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Protein

Low-density lipoprotein receptor-related protein 2

Gene

Lrp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts together with cubilin to mediate HDL endocytosis (By similarity). Receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1206 – 12061Calcium; via carbonyl oxygen
Metal bindingi1209 – 12091Calcium
Metal bindingi1211 – 12111Calcium; via carbonyl oxygen
Metal bindingi1213 – 12131Calcium
Metal bindingi1219 – 12191Calcium
Metal bindingi1220 – 12201Calcium

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • hemoglobin binding Source: RGD
  • hormone binding Source: RGD
  • low-density lipoprotein particle receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD
  • receptor activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • endosomal transport Source: RGD
  • hemoglobin import Source: RGD
  • hormone secretion Source: RGD
  • lipoprotein transport Source: RGD
  • negative regulation of endopeptidase activity Source: BHF-UCL
  • organ regeneration Source: RGD
  • receptor-mediated endocytosis Source: BHF-UCL
  • response to drug Source: RGD
  • response to retinoic acid Source: RGD
  • response to vitamin D Source: RGD
  • response to X-ray Source: RGD
  • transcytosis Source: RGD
  • vitamin metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name:
LRP-2
Alternative name(s):
Glycoprotein 330
Short name:
gp330
Megalin
Gene namesi
Name:Lrp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68407. Lrp2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 44254400ExtracellularSequence analysisAdd
BLAST
Transmembranei4426 – 444621HelicalSequence analysisAdd
BLAST
Topological domaini4447 – 4660214CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • brush border Source: RGD
  • brush border membrane Source: RGD
  • coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
  • endosome Source: RGD
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: RGD
  • membrane raft Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 46604635Low-density lipoprotein receptor-related protein 2PRO_0000017322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 40By similarity
Disulfide bondi35 ↔ 53By similarity
Disulfide bondi47 ↔ 62By similarity
Disulfide bondi67 ↔ 80By similarity
Disulfide bondi74 ↔ 93By similarity
Disulfide bondi87 ↔ 103By similarity
Disulfide bondi108 ↔ 120By similarity
Disulfide bondi115 ↔ 133By similarity
Disulfide bondi127 ↔ 142By similarity
Disulfide bondi147 ↔ 157By similarity
Disulfide bondi152 ↔ 170By similarity
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi164 ↔ 179By similarity
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi183 ↔ 195By similarity
Disulfide bondi190 ↔ 208By similarity
Disulfide bondi202 ↔ 217By similarity
Disulfide bondi222 ↔ 234By similarity
Disulfide bondi229 ↔ 247By similarity
Disulfide bondi241 ↔ 256By similarity
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi265 ↔ 278By similarity
Disulfide bondi272 ↔ 291By similarity
Disulfide bondi285 ↔ 306By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence analysis
Disulfide bondi311 ↔ 320By similarity
Disulfide bondi316 ↔ 329By similarity
Disulfide bondi331 ↔ 345By similarity
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi351 ↔ 361By similarity
Disulfide bondi357 ↔ 370By similarity
Disulfide bondi372 ↔ 384By similarity
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence analysis
Glycosylationi657 – 6571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi662 ↔ 673By similarity
Disulfide bondi669 ↔ 688By similarity
Disulfide bondi690 ↔ 703By similarity
Glycosylationi865 – 8651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi973 ↔ 987By similarity
Disulfide bondi983 ↔ 997By similarity
Disulfide bondi999 ↔ 1012By similarity
