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Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)

 LRP2_MOUSE              Reviewed;        4660 AA.
A2ARV4; P70215; Q3TL35; Q9JLB3;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
22-NOV-2017, entry version 107.
RecName: Full=Low-density lipoprotein receptor-related protein 2;
Short=LRP-2;
AltName: Full=Glycoprotein 330;
Short=gp330;
AltName: Full=Megalin;
Flags: Precursor;
Name=Lrp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4054-4660.
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4198-4320.
STRAIN=NMRI; TISSUE=Kidney;
Moll S., Menoud P.A., Izui S.;
"Tubular modulation of clusterin in lupus-like glomerulonephritis.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 4465-4660, AND FUNCTION.
PubMed=10766831; DOI=10.1074/jbc.275.16.12003;
Hammad S.M., Barth J.L., Knaak C., Argraves W.S.;
"Megalin acts in concert with cubilin to mediate endocytosis of high
density lipoproteins.";
J. Biol. Chem. 275:12003-12008(2000).
[5]
FUNCTION, INTERACTION WITH GC, AND DISRUPTION PHENOTYPE.
PubMed=10052453;
Nykjaer A., Dragun D., Walther D., Vorum H., Jacobsen C., Herz J.,
Melsen F., Christensen E.I., Willnow T.E.;
"An endocytic pathway essential for renal uptake and activation of the
steroid 25-(OH) vitamin D3.";
Cell 96:507-515(1999).
[6]
INTERACTION WITH DAB2.
PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
Morris S.M., Cooper J.A.;
"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and
interacts with AP-2.";
Traffic 2:111-123(2001).
[7]
INTERACTION WITH SHH.
PubMed=11964399; DOI=10.1074/jbc.M201933200;
McCarthy R.A., Barth J.L., Chintalapudi M.R., Knaak C., Argraves W.S.;
"Megalin functions as an endocytic sonic hedgehog receptor.";
J. Biol. Chem. 277:25660-25667(2002).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12724130; DOI=10.1152/ajprenal.00062.2003;
Gburek J., Birn H., Verroust P.J., Goj B., Jacobsen C., Moestrup S.K.,
Willnow T.E., Christensen E.I.;
"Renal uptake of myoglobin is mediated by the endocytic receptors
megalin and cubilin.";
Am. J. Physiol. 285:F451-F458(2003).
[9]
INTERACTION WITH ANGIOTENSIN-2.
PubMed=15467006; DOI=10.1152/ajprenal.00243.2004;
Gonzalez-Villalobos R., Klassen R.B., Allen P.L., Navar L.G.,
Hammond T.G.;
"Megalin binds and internalizes angiotensin II.";
Am. J. Physiol. 288:F420-F427(2005).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=16143106; DOI=10.1016/j.cell.2005.06.032;
Hammes A., Andreassen T.K., Spoelgen R., Raila J., Hubner N.,
Schulz H., Metzger J., Schweigert F.J., Luppa P.B., Nykjaer A.,
Willnow T.E.;
"Role of endocytosis in cellular uptake of sex steroids.";
Cell 122:751-762(2005).
[11]
FUNCTION, INTERACTION WITH BMP4, AND DISRUPTION PHENOTYPE.
PubMed=15623804; DOI=10.1242/dev.01580;
Spoelgen R., Hammes A., Anzenberger U., Zechner D., Andersen O.M.,
Jerchow B., Willnow T.E.;
"LRP2/megalin is required for patterning of the ventral
telencephalon.";
Development 132:405-414(2005).
[12]
INTERACTION WITH ANGIOTENSIN 1-7.
PubMed=16380466; DOI=10.1152/ajprenal.00164.2005;
Gonzalez-Villalobos R., Klassen R.B., Allen P.L., Johanson K.,
Baker C.B., Kobori H., Navar L.G., Hammond T.G.;
"Megalin binds and internalizes angiotensin-(1-7).";
Am. J. Physiol. 290:F1270-F1275(2006).
[13]
INTERACTION WITH APOM, AND DISRUPTION PHENOTYPE.
PubMed=16099815; DOI=10.1210/me.2005-0209;
Faber K., Hvidberg V., Moestrup S.K., Dahlbaeck B., Nielsen L.B.;
"Megalin is a receptor for apolipoprotein M, and kidney-specific
megalin-deficiency confers urinary excretion of apolipoprotein M.";
Mol. Endocrinol. 20:212-218(2006).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17462596; DOI=10.1016/j.bbrc.2007.04.072;
Kaseda R., Iino N., Hosojima M., Takeda T., Hosaka K., Kobayashi A.,
Yamamoto K., Suzuki A., Kasai A., Suzuki Y., Gejyo F., Saito A.;
"Megalin-mediated endocytosis of cystatin C in proximal tubule
cells.";
Biochem. Biophys. Res. Commun. 357:1130-1134(2007).
[15]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=17846082; DOI=10.1096/fj.07-9171com;
Koenig O., Ruettiger L., Mueller M., Zimmermann U., Erdmann B.,
Kalbacher H., Gross M., Knipper M.;
"Estrogen and the inner ear: megalin knockout mice suffer progressive
hearing loss.";
FASEB J. 22:410-417(2008).
[16]
FUNCTION, AND INTERACTION WITH SEPP1.
