLYWVDAF YDRIETILLN GTDRKIVYEG PELNHAFGLC 750
HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV TLLRSERPPI FEIRMYDAQQ 800
QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG VTCLANPSYV 850
PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR 900
FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI 950
PISWTCDLDD DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND 1000
NDCGDNSDEA GCSHSCSSTQ FKCNSGRCIP EHWTCDGDND CGDYSDETHA 1050
NCTNQATRPP GGCHSDEFQC RLDGLCIPLR WRCDGDTDCM DSSDEKSCEG 1100
VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN CEALACRPPS 1150
HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA 1200
PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY 1250
EGWVLEPDGE SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT 1300
IALDFHLSQS ALYWTDVVED KIYRGKLLDN GALTSFEVVI QYGLATPEGL 1350
AVDWIAGNIY WVESNLDQIE VAKLDGTLRT TLLAGDIEHP RAIALDPRDG 1400
ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL TVDYLEKRIL 1450
WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN 1500
TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC 1550
SHLCLINYNR TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD 1600
APYYNYIISF TVPDIDNVTV LDYDAREQRV YWSDVRTQAI KRAFINGTGV 1650
ETVVSADLPN AHGLAVDWVS RNLFWTSYDT NKKQINVARL DGSFKNAVVQ 1700
GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS GQKGPVGLAI 1750
DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL 1800
WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP 1850
CSVNNGDCSQ LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE 1900
GIRGIPLDPN DKSDALVPVS GTSLAVGIDF HAENDTIYWV DMGLSTISRA 1950
KRDQTWREDV VTNGIGRVEG IAVDWIAGNI YWTDQGFDVI EVARLNGSFR 2000
YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD GTERVVLVNV 2050
SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF 2100
SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN 2150
RDRQKGTNVC AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG 2200
YLLYSERTIL KSIHLSDERN LNAPVQPFED PEHMKNVIAL AFDYRAGTSP 2250
GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV ENVGSVEGLA YHRGWDTLYW 2300
TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL DECQNLMFWT 2350
NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD 2400
KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV 2450
GSDMKLLRVD IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG 2500
HVNCSCRGGR ILQEDFTCRA VNSSCRAQDE FECANGECIS FSLTCDGVSH 2550
CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV SNMLWCNGVD DCGDGSDEIP 2600
CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC SATDCSSYFR 2650
LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN 2700
YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK 2750
QWLCDGSDDC GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD 2800
CTDGADESVT AGCLYNSTCD DREFMCQNRL CIPKHFVCDH DRDCADGSDE 2850
SPECEYPTCG PNEFRCANGR CLSSRQWECD GENDCHDHSD EAPKNPHCTS 2900
PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC HVNECLSRKL 2950
SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT 3000
HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY 3050
TLLKQGLNNA VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT 3100
GLSNPDGLAV DWVGGNLYWC DKGRDTIEVS KLNGAYRTVL VSSGLREPRA 3150
LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG RSIIVDTKIT WPNGLTVDYV 3200
TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL FEDYVYWTDW 3250
ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG 3300
GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF 3350
WWKCDTEDDC GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC 3400
QDNSDEANCD IHVCLPSQFK CTNTNRCIPG IFRCNGQDNC GDGEDERDCP 3450
EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC VDGSDEPANC TQMTCGVDEF 3500
RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY QFRCKNNRCV 3550
PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD 3600
CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT 3650
GVRTCPLDEF QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR 3700
PFRCKNDRVC LWIGRQCDGV DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC 3750
RNQRCLSSSL RCNMFDDCGD GSDEEDCSID PKLTSCATNA SMCGDEARCV 3800
RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN NTKGGHLCSC 3850
ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES 3900
VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV 3950
THLNISGLKM PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM 4000
IDEPHAIVVD PLRGTMYWSD WGNHPKIETA AMDGTLRETL VQDNIQWPTG 4050
LAVDYHNERL YWADAKLSVI GSIRLNGTDP IVAADSKRGL SHPFSIDVFE 4100
DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY HQHKQPEVTN 4150
PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT 4200
CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS 4250
PSGMPTCRCP TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL 4300
GDRCQYRQCS GFCENFGTCQ MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ 4350
GACVVNKQTG DVTCNCTDGR VAPSCLTCID HCSNGGSCTM NSKMMPECQC 4400
PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG VVFWYKRRVR 4450
GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP 4500
TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA 4545
Length:4,545
Mass (Da):504,742
Last modified:December 1, 2001 - v1
Checksum:i9904CF5DF5EE333E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2642 – 26421A → T in AAL09567. 1 Publication

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, 2529-4412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201201. 6 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 ENSGT00750000117273.
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

ArrayExpressi Q91ZX7.
Bgeei Q91ZX7.
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: Liver.
  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/J and CBA.
  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: September 3, 2014
This is version 106 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

Similar proteinsi