Disulfide bondi1025 ↔ 1037By similarity
Disulfide bondi1032 ↔ 1050By similarity
Disulfide bondi1044 ↔ 1059By similarity
Glycosylationi1063 – 10631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1066 ↔ 1079By similarity
Disulfide bondi1073 ↔ 1092By similarity
Disulfide bondi1086 ↔ 1101By similarity
Disulfide bondi1110 ↔ 1122By similarity
Disulfide bondi1117 ↔ 1135By similarity
Disulfide bondi1129 ↔ 1144By similarity
Disulfide bondi1150 ↔ 1162By similarity
Disulfide bondi1157 ↔ 1175By similarity
Disulfide bondi1169 ↔ 1184By similarity
Glycosylationi1187 – 11871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1188 ↔ 12011 Publication
Disulfide bondi1195 ↔ 12141 Publication
Disulfide bondi1208 ↔ 12231 Publication
Disulfide bondi1231 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1257By similarity
Disulfide bondi1251 ↔ 1267By similarity
Disulfide bondi1272 ↔ 1284By similarity
Disulfide bondi1279 ↔ 1297By similarity
Disulfide bondi1291 ↔ 1306By similarity
Disulfide bondi1313 ↔ 1326By similarity
Disulfide bondi1320 ↔ 1339By similarity
Glycosylationi1328 – 13281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1333 ↔ 1349By similarity
Glycosylationi1341 – 13411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1354 ↔ 1365By similarity
Disulfide bondi1361 ↔ 1374By similarity
Disulfide bondi1376 ↔ 1389By similarity
Glycosylationi1384 – 13841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1395 ↔ 1405By similarity
Disulfide bondi1401 ↔ 1414By similarity
Disulfide bondi1416 ↔ 1429By similarity
Glycosylationi1451 – 14511N-linked (GlcNAc...)Sequence analysis
Glycosylationi1497 – 14971N-linked (GlcNAc...)Sequence analysis
Glycosylationi1551 – 15511N-linked (GlcNAc...)Sequence analysis
Glycosylationi1676 – 16761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1705 ↔ 1714By similarity
Disulfide bondi1710 ↔ 1726By similarity
Disulfide bondi1728 ↔ 1741By similarity
Glycosylationi1733 – 17331N-linked (GlcNAc...)Sequence analysis
Glycosylationi1811 – 18111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2023 ↔ 2034By similarity
Disulfide bondi2030 ↔ 2044By similarity
Disulfide bondi2046 ↔ 2059By similarity
Glycosylationi2134 – 21341N-linked (GlcNAc...)Sequence analysis
Glycosylationi2178 – 21781N-linked (GlcNAc...)Sequence analysis
Glycosylationi2225 – 22251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2347 ↔ 2358By similarity
Disulfide bondi2354 ↔ 2369By similarity
Disulfide bondi2371 ↔ 2383By similarity
Glycosylationi2396 – 23961N-linked (GlcNAc...)Sequence analysis
Glycosylationi2488 – 24881N-linked (GlcNAc...)Sequence analysis
Glycosylationi2548 – 25481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2656 ↔ 2667By similarity
Disulfide bondi2663 ↔ 2676By similarity
Disulfide bondi2678 ↔ 2693By similarity
Disulfide bondi2701 ↔ 2713By similarity
Disulfide bondi2708 ↔ 2726By similarity
Disulfide bondi2720 ↔ 2737By similarity
Disulfide bondi2742 ↔ 2754By similarity
Disulfide bondi2749 ↔ 2767By similarity
Disulfide bondi2761 ↔ 2776By similarity
Disulfide bondi2781 ↔ 2794By similarity
Glycosylationi2782 – 27821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2789 ↔ 2807By similarity
Disulfide bondi2801 ↔ 2818By similarity
Glycosylationi2810 – 28101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2823 ↔ 2836By similarity
Disulfide bondi2830 ↔ 2849By similarity
Disulfide bondi2843 ↔ 2860By similarity
Disulfide bondi2865 ↔ 2878By similarity
Disulfide bondi2872 ↔ 2891By similarity
Disulfide bondi2885 ↔ 2901By similarity
Disulfide bondi2908 ↔ 2920By similarity
Disulfide bondi2915 ↔ 2933By similarity
Disulfide bondi2927 ↔ 2945By similarity
Glycosylationi2949 – 29491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2950 ↔ 2967By similarity
Disulfide bondi2957 ↔ 2980By similarity
Disulfide bondi2974 ↔ 2990By similarity