PubMed=18174160; DOI=10.1074/jbc.M709945200;
Olson G.E., Winfrey V.P., Hill K.E., Burk R.F.;
"Megalin mediates selenoprotein P uptake by kidney proximal tubule
epithelial cells.";
J. Biol. Chem. 283:6854-6860(2008).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-387 AND ASN-399.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4464; SER-4467;
SER-4577; THR-4637 AND SER-4658, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=20460439; DOI=10.1242/jcs.065912;
Gajera C.R., Emich H., Lioubinski O., Christ A.,
Beckervordersandforth-Bonk R., Yoshikawa K., Bachmann S.,
Christensen E.I., Goetz M., Kempermann G., Peterson A.S.,
Willnow T.E., Hammes A.;
"LRP2 in ependymal cells regulates BMP signaling in the adult
neurogenic niche.";
J. Cell Sci. 123:1922-1930(2010).
[20]
FUNCTION, INTERACTION WITH APPB1 AND APP, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=20637285; DOI=10.1016/j.mcn.2010.07.005;
Alvira-Botero X., Perez-Gonzalez R., Spuch C., Vargas T.,
Antequera D., Garzon M., Bermejo-Pareja F., Carro E.;
"Megalin interacts with APP and the intracellular adapter protein FE65
in neurons.";
Mol. Cell. Neurosci. 45:306-315(2010).
[21]
FUNCTION, AND INDUCTION BY CANNABINOIDS.
PubMed=22841573; DOI=10.1016/j.cmet.2012.07.002;
Tam J., Cinar R., Liu J., Godlewski G., Wesley D., Jourdan T.,
Szanda G., Mukhopadhyay B., Chedester L., Liow J.S., Innis R.B.,
Cheng K., Rice K.C., Deschamps J.R., Chorvat R.J., McElroy J.F.,
Kunos G.;
"Peripheral cannabinoid-1 receptor inverse agonism reduces obesity by
reversing leptin resistance.";
Cell Metab. 16:167-179(2012).
[22]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=22340494; DOI=10.1016/j.devcel.2011.11.023;
Christ A., Christa A., Kur E., Lioubinski O., Bachmann S.,
Willnow T.E., Hammes A.;
"LRP2 is an auxiliary SHH receptor required to condition the forebrain
ventral midline for inductive signals.";
Dev. Cell 22:268-278(2012).
[23]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=22354480; DOI=10.1002/glia.22316;
Ortega M.C., Cases O., Merchan P., Kozyraki R., Clemente D.,
de Castro F.;
"Megalin mediates the influence of sonic hedgehog on oligodendrocyte
precursor cell migration and proliferation during development.";
Glia 60:851-866(2012).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23825075; DOI=10.1152/ajprenal.00546.2012;
Jobst-Schwan T., Knaup K.X., Nielsen R., Hackenbeck T.,
Buettner-Herold M., Lechler P., Kroening S., Goppelt-Struebe M.,
Schloetzer-Schrehardt U., Fuernrohr B.G., Voll R.E., Amann K.,
Eckardt K.U., Christensen E.I., Wiesener M.S.;
"Renal uptake of the antiapoptotic protein survivin is mediated by
megalin at the apical membrane of the proximal tubule.";
Am. J. Physiol. 305:F734-F744(2013).
[25]
FUNCTION.
PubMed=24825475; DOI=10.15252/embr.201338317;
Byun K., Gil S.Y., Namkoong C., Youn B.S., Huang H., Shin M.S.,
Kang G.M., Kim H.K., Lee B., Kim Y.B., Kim M.S.;
"Clusterin/ApoJ enhances central leptin signaling through Lrp2-
mediated endocytosis.";
EMBO Rep. 15:801-808(2014).
[26]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24639464; DOI=10.1242/jcs.140145;
Kur E., Mecklenburg N., Cabrera R.M., Willnow T.E., Hammes A.;
"LRP2 mediates folate uptake in the developing neural tube.";
J. Cell Sci. 127:2261-2268(2014).
[27]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26439398; DOI=10.1016/j.devcel.2015.09.001;
Christ A., Christa A., Klippert J., Eule J.C., Bachmann S.,
Wallace V.A., Hammes A., Willnow T.E.;
"LRP2 acts as SHH clearance receptor to protect the retinal margin
from mitogenic stimuli.";
Dev. Cell 35:36-48(2015).
[28]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26822476; DOI=10.1242/dmm.022053;
Baardman M.E., Zwier M.V., Wisse L.J., Gittenberger-de Groot A.C.,
Kerstjens-Frederikse W.S., Hofstra R.M., Jurdzinski A., Hierck B.P.,
Jongbloed M.R., Berger R.M., Ploesch T., DeRuiter M.C.;
"Common arterial trunk and ventricular non-compaction in Lrp2 knockout
mice indicate a crucial role of LRP2 in cardiac development.";
Dis. Model. Mech. 9:413-425(2016).
[29]
GLYCOSYLATION.
PubMed=27773703; DOI=10.1016/j.bbagen.2016.10.015;
Hirano M., Totani K., Fukuda T., Gu J., Suzuki A.;
"N-glycoform-dependent interactions of megalin with its ligands.";
Biochim. Biophys. Acta 1861:3106-3118(2017).
[30]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28659595; DOI=10.1038/s41598-017-04648-y;
Johanns M., Lemoine P., Janssens V., Grieco G., Moestrup S.K.,
Nielsen R., Christensen E.I., Courtoy P.J., Emonard H., Marbaix E.,
Henriet P.;
"Cellular uptake of proMMP-2:TIMP-2 complexes by the endocytic
receptor megalin/LRP-2.";
Sci. Rep. 7:4328-4328(2017).
-!- FUNCTION: Multiligand endocytic receptor. Acts together with CUBN
to mediate endocytosis of high-density lipoproteins
(PubMed:10766831). Mediates receptor-mediated uptake of polybasic
drugs such as aprotinin, aminoglycosides and polymyxin B (By
similarity). In the kidney, mediates the tubular uptake and
clearance of leptin (PubMed:22841573). Also mediates transport of
leptin across the blood-brain barrier through endocytosis at the
choroid plexus epithelium (By similarity). Endocytosis of leptin
in neuronal cells is required for hypothalamic leptin signaling
and leptin-mediated regulation of feeding and body weight
(PubMed:24825475). Mediates endocytosis and subsequent lysosomal
degradation of CST3 in kidney proximal tubule cells
(PubMed:17462596). Mediates renal uptake of 25-hydroxyvitamin D3
in complex with the vitamin D3 transporter GC/DBP
(PubMed:10052453). Mediates renal uptake of metallothionein-bound
heavy metals (By similarity). Together with CUBN, mediates renal
reabsorption of myoglobin (By similarity). Mediates renal uptake
and subsequent lysosomal degradation of APOM (By similarity).
Plays a role in kidney selenium homeostasis by mediating renal
endocytosis of selenoprotein SEPP1 (PubMed:18174160). Mediates
renal uptake of the antiapoptotic protein BIRC5/survivin which may
be important for functional integrity of the kidney
(PubMed:23825075). Mediates renal uptake of matrix
metalloproteinase MMP2 in complex with metalloproteinase inhibitor
TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog
protein N-product (ShhN), the active product of SHH (By
similarity). Also mediates ShhN transcytosis (By similarity). In
the embryonic neuroepithelium, mediates endocytic uptake and
degradation of BMP4, is required for correct SHH localization in
the ventral neural tube and plays a role in patterning of the
ventral telencephalon (PubMed:15623804). Required at the onset of
neurulation to sequester SHH on the apical surface of
neuroepithelial cells of the rostral diencephalon ventral midline
and to control PTCH1-dependent uptake and intracellular
trafficking of SHH (PubMed:22340494). During neurulation, required
in neuroepithelial cells for uptake of folate bound to the folate
receptor FOLR1 which is necessary for neural tube closure
(PubMed:24639464). In the adult brain, negatively regulates BMP
signaling in the subependymal zone which enables neurogenesis to
proceed (PubMed:20460439). In astrocytes, mediates endocytosis of
ALB which is required for the synthesis of the neurotrophic factor
oleic acid (By similarity). Involved in neurite branching
(PubMed:20637285). During optic nerve development, required for
SHH-mediated migration and proliferation of oligodendrocyte
precursor cells (PubMed:22354480). Mediates endocytic uptake and
clearance of SHH in the retinal margin which protects retinal
progenitor cells from mitogenic stimuli and keeps them quiescent
(PubMed:26439398). Plays a role in reproductive organ development
by mediating uptake in reproductive tissues of androgen and
estrogen bound to the sex hormone binding protein SHBG
(PubMed:16143106). Mediates endocytosis of angiotensin-2 (By
similarity). Also mediates endocytosis of angiotensin 1-7 (By
similarity). Binds to the complex composed of beta-amyloid protein
40 and CLU/APOJ and mediates its endocytosis and lysosomal
degradation (By similarity). Required for embryonic heart
development (PubMed:26822476). Required for normal hearing,
possibly through interaction with estrogen in the inner ear
(PubMed:17846082). {ECO:0000250|UniProtKB:C0HL13,
ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164,
ECO:0000269|PubMed:10052453, ECO:0000269|PubMed:10766831,
ECO:0000269|PubMed:15623804, ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:17462596,
ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18174160,
ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:20637285,
ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480,
ECO:0000269|PubMed:22841573, ECO:0000269|PubMed:23825075,
ECO:0000269|PubMed:24639464, ECO:0000269|PubMed:24825475,
ECO:0000269|PubMed:26439398, ECO:0000269|PubMed:26822476,
ECO:0000269|PubMed:28659595}.
-!- SUBUNIT: 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 LRPAP1 (By similarity). Interacts (via PxLPxI/L
motif) with ANKRA2 (via ankyrin repeats) (By similarity).
Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the
interaction is not affected by tyrosine phosphorylation of the
NPXY motif (PubMed:11247302). Interacts with MB (By similarity).
Interacts with BMP4 (PubMed:15623804). Interacts with the Sonic
hedgehog protein N-product which is the active product of SHH
(PubMed:11964399). Interacts with CST3 in a calcium-dependent
manner (By similarity). Interacts with the vitamin-D binding
protein GC/DBP (PubMed:10052453). Interacts with sex hormone-
binding protein SHBG (By similarity). Interacts with angiotensin-2
(PubMed:15467006). Also interacts with angiotensin 1-7
(PubMed:16380466). Interacts with APOM (PubMed:16099815).
Interacts with selenoprotein SEPP1 (PubMed:18174160). Interacts
with LEP (By similarity). Interacts with ALB (By similarity).
Interacts with the antiapoptotic protein BIRC5/survivin (By
similarity). Interacts with matrix metalloproteinase MMP2 in
complex with metalloproteinase inhibitor TIMP1 (By similarity). In
neurons, forms a trimeric complex with APP and APPB1/FE65
(PubMed:20637285). Interacts with LDLRAP1/ARH; mediates
trafficking of LRP2 to the endocytic recycling compartment (By
similarity). Does not interact with beta-amyloid protein 40 alone
but interacts with the complex composed of beta-amyloid protein 40
and CLU/APOJ (By similarity). {ECO:0000250|UniProtKB:C0HL13,
ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164,
ECO:0000269|PubMed:10052453, ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:11964399, ECO:0000269|PubMed:15467006,
ECO:0000269|PubMed:15623804, ECO:0000269|PubMed:16099815,
ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:18174160,
ECO:0000269|PubMed:20637285}.