Glycosylationi2989 – 29891N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2995 ↔ 3007By similarity
Disulfide bondi3002 ↔ 3020By similarity
Disulfide bondi3014 ↔ 3029By similarity
Disulfide bondi3034 ↔ 3046By similarity
Disulfide bondi3041 ↔ 3059By similarity
Disulfide bondi3053 ↔ 3070By similarity
Disulfide bondi3077 ↔ 3089By similarity
Disulfide bondi3084 ↔ 3102By similarity
Disulfide bondi3096 ↔ 3111By similarity
Disulfide bondi3116 ↔ 3128By similarity
Disulfide bondi3124 ↔ 3137By similarity
Glycosylationi3127 – 31271N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3139 ↔ 3152By similarity
Disulfide bondi3158 ↔ 3169By similarity
Disulfide bondi3165 ↔ 3178By similarity
Disulfide bondi3180 ↔ 3193By similarity
Glycosylationi3213 – 32131N-linked (GlcNAc...)Sequence analysis
Glycosylationi3259 – 32591N-linked (GlcNAc...)Sequence analysis
Glycosylationi3317 – 33171N-linked (GlcNAc...)Sequence analysis
Glycosylationi3357 – 33571N-linked (GlcNAc...)Sequence analysis
Glycosylationi3448 – 34481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3471 ↔ 3482By similarity
Disulfide bondi3478 ↔ 3493By similarity
Disulfide bondi3495 ↔ 3510By similarity
Disulfide bondi3514 ↔ 3527By similarity
Disulfide bondi3521 ↔ 3540By similarity
Disulfide bondi3534 ↔ 3550By similarity
Disulfide bondi3555 ↔ 3567By similarity
Disulfide bondi3562 ↔ 3580By similarity
Glycosylationi3566 – 35661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3574 ↔ 3591By similarity
Disulfide bondi3596 ↔ 3608By similarity
Disulfide bondi3603 ↔ 3621By similarity
Disulfide bondi3615 ↔ 3632By similarity
Disulfide bondi3637 ↔ 3649By similarity
Disulfide bondi3644 ↔ 3662By similarity
Disulfide bondi3656 ↔ 3673By similarity
Disulfide bondi3680 ↔ 3694By similarity
Glycosylationi3682 – 36821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3688 ↔ 3707By similarity
Disulfide bondi3701 ↔ 3716By similarity
Disulfide bondi3721 ↔ 3734By similarity
Disulfide bondi3729 ↔ 3747By similarity
Disulfide bondi3741 ↔ 3756By similarity
Disulfide bondi3761 ↔ 3773By similarity
Disulfide bondi3768 ↔ 3786By similarity
Disulfide bondi3780 ↔ 3795By similarity
Disulfide bondi3800 ↔ 3812By similarity
Disulfide bondi3807 ↔ 3825By similarity
Disulfide bondi3819 ↔ 3834By similarity
Glycosylationi3840 – 38401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3844 ↔ 3856By similarity
Disulfide bondi3851 ↔ 3869By similarity
Disulfide bondi3863 ↔ 3880By similarity
Disulfide bondi3885 ↔ 3898By similarity
Disulfide bondi3893 ↔ 3911By similarity
Disulfide bondi3905 ↔ 3922By similarity
Disulfide bondi3930 ↔ 3942By similarity
Disulfide bondi3937 ↔ 3955By similarity
Disulfide bondi3949 ↔ 3964By similarity
Glycosylationi3969 – 39691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3972 ↔ 3981By similarity
Disulfide bondi3977 ↔ 3991By similarity
Glycosylationi3980 – 39801N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3993 ↔ 4007By similarity
Disulfide bondi4013 ↔ 4023By similarity
Disulfide bondi4019 ↔ 4032By similarity
Disulfide bondi4034 ↔ 4049By similarity
Glycosylationi4070 – 40701N-linked (GlcNAc...)Sequence analysis
Glycosylationi4329 – 43291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi4336 ↔ 4344By similarity
Disulfide bondi4340 ↔ 4353By similarity
Disulfide bondi4355 ↔ 4369By similarity
Disulfide bondi4383 ↔ 4391By similarity
Disulfide bondi4385 ↔ 4401By similarity
Disulfide bondi4403 ↔ 4412By similarity
Modified residuei4464 – 44641PhosphoserineCombined sources
Modified residuei4467 – 44671PhosphoserineBy similarity
Modified residuei4577 – 45771PhosphoserineCombined sources
Modified residuei4624 – 46241PhosphoserineCombined sources
Modified residuei4637 – 46371PhosphothreonineBy similarity
Modified residuei4658 – 46581PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP98158.
PRIDEiP98158.