-!- INTERACTION:
P97318:Dab1; NbExp=2; IntAct=EBI-300875, EBI-81680;
Q62108:Dlg4; NbExp=2; IntAct=EBI-300875, EBI-300895;
Q9Z0G0:Gipc1; NbExp=2; IntAct=EBI-300875, EBI-300855;
Q9WVI9:Mapk8ip1; NbExp=2; IntAct=EBI-300875, EBI-74515;
Q9ERE9:Mapk8ip2; NbExp=2; IntAct=EBI-300875, EBI-74576;
Q9D6K5:Synj2bp; NbExp=2; IntAct=EBI-300875, EBI-300910;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:20460439,
ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480}; Single-
pass type I membrane protein {ECO:0000255}. Endosome lumen
{ECO:0000250|UniProtKB:P98158}. Membrane, coated pit
{ECO:0000269|PubMed:22340494}. Cell projection, dendrite
{ECO:0000269|PubMed:20637285}. Cell projection, axon
{ECO:0000269|PubMed:20637285}. Note=Localizes to brush border
membranes in the kidney. In the endolymphatic sac of the inner
ear, located in the lumen of endosomes as a soluble form.
{ECO:0000250|UniProtKB:P98158}.
-!- TISSUE SPECIFICITY: In the inner ear, strongly expressed in the
marginal cells of the stria vascularis (at protein level)
(PubMed:17846082). In the female reproductive tract, expressed on
the luminal side of the uterine epithelium (at protein level)
(PubMed:16143106). In the adult brain, expressed in ependymal
cells of the lateral ventricles where expression is restricted to
the ependyma that faces the stem cell niche (at protein level)
(PubMed:20460439). Expressed in neurons throughout the brain
including in the hippocampus, limbic cortices and cerebellum (at
protein level) (PubMed:20637285). In the developing optic nerve,
expressed exclusively in astrocytes at E14.5, E16.5 and E18.5 (at
protein level) (PubMed:22354480). {ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:20460439,
ECO:0000269|PubMed:20637285, ECO:0000269|PubMed:22354480}.
-!- DEVELOPMENTAL STAGE: In the developing optic nerve, more strongly
expressed at E14.5 and E16.5 than at E18.5 (at protein level)
(PubMed:22354480). In the embryo, expression is detected from E7.5
on the apical side of the developing neural plate and persists
throughout later stages of development (PubMed:22340494). After
neural tube closure at E9.5, becomes progressively restricted to
the midline region (PubMed:22340494). During the estrus cycle,
expression is highest in metestrus II and diestrus
(PubMed:16143106). {ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480}.
-!- INDUCTION: Down-regulated in the kidney by cannabinoids, such as
endocannabinoid anandamide and synthetic cannabinoid HU-210.
{ECO:0000269|PubMed:22841573}.
-!- DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with
ankyrin repeats of ANKRA2. {ECO:0000250|UniProtKB:P98158}.
-!- DOMAIN: The cytoplasmic domain is required for sorting to the
apical cell membrane. {ECO:0000250|UniProtKB:P98158}.
-!- PTM: A fraction undergoes proteolytic cleavage of the
extracellular domain at the cell membrane to generate a
cytoplasmic tail fragment. This is internalized into the early
endosome from where it trafficks in an LDLRAP1/ARH-dependent
manner to the endocytic recycling compartment (ERC). In the ERC,
it is further cleaved by gamma-secretase to release a fragment
which translocates to the nucleus and mediates transcriptional
repression. {ECO:0000250|UniProtKB:P98158}.
-!- PTM: N-glycosylation is required for ligand binding. Contains
core-fucosylated N-glycans in kidney proximal convoluted tubules
(PCTs) and hybrid-type N-glycans in proximal straight tubules
(PSTs). Interacts with ligands in a glycoform-dependent manner.
Retinol-binding protein and the vitamin D carrier GC/DBP are
endocytosed primarily by PCTs, albumin is endocytosed equally by
PCTs and PSTs, and the aminoglycoside kanamycin is endocytosed
primarily by PSTs. {ECO:0000269|PubMed:27773703}.
-!- DISRUPTION PHENOTYPE: Severe facial dysgenesis and impaired
forebrain development around mid-gestation, absence of Shh
expression and decreased cell proliferation in the ventral neural
tube, and aberrant expression of morphogens Fgf8 and Bmp4
(PubMed:15623804). Reduced expression of homeobox protein Six3 at
E8.0 in the prospective forebrain and impaired Shh expression at
the ventral midline with resulting midline formation defects and
holoprosencephaly (PubMed:22340494). At E9.5, loss of Shh in the
ventral anterior diencephalon and increased Bmp4 expression in the
dorsal forebrain (PubMed:22340494). Increased Bmp4 expression and
impaired proliferation of neural precursor cells in the
subependymal zone of the brain which results in decreased numbers
of neuroblasts reaching the olfactory bulb (PubMed:20460439).
Compound heterozygotes display enlarged and exophthalmic eyes with
thinning of the retina (PubMed:26439398). Severe cardiovascular
abnormalities including aortic arch anomalies, persistent truncus
arteriosus with coronary artery anomalies, ventricular septal
defects, overriding of the tricuspid valve, marked thinning of the
ventricular myocardium, and abnormal positioning of the neural
crest cells and second heart field (PubMed:26822476). Impaired
endocytosis of folate bound to the folate receptor FOLR1, reduced
folate levels in embryos and impaired closure of the rostral
neural tube (PubMed:24639464). High lethality at and after birth
with survivors showing profound hearing loss, elevated lipofuscin
granule levels and irregular apical surfaces in marginal cells of
the stria vascularis, complete loss of potassium ion channel KCQN1
in basal and midbasal cochlear turns, and reduced estrogen uptake
in the stria vascularis (PubMed:17846082). Survivors also display
severe vitamin D deficiency and bone formation defects
(PubMed:10052453). Failure of the vaginal cavity to open after
birth in females and impaired testis descent in males with the
left testis poorly developed and severely retarded in size
(PubMed:16143106). Conditional knockout in the kidney results in
reduced expression of CUBN in kidney cells and little or no uptake
of myoglobin (PubMed:12724130). It also results in reduced uptake
of Cst3 by kidney proximal tubule cells (PubMed:17462596). In
addition, it causes pronounced urinary excretion of Apom,
Birc5/survivin, and Mmp2 together with Timp1 (PubMed:16099815,
PubMed:23825075, PubMed:28659595). {ECO:0000269|PubMed:10052453,
ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:15623804,
ECO:0000269|PubMed:16099815, ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:17846082,
ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:22340494,
ECO:0000269|PubMed:23825075, ECO:0000269|PubMed:24639464,
ECO:0000269|PubMed:26439398, ECO:0000269|PubMed:26822476,
ECO:0000269|PubMed:28659595}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL845489; CAM20178.1; -; Genomic_DNA.
EMBL; AK166702; BAE38957.1; -; mRNA.
EMBL; Y08566; CAA69877.1; -; mRNA.
EMBL; AF197160; AAF61488.1; -; mRNA.
CCDS; CCDS38135.1; -.
RefSeq; NP_001074557.1; NM_001081088.1.
UniGene; Mm.23847; -.
ProteinModelPortal; A2ARV4; -.
BioGrid; 200005; 5.
IntAct; A2ARV4; 11.
MINT; MINT-4106203; -.
STRING; 10090.ENSMUSP00000079752; -.
TCDB; 9.B.87.1.1; the selenoprotein p receptor (selp-receptor) family.
iPTMnet; A2ARV4; -.
PhosphoSitePlus; A2ARV4; -.
MaxQB; A2ARV4; -.
PaxDb; A2ARV4; -.
PeptideAtlas; A2ARV4; -.
PRIDE; A2ARV4; -.
Ensembl; ENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070.
GeneID; 14725; -.
KEGG; mmu:14725; -.
UCSC; uc008jyc.1; mouse.
CTD; 4036; -.
MGI; MGI:95794; Lrp2.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XP34; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000230574; -.
HOVERGEN; HBG097941; -.
InParanoid; A2ARV4; -.
KO; K06233; -.
OMA; PNGDCSH; -.
OrthoDB; EOG091G000N; -.
PhylomeDB; A2ARV4; -.
TreeFam; TF315253; -.
Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-975634; Retinoid metabolism and transport.
PRO; PR:A2ARV4; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027070; -.
ExpressionAtlas; A2ARV4; baseline and differential.
Genevisible; A2ARV4; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005903; C:brush border; IDA:MGI.
GO; GO:0031526; C:brush border membrane; IDA:MGI.
GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0004872; F:receptor activity; ISS:MGI.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0035258; F:steroid hormone receptor binding; ISS:UniProtKB.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0060982; P:coronary artery morphogenesis; IMP:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:1904447; P:folic acid import across plasma membrane; IMP:UniProtKB.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0008584; P:male gonad development; IMP:UniProtKB.
GO; GO:0030001; P:metal ion transport; ISS:UniProtKB.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:UniProtKB.
GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
GO; GO:0140058; P:neuron projection arborization; IMP:UniProtKB.
GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IMP:UniProtKB.
GO; GO:0061156; P:pulmonary artery morphogenesis; IMP:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
GO; GO:0003139; P:secondary heart field specification; IMP:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0060068; P:vagina development; IMP:UniProtKB.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IMP:UniProtKB.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
GO; GO:0006766; P:vitamin metabolic process; IMP:MGI.
CDD; cd00112; LDLa; 36.
Gene3D; 2.120.10.30; -; 8.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF12662; cEGF; 2.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 34.
Pfam; PF00058; Ldl_recept_b; 17.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 25.
SMART; SM00179; EGF_CA; 9.
SMART; SM00192; LDLa; 36.
SMART; SM00135; LY; 37.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF57424; SSF57424; 35.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS01209; LDLRA_1; 31.
PROSITE; PS50068; LDLRA_2; 36.
PROSITE; PS51120; LDLRB; 36.
1: Evidence at protein level;
Calcium; Cell membrane; Cell projection; Coated pit;
Complete proteome; Disulfide bond; EGF-like domain; Endocytosis;
Endosome; Glycoprotein; Hearing; Membrane; Metal-binding;
Neurogenesis; Phosphoprotein; Receptor; Reference proteome; Repeat;
SH3-binding; Signal; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 4660 Low-density lipoprotein receptor-related
protein 2.
/FTId=PRO_0000309845.
TOPO_DOM 26 4425 Extracellular. {ECO:0000255}.