PTM databases

iPTMnetiP98158.
UniCarbKBiP98158.

Expressioni

Tissue specificityi

Epithelial cells of kidney glomerulus and proximal tubule, lung, epididymis, yolk sac, among others.1 Publication

Interactioni

Subunit structurei

Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex together with a receptor-associated protein (RAP). Binds to ankyrin-repeat family A protein 2 (ANKRA2). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif.

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab2O887972EBI-6306650,EBI-6109302
Ldlrap1D3ZAR13EBI-9251342,EBI-9250714

GO - Molecular functioni

  • hemoglobin binding Source: RGD
  • low-density lipoprotein particle receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi247894. 2 interactions.
DIPiDIP-44866N.
IntActiP98158. 4 interactions.
MINTiMINT-1541513.
STRINGi10116.ENSRNOP00000066394.

Structurei

Secondary structure

1
4660
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1190 – 11945Combined sources
Beta strandi1196 – 11994Combined sources
Helixi1204 – 12063Combined sources
Beta strandi1207 – 12115Combined sources
Beta strandi1214 – 12174Combined sources
Helixi1218 – 12214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I1PNMR-A1185-1229[»]
3V2OX-ray1.89B4448-4466[»]
3V2XX-ray1.85B4455-4465[»]
ProteinModelPortaliP98158.
SMRiP98158. Positions 1185-1263, 2862-2939, 3596-3668.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6439LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini65 – 10541LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini106 – 14439LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini145 – 18137LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini181 – 21939LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini220 – 25839LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini263 – 30745LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini308 – 34639EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 38539EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Repeati435 – 47743LDL-receptor class B 1Add
BLAST
Repeati478 – 52043LDL-receptor class B 2Add
BLAST
Repeati521 – 56747LDL-receptor class B 3Add
BLAST
Repeati568 – 61144LDL-receptor class B 4Add
BLAST
Repeati612 – 65241LDL-receptor class B 5Add
BLAST
Domaini658 – 70447EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Repeati752 – 79443LDL-receptor class B 6Add
BLAST
Repeati795 – 83642LDL-receptor class B 7Add
BLAST
Repeati837 – 88044LDL-receptor class B 8Add
BLAST
Repeati881 – 92444LDL-receptor class B 9Add
BLAST
Domaini969 – 101345EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini1023 – 106139LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini1064 – 110340LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini1108 – 114639LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini1148 – 118639LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST
Domaini1186 – 122540LDL-receptor class A 12PROSITE-ProRule annotationAdd
BLAST
Domaini1229 – 126941LDL-receptor class A 13PROSITE-ProRule annotationAdd
BLAST
Domaini1270 – 130839LDL-receptor class A 14PROSITE-ProRule annotationAdd
BLAST
Domaini1311 – 135141LDL-receptor class A 15PROSITE-ProRule annotationAdd
BLAST
Domaini1350 – 139041EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini1391 – 143040EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati1479 – 152143LDL-receptor class B 10Add
BLAST
Repeati1522 – 156443LDL-receptor class B 11Add
BLAST
Repeati1567 – 161044LDL-receptor class B 12Add
BLAST
Repeati1611 – 165444LDL-receptor class B 13Add
BLAST
Repeati1655 – 169642LDL-receptor class B 14Add
BLAST
Domaini1701 – 174242EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Repeati1791 – 183343LDL-receptor class B 15Add
BLAST
Repeati1834 – 188350LDL-receptor class B 16Add
BLAST
Repeati1884 – 193148LDL-receptor class B 17Add
BLAST
Repeati1932 – 197241LDL-receptor class B 18Add
BLAST
Repeati1973 – 201442LDL-receptor class B 19Add
BLAST
Domaini2019 – 206042EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati2108 – 215750LDL-receptor class B 20Add
BLAST
Repeati2158 – 220245LDL-receptor class B 21Add
BLAST
Repeati2203 – 224644LDL-receptor class B 22Add