TRANSMEM 4426 4446 Helical. {ECO:0000255}.
TOPO_DOM 4447 4660 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 63 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 66 104 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 107 143 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 146 180 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 182 218 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 221 257 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 264 307 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REPEAT 435 477 LDL-receptor class B 1.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 478 520 LDL-receptor class B 2.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 521 567 LDL-receptor class B 3.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 568 612 LDL-receptor class B 4.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 752 794 LDL-receptor class B 5.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 795 836 LDL-receptor class B 6.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 837 880 LDL-receptor class B 7.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 881 924 LDL-receptor class B 8.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 1024 1060 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1065 1102 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1109 1145 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1149 1185 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1187 1224 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1230 1268 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1271 1307 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1312 1350 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1350 1390 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1391 1430 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 1479 1521 LDL-receptor class B 9.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1522 1564 LDL-receptor class B 10.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1567 1610 LDL-receptor class B 11.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1611 1655 LDL-receptor class B 12.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1656 1696 LDL-receptor class B 13.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1791 1833 LDL-receptor class B 14.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1834 1883 LDL-receptor class B 15.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1884 1931 LDL-receptor class B 16.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1932 1973 LDL-receptor class B 17.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1974 2014 LDL-receptor class B 18.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2108 2157 LDL-receptor class B 19.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2158 2202 LDL-receptor class B 20.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2203 2246 LDL-receptor class B 21.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2247 2290 LDL-receptor class B 22.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2291 2333 LDL-receptor class B 23.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2432 2478 LDL-receptor class B 24.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2479 2519 LDL-receptor class B 25.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2520 2563 LDL-receptor class B 26.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2564 2605 LDL-receptor class B 27.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2606 2647 LDL-receptor class B 28.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 2700 2738 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2741 2777 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2780 2819 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2822 2861 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2864 2902 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2907 2946 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2949 2991 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2994 3030 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3033 3071 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3076 3112 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3112 3153 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3154 3194 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3241 3283 LDL-receptor class B 29.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3284 3326 LDL-receptor class B 30.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3335 3378 LDL-receptor class B 31.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3379 3421 LDL-receptor class B 32.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3422 3462 LDL-receptor class B 33.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 3513 3551 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3554 3592 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3595 3633 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3636 3674 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3679 3717 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3720 3757 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3760 3796 LDL-receptor class A 32.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3799 3835 LDL-receptor class A 33.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3843 3881 LDL-receptor class A 34.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3884 3923 LDL-receptor class A 35.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3929 3965 LDL-receptor class A 36.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 4009 4050 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 4156 4198 LDL-receptor class B 34.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4199 4242 LDL-receptor class B 35.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4244 4285 LDL-receptor class B 36.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 4379 4413 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4597 4610 Interaction with DAB2.
{ECO:0000250|UniProtKB:P98164}.
MOTIF 4454 4463 SH3-binding. {ECO:0000255}.
MOTIF 4457 4462 PxLPxI/L motif 1; mediates interaction
with ANKRA2.
{ECO:0000250|UniProtKB:P98158}.
MOTIF 4460 4465 PxLPxI/L motif 2; mediates interaction
with ANKRA2.
{ECO:0000250|UniProtKB:P98158}.
MOTIF 4522 4527 Endocytosis signal. {ECO:0000255}.
MOTIF 4603 4606 NPXY motif.
MOTIF 4606 4609 SH2-binding. {ECO:0000255}.
MOTIF 4619 4630 SH3-binding. {ECO:0000255}.
METAL 1127 1127 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98164}.
METAL 1130 1130 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1132 1132 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98164}.
METAL 1134 1134 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1140 1140 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1141 1141 Calcium. {ECO:0000250|UniProtKB:P98164}.
METAL 1206 1206 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98158}.
METAL 1209 1209 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1211 1211 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98158}.
METAL 1213 1213 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1219 1219 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1220 1220 Calcium. {ECO:0000250|UniProtKB:P98158}.
MOD_RES 4464 4464 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4467 4467 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4577 4577 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4624 4624 Phosphoserine.
{ECO:0000250|UniProtKB:P98158}.
MOD_RES 4637 4637 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 4658 4658 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 462 462 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1063 1063 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1187 1187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1328 1328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1341 1341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1384 1384 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1451 1451 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1497 1497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1551 1551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1676 1676 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1733 1733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1811 1811 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2131 2131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2134 2134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2178 2178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2225 2225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2396 2396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2488 2488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2548 2548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2782 2782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2810 2810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2949 2949 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2989 2989 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3127 3127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3213 3213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3259 3259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3317 3317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3357 3357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3448 3448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3566 3566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3682 3682 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3840 3840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3969 3969 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3980 3980 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4070 4070 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4329 4329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 40 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 35 53 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 47 62 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 67 80 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 74 93 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 87 103 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 108 120 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 115 133 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 127 142 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 147 157 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 152 170 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 164 179 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 183 195 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 190 208 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 202 217 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 222 234 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 229 247 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 241 256 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 265 278 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 272 291 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 285 306 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1025 1037 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1032 1050 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1044 1059 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1066 1079 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1073 1092 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1086 1101 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1110 1122 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1117 1135 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1129 1144 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1150 1162 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1157 1175 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1169 1184 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1188 1201 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1195 1214 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1208 1223 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1231 1244 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1238 1257 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1251 1267 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1272 1284 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1279 1297 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1291 1306 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1313 1326 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1320 1339 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1333 1349 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1354 1365 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1361 1374 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1376 1389 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1395 1405 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1401 1414 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1416 1429 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2701 2713 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2708 2726 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2720 2737 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2742 2754 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2749 2767 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2761 2776 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2781 2794 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2789 2807 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2801 2818 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2823 2836 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2830 2849 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2843 2860 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2865 2878 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2872 2891 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2885 2901 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2908 2920 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2915 2933 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2927 2945 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2950 2967 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2957 2980 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2974 2990 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2995 3007 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3002 3020 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3014 3029 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3034 3046 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3041 3059 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3053 3070 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3077 3089 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3084 3102 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3096 3111 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3116 3128 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3124 3137 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3139 3152 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3158 3169 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3165 3178 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3180 3193 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3514 3527 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3521 3540 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3534 3550 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3555 3567 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3562 3580 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3574 3591 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3596 