BLAST
Repeati2247 – 229044LDL-receptor class B 23Add
BLAST
Repeati2291 – 233242LDL-receptor class B 24Add
BLAST
Domaini2343 – 238442EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Repeati2433 – 247846LDL-receptor class B 25Add
BLAST
Repeati2479 – 251941LDL-receptor class B 26Add
BLAST
Repeati2520 – 256344LDL-receptor class B 27Add
BLAST
Repeati2564 – 260441LDL-receptor class B 28Add
BLAST
Repeati2605 – 264743LDL-receptor class B 29Add
BLAST
Domaini2652 – 269443EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini2699 – 273941LDL-receptor class A 16PROSITE-ProRule annotationAdd
BLAST
Domaini2740 – 277839LDL-receptor class A 17PROSITE-ProRule annotationAdd
BLAST
Domaini2779 – 282042LDL-receptor class A 18PROSITE-ProRule annotationAdd
BLAST
Domaini2821 – 286242LDL-receptor class A 19PROSITE-ProRule annotationAdd
BLAST
Domaini2863 – 290341LDL-receptor class A 20PROSITE-ProRule annotationAdd
BLAST
Domaini2906 – 294742LDL-receptor class A 21PROSITE-ProRule annotationAdd
BLAST
Domaini2948 – 299245LDL-receptor class A 22PROSITE-ProRule annotationAdd
BLAST
Domaini2993 – 303139LDL-receptor class A 23PROSITE-ProRule annotationAdd
BLAST
Domaini3032 – 307241LDL-receptor class A 24PROSITE-ProRule annotationAdd
BLAST
Domaini3075 – 311238LDL-receptor class A 25PROSITE-ProRule annotationAdd
BLAST
Domaini3113 – 315341EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini3154 – 319441EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati3241 – 328343LDL-receptor class B 30Add
BLAST
Repeati3284 – 332643LDL-receptor class B 31Add
BLAST
Repeati3335 – 337844LDL-receptor class B 32Add
BLAST
Repeati3379 – 342042LDL-receptor class B 33Add
BLAST
Repeati3421 – 346242LDL-receptor class B 34Add
BLAST
Domaini3467 – 351145EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini3512 – 355241LDL-receptor class A 26PROSITE-ProRule annotationAdd
BLAST
Domaini3553 – 359341LDL-receptor class A 27PROSITE-ProRule annotationAdd
BLAST
Domaini3594 – 363441LDL-receptor class A 28PROSITE-ProRule annotationAdd
BLAST
Domaini3635 – 367541LDL-receptor class A 29PROSITE-ProRule annotationAdd
BLAST
Domaini3678 – 371841LDL-receptor class A 30PROSITE-ProRule annotationAdd
BLAST
Domaini3719 – 375840LDL-receptor class A 31PROSITE-ProRule annotationAdd
BLAST
Domaini3759 – 379739LDL-receptor class A 32PROSITE-ProRule annotationAdd
BLAST
Domaini3798 – 383639LDL-receptor class A 33PROSITE-ProRule annotationAdd
BLAST
Domaini3842 – 388241LDL-receptor class A 34PROSITE-ProRule annotationAdd
BLAST
Domaini3883 – 392442LDL-receptor class A 35PROSITE-ProRule annotationAdd
BLAST
Domaini3928 – 396639LDL-receptor class A 36PROSITE-ProRule annotationAdd
BLAST
Domaini3968 – 400841EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini4009 – 405042EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati4156 – 419843LDL-receptor class B 35Add
BLAST
Repeati4199 – 424244LDL-receptor class B 36Add
BLAST
Repeati4244 – 428542LDL-receptor class B 37Add
BLAST
Domaini4332 – 437039EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini4379 – 441335EGF-like 17PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4597 – 461014Interaction with DAB2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1743 – 17453Cell attachment siteSequence analysis
Motifi4454 – 446310SH3-bindingSequence analysis
Motifi4522 – 45276Endocytosis signalSequence analysis
Motifi4601 – 46066NPXY motif
Motifi4606 – 46094SH2-bindingSequence analysis
Motifi4619 – 463012SH3-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 17 EGF-like domains.PROSITE-ProRule annotation
Contains 36 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 37 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
HOGENOMiHOG000231853.
HOVERGENiHBG097941.
InParanoidiP98158.
KOiK06233.
PhylomeDBiP98158.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
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.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 35 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 22 hits.
SM00179. EGF_CA. 9 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 36 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 35 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 8 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P98158-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT
60 70 80 90 100
RDCLDDTDEI GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ
110 120 130 140 150
QNCAGTTCSA QQMTCSNGQC IPSEYRCDHV SDCPDGSDER NCHYPTCDQL
160 170 180 190 200
TCANGACYNT SQRCDQKVDC RDSSDEANCT TLCSQKEFEC GSGECILRAY
210 220 230 240 250
VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV CDGDDDCQDS
260 270 280 290 300
GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV
310 320 330 340 350
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD
360 370 380 390 400
CQIWGICDQK CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG
410 420 430 440 450
RDLLVGDLHG RNFRILAESK NRGMVMGVDF HYQKHRVFWT DPMQEKVFST
460 470 480 490 500
DINGLNTQEI LNVSVDTPEN LAVDWINNKL YLVETKVNRI DVVNLEGNQR
510 520 530 540 550
VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA FMDGSNRKDL
560 570 580 590 600
VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
610 620 630 640 650
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY
660 670 680 690 700
HALRQPNATN PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE
710 720 730 740 750
HRCVAVKNFL LFSSKTAVRG IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ
760 770 780 790 800
HSTVFYSDLS KDIIYKQKID GTGKEVITAN RLESVECLTF DWISRNLYWT
810 820 830 840 850
DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF LSDWFRPAKI
860 870 880 890 900
MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG
910 920 930 940 950
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR
960 970 980 990 1000
RGISSVMHVK AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP
1010 1020 1030 1040 1050
YGMKLQRDQM TCEGDPAREP PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC
1060 1070 1080 1090 1100
HDNSDEHQCG VFNNTCSPSA FACVRGGQCI PGQWHCDRQN DCLDGSDEQN
1110 1120 1130 1140 1150
CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD EKNCQASGTC
1160 1170 1180 1190 1200
QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS
1210 1220 1230 1240 1250
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE
1260 1270 1280 1290 1300
CDGHPDCIHG SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM
1310 1320 1330 1340 1350
SDEKDCPTQP FHCPSTQWQC PGYSTCINLS ALCDGVFDCP NGTDESPLCN
1360 1370 1380 1390 1400
QDSCSHFNGG CTHQCMQGPF GATCLCPLGY QLANDTKTCE DINECDIPGF
1410 1420 1430 1440 1450
CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV VASRDKIIVD
1460 1470 1480 1490 1500
NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD
1510 1520 1530 1540 1550
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK
1560 1570 1580 1590 1600
NVTKPRGLAL DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW
1610 1620 1630 1640 1650
PCGLSIDYPN RLIYFMDAYL DYIEFCDYDG HNRRQVIASD LVLHHPHALT
1660 1670 1680 1690 1700
LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV MYSVHQPLGI TAIHPSRQPP
1710 1720 1730 1740 1750
SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN CVRGDQPFLM
1760 1770 1780 1790 1800
SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
1810 1820 1830 1840 1850
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT
1860 1870 1880 1890 1900
LKGDTRYGKT LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK
1910 1920 1930 1940 1950
IASANMDGTS LKILFTGNLQ HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD
1960 1970 1980 1990 2000
GTERMILVHH LAHPWGLVVY GSFLYYSDEQ YEVIERVDKS SGNNKVVLRD
2010 2020 2030 2040 2050
NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG MFSCACASGF
2060 2070 2080 2090 2100
KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
2110 2120 2130 2140 2150
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG
2160 2170 2180 2190 2200
VALDWAAGNL YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP
2210 2220 2230 2240 2250
KHRYLFWADY GQKPKIERSF LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY
2260 2270 2280 2290 2300
WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT PYGITVFGES IIWVDRNLKK
2310 2320 2330 2340 2350
VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA ELNNNPCLQS
2360 2370 2380 2390 2400
NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR
2410 2420 2430 2440 2450
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV
2460 2470 2480 2490 2500
SLYSGSSSPT VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN
2510 2520 2530 2540 2550
RAVIARVSKP RAIVLDPCRG YMYWTDWGTN AKIERATLGG NFRVPIVNTS
2560 2570 2580 2590 2600
LVWPNGLALD LETDLLYWAD ASLQKIERST LTGTNREVVV STAFHSFGLT
2610 2620 2630 2640 2650
VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG ISTVVKTQRQ
2660 2670 2680 2690 2700
QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR
2710 2720 2730 2740 2750
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG
2760 2770 2780 2790 2800
NGRCVPYHYR CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV
2810 2820 2830 2840 2850
CNGINNCHDN DTSDEKNCPP HTCPPDFTKC QTTNICVPRA FLCDGDNDCG
2860 2870 2880 2890 2900
DGSDENPIYC ASHTCRSNEF QCLSPQRCIP SYWFCDGEAD CADGSDEPDT
2910 2920 2930 2940 2950
CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED QRHHCELQNC
2960 2970 2980 2990 3000
SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF
3010 3020 3030 3040 3050
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF
3060 3070 3080 3090 3100
FVCDEDNDCG DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD
3110 3120 3130 3140 3150
DCSDNSDEKG CGINECLDSS ISRCDHNCTD TITSFYCSCL PGYKLMSDKR
3160 3170 3180 3190 3200
SCVDIDECKE SPQLCSQKCE NVVGSYICKC APGYIREPDG KSCRQNSNIE
3210 3220 3230 3240 3250
PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE KRLYWIDAEK
3260 3270 3280 3290 3300
QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
3310 3320 3330 3340 3350
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR
3360 3370 3380 3390 3400
IGMDGTNKSV IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH
3410 3420 3430 3440 3450
RHTVYDGSLP HPFALTIFED TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT
3460 3470 3480 3490 3500
HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH LCLIKAGGRG FTCACPDDFQ
3510 3520 3530 3540 3550
TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC SDGSDEPDLC
3560 3570 3580 3590 3600
PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE
3610 3620 3630 3640 3650
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI
3660 3670 3680 3690 3700
PQSWKCDVDN DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV
3710 3720 3730 3740 3750
CNGFDDCRDN SDEQGCESVP CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN
3760 3770 3780 3790 3800
SDEENCVPRE CSESEFRCAD QQCIPSRWVC DQENDCGDNS DERDCEMKTC
3810 3820 3830 3840 3850
HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN GTYCPAAMFE
3860 3870 3880 3890 3900
CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY
3910 3920 3930 3940 3950
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD
3960 3970 3980 3990 4000
NVNDCGDLSD ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS
4010 4020 4030 4040 4050
TSDKNSCQDI NECEEFGICP QSCRNSKGSY ECFCVDGFKS MSTHYGERCA
4060 4070 4080 4090 4100
ADGSPPLLLL PENVRIRKYN TSSEKFSEYL EEEEHIQTID YDWDPEHIGL
4110 4120 4130 4140 4150
SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL KYLMQPDGLA
4160 4170 4180 4190 4200
VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
4210 4220 4230 4240 4250
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD
4260 4270 4280 4290 4300
SKEDVIEAIK YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN
4310 4320 4330 4340 4350
KFGKENKEKV LVVNPWLTQV RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG
4360 4370 4380 4390 4400
YSCACPQGSD FVTGSTVQCD AASELPVTMP PPCRCMHGGN CYFDENELPK
4410 4420 4430 4440 4450
CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA LVLVGLFHYR
4460 4470 4480 4490 4500
KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
4510 4520 4530 4540 4550
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT
4560 4570 4580 4590 4600
VPENVENQNY GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN
4610 4620 4630 4640 4650
FENPIYAEMD SEVKDAVAVA PPPSPSLPAK ASKRNLTPGY TATEDTFKDT
4660
ANLVKEDSDV
Length:4,660
Mass (Da):519,276
Last modified:October 1, 1996 - v1
Checksum:iE2A0CFD23D0923C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34049 mRNA. Translation: AAA51369.1.
PIRiT42737.
RefSeqiNP_110454.1. NM_030827.1.
UniGeneiRn.26430.