3608 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3603 3621 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3615 3632 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3637 3649 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3644 3662 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3656 3673 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3680 3694 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3688 3707 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3701 3716 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3721 3734 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3729 3747 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3741 3756 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3761 3773 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3768 3786 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3780 3795 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3800 3812 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3807 3825 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3819 3834 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3844 3856 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3851 3869 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3863 3880 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3885 3898 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3893 3911 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3905 3922 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3930 3942 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3937 3955 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3949 3964 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 4013 4023 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4019 4032 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4034 4049 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4383 4391 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4385 4401 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4403 4412 {ECO:0000255|PROSITE-ProRule:PRU00076}.
CONFLICT 4198 4198 L -> F (in Ref. 3; CAA69877).
{ECO:0000305}.
SEQUENCE 4660 AA; 519208 MW; 4CF399C24DF2FAA4 CRC64;
MERGAAAAAW MLLLAIAACL APVSGQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI
GCPPRSCGSG FFLCPAEGTC IPSSWVCDQD KDCSDGADEQ QNCPGTTCSS QQLTCSNGQC
VPIEYRCDHV SDCPDGSDER NCYYPTCDQL TCANGACYNT SQKCDHKVDC RDSSDEANCT
TLCSQKEFQC GSGECILRAY VCDHDNDCED NSDEHNCNYD TCGGHQFTCS NGQCINQNWV
CDGDDDCQDS GDEDGCESNQ RHHTCYPREW ACPGSGRCIS MDKVCDGVPD CPEGEDENNA
TSGRYCGTGL CSILNCEYQC HQTPYGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK
CESRQGRHQC LCEEGYILER GQHCKSNDSF SAASIIFSNG RDLLVGDLHG RNFRILAESK
NRGIVMGVDF HYQKHRVFWT DPMQAKVFST DINGLNTQEI LNVSIDAPEN LAVDWINNKL
YLVETRVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA
FMDGSNRKDL VTTKLGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
PHPFGISLFE EHVFFTDWTK MAVMKANKFT DTNPQVYHQS SLTPFGVTVY HALRQPNATN
PCGNNNGGCA QICVLSHRTD NGGLGYRCKC EFGFELDADE HHCVAVKNFL LFSSQTAVRG
IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTIFYSDLS KNIIYQQKID GTGKEVITAN
RLQNVECLSF DWISRNLYWT DGGSKSVTVM KLADKSRRQI ISNLNNPRSI VVHPAAGYMF
LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWST SRLYWVDAFF DKIEHSNLDG
LDRKRLGHVD QMTHPFGLTV FKDNVFLTDW RLGAIIRVRK SDGGDMTVVR RGISSIMHVK
AYDADLQTGT NYCSQTTHPN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP
PTQQCGSSSF PCNNGKCVPS IFRCDGVDDC HDNSDEHQCG ALNNTCSSSA FTCVHGGQCI
PGQWRCDKQN DCLDGSDEQN CPTRSPSSTC PPTSFTCDNH MCIPKEWVCD TDNDCSDGSD
EKNCQASGTC HPTQFRCPDH RCISPLYVCD GDKDCVDGSD EAGCVLNCTS SQFKCADGSS
CINSRYRCDG VYDCKDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIQG
SDEHNGCVPK TCSPSHFLCD NGNCIYNSWV CDGDNDCRDM SDEKDCPTQP FHCPSSQWQC
PGYSICVNLS ALCDGVFDCP NGTDESPLCN QDSCLHFNGG CTHRCIQGPF GATCVCPIGY
QLANDTKTCE DVNECDIPGF CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTASENLLLV
VASRDKIIMD NITAHTHNIY SLVQDVSFVV ALDFDSVTGR VFWSDLLEGK TWSAFQNGTD
KRVVHDSGLS LTEMIAVDWI GRNIYWTDYT LETIEVSKID GSHRTVLISK NVTKPRGLAL
DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW PCGLSIDYPN RLIYFMDAYL
DYIEFCDYDG QNRRQVIASD LVLHHPHALT LFEDSVFWTD RGTHQVMQAN KWHGRNQSVV
MYSVPQPLGI IAIHPSRQPS SPNPCASATC SHLCLLSAQE PRHYSCACPS GWNLSDDSVN
CVRGDQPFLI SVRENVIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
EIHRVKTDGS NRTAFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT LRGDTRYGKT
LITNDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK IASANMDGTS LKILFTGNME
HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD GTERMILVHH LAHPWGLVVH GSFLYYSDEQ
YEVIERVDKS SGSNKVVFRD NIPYLRGLRV YHHRNAADSS NGCSNNPNAC QQICLPVPGG
MFSCACASGF KLSPDGRSCS PYNSFIVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP NGSNFTNIVT YGIGANGIRG VAVDWVAGNL
YFTNAFVYET LIEVIRINTT YRRVLLKVSV DMPRHIVVDP KHRYLFWADY GQKPKIERSF
LDCTNRTVLV SEGIVTPRGL AVDHDTGYIY WVDDSLDIIA RIHRDGGESQ VVRYGSRYPT
PYGITVFGES IIWVDRNLRK VFQASKQPGN TDPPTVIRDS INLLRDVTIF DEHVQPLSPA
ELNNNPCLQS NGGCSHFCFA LPELPTPKCG CAFGTLEDDG KNCATSREDF LIYSLNNSLR
SLHFDPQDHN LPFQAISVEG MAIALDYDRR NNRIFFTQKL NPIRGQISYV NLYSGASSPT
ILLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN RAVIARVSKP RAIVLDPCRG
YMYWTDWGTN AKIERATLGG NFRVPIVNTS LVWPNGLTLD LETDLLYWAD ASLQKIERST
LTGSNREVVI STAFHSFGLT VYGQYIYWTD FYTKKIYRAN KYDGSDLIAM TTRLPTQPSG
ISTVVKTQQQ QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGSWYLANDN KYCVVDTGAR
CNQFQFTCLN GRCISQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCA NGRCVPYHYR
CDFYNDCGDN SDEAGCLFRS CNSTTEFTCS NGRCIPLSYV CNGINNCHDN DTSDEKNCPP
ITCQPDFAKC QTTNICVPRA FLCDGDNDCG DGSDENPIYC ASHTCRSNEF QCVSPHRCIP
SYWFCDGEAD CVDSSDEPDT CGHSLNSCSA NQFHCDNGRC ISSSWVCDGD NDCGDMSDED
QRHHCELQNC SSTEFTCINS RPPNRRCIPQ HWVCDGDADC ADALDELQNC TMRACSTGEF
SCANGRCIRQ SFRCDRRNDC GDYSDERGCS YPPCRDDQFT CQNGQCITKL YVCDEDNDCG
DGSDEQEHLC HTPEPTCPPH QFRCDNGHCI EMGTVCNHVD DCSDNSDEKG CGINECQDSS
ISHCDHNCTD TITSFYCSCL PGYKLMSDKR TCVDIDECKE TPQLCSQKCE NVIGSYICKC
APGYIREPDG KSCRQNSNIE PYLVFSNRYY IRNLTIDGTS YSLILQGLGN VVALDFDRVE
ERLYWIDAEK QIIERMFLNK TNQETIISHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
LEGRQRKMLA QHCVDANNTF CFENPRGIVL HPQRGYVYWA DWGDHAYIAR IGMDGTNKTV
IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH RHTVYDGTLP HPFALTIFED
TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT HKPFDIHVLH PYRQPIMSNP CATNNGGCSH
LCLIKAGGRG FTCECPDDFQ TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC
SDGSDESDLC PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCEANE
WQCANKRCIP EYWQCDSVDD CLDNSDEDPS HCASRTCRPG QFKCNNGRCI PQSWKCDVDN
DCGDYSDEPI HECMTAAYNC DNHTEFSCKT NYRCIPQWAV CNGFDDCRDN SDEQGCESVP
CHPSGDFRCG NHHCIPLRWK CDGIDDCGDN SDEESCVPRE CTESEFRCAD QQCIPSRWVC
DQENDCGDNS DERDCEMKTC HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN
GTYCPAAMFE CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNVPCESPQR FRCDNSRCIY
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCVSQHYVCD NVDDCGDLSD
ETGCNLGENR TCAEKICEQN CTQLSNGGFI CSCRPGFKPS TLDKNSCQDI NECEEFGICP
QSCRNSKGSY ECFCVDGFKS MSTHYGERCA ADGSPPLLLL PENVRIRKYN ISSEKFSEYL
EEEEHIQAID YDWDPEGIGL SVVYYTVLSQ GSQFGAIKRA YLPDFESGSN NPVREVDLGL
KYLMQPDGLA VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
MFWTDQGKQP KIESAWMNGE HRSVLASANL GWPNGLSIDY LNGDRIYWSD SKEDVIESIK
YDGTDRRLII NDAMKPFSLD IFEDQLYWVA KEKGEVWRQN KFGKGNKEKL LVVNPWLTQV
RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG YSCACPQGSD FVTGSTVECD AASELPITMP
SPCRCMHGGS CYFDENDLPK CKCSSGYSGE YCEIGLSRGI PPGTTMALLL TFAMVIIVGA
LVLVGFFHYR KTGSLLPSLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
IDRSMAMNEQ FVMEVGKQPV IFENPMYAAK DSTSKVGLAV QGPSVSSQVT VPENVENQNY
GRSIDPSEIV PEPKPASPGA DETQGTKWNI FKRKPKQTTN FENPIYAEMD TEQKEAVAVA
PPPSPSLPAK ASKRSSTPGY TATEDTFKDT ANLVKEDSDV


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C389 Low-Density Lipoprotein Receptor-Related Protein 12 LRP12 500
E02S0268 Rat Soluble low density lipoprotein receptor related protein 1 96T/kit
E03L0279 Mouse low-density lipoprotein-receptor-related protein 6 96 Tests/kit
E03L0278 Mouse low-density lipoprotein receptor-related protein 1 96 Tests/kit
EH1183 Low-density lipoprotein receptor-related protein 11 Elisa Kit 96T


 

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