Genome annotation databases

GeneIDi29216.
KEGGirno:29216.
UCSCiRGD:68407. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34049 mRNA. Translation: AAA51369.1.
PIRiT42737.
RefSeqiNP_110454.1. NM_030827.1.
UniGeneiRn.26430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I1PNMR-A1185-1229[»]
3V2OX-ray1.89B4448-4466[»]
3V2XX-ray1.85B4455-4465[»]
ProteinModelPortaliP98158.
SMRiP98158. Positions 1185-1263, 2862-2939, 3596-3668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247894. 2 interactions.
DIPiDIP-44866N.
IntActiP98158. 4 interactions.
MINTiMINT-1541513.
STRINGi10116.ENSRNOP00000066394.

PTM databases

iPTMnetiP98158.
UniCarbKBiP98158.

Proteomic databases

PaxDbiP98158.
PRIDEiP98158.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29216.
KEGGirno:29216.
UCSCiRGD:68407. rat.

Organism-specific databases

CTDi4036.
RGDi68407. Lrp2.

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
HOGENOMiHOG000231853.
HOVERGENiHBG097941.
InParanoidiP98158.
KOiK06233.
PhylomeDBiP98158.

Miscellaneous databases

EvolutionaryTraceiP98158.
NextBioi608401.
PROiP98158.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
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.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 35 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 22 hits.
SM00179. EGF_CA. 9 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 36 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 35 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 8 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete cloning and sequencing of rat gp330/'megalin,' a distinctive member of the low density lipoprotein receptor gene family."
    Saito A., Pietromonaco S., Loo A.K.C., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 91:9725-9729(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  2. "Evidence that epithelial glycoprotein 330/megalin mediates uptake of polybasic drugs."
    Moestrup S.K., Cui S., Vorum H., Bregengaard C., Bjorn S.E., Norris K., Gliemann J., Christensen E.I.
    J. Clin. Invest. 96:1404-1413(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UPTAKE OF POLYBASIC DRUGS.
  3. "Organ distribution in rats of two members of the low-density lipoprotein receptor gene family, gp330 and LRP/alpa 2MR, and the receptor-associated protein (RAP)."
    Zheng G., Bachinsky D.R., Stamenkovic I., Strickland D.K., Brown D., Andres G., McCluskey R.T.
    J. Histochem. Cytochem. 42:531-542(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4464; SER-4577; SER-4624 AND SER-4658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin."
    Wolf C.A., Dancea F., Shi M., Bade-Noskova V., Ruterjans H., Kerjaschki D., Lucke C.
    J. Biomol. NMR 37:321-328(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1185-1229, CALCIUM-BINDING SITE, DISULFIDE BONDS.

Entry informationi

Entry nameiLRP2_RAT
AccessioniPrimary (citable) accession number: P98158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 141 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.