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

 LRP2_HUMAN              Reviewed;        4655 AA.
P98164; O00711; Q16215;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 3.
22-NOV-2017, entry version 182.
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 {ECO:0000312|HGNC:HGNC:6694};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-83.
TISSUE=Kidney;
PubMed=8706697; DOI=10.1111/j.1432-1033.1996.0132u.x;
Hjaelm G., Murray E., Crumley G., Harazim W., Lundgren S., Onyango I.,
Ek B., Larsson M., Juhlin C., Hellman P., Davis H., Aekerstroem G.,
Rask L., Morse B.;
"Cloning and sequencing of human gp330, a Ca(2+)-binding receptor with
potential intracellular signaling properties.";
Eur. J. Biochem. 239:132-137(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 2705-4453, AND VARIANTS GLU-4094 AND
LEU-4210.
TISSUE=Kidney;
PubMed=7959795; DOI=10.1006/geno.1994.1348;
Korenberg J.R., Argraves K.M., Chen X.N., Tran H., Strickland D.K.,
Argraves W.S.;
"Chromosomal localization of human genes for the LDL receptor family
member glycoprotein 330 (LRP2) and its associated protein RAP
(LRPAP1).";
Genomics 22:88-93(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 4139-4406.
PubMed=8187828; DOI=10.1006/excr.1994.1153;
Lundgren S., Hjaelm G., Hellman P., Ek B., Juhlin C., Rastad J.,
Klareskog L., Aakerstroem G., Rask L.;
"A protein involved in calcium sensing of the human parathyroid and
placental cytotrophoblast cells belongs to the LDL-receptor protein
superfamily.";
Exp. Cell Res. 212:344-350(1994).
[5]
INTERACTION WITH LRPAP1.
PubMed=1400426;
Kounnas M.Z., Argraves W.S., Strickland D.K.;
"The 39-kDa receptor-associated protein interacts with two members of
the low density lipoprotein receptor family, alpha 2-macroglobulin
receptor and glycoprotein 330.";
J. Biol. Chem. 267:21162-21166(1992).
[6]
SUBUNIT, AND INTERACTION WITH CLU.
PubMed=7768901; DOI=10.1074/jbc.270.22.13070;
Kounnas M.Z., Loukinova E.B., Stefansson S., Harmony J.A.K.,
Brewer B.H., Strickland D.K., Argraves W.S.;
"Identification of glycoprotein 330 as an endocytic receptor for
apolipoprotein J/clusterin.";
J. Biol. Chem. 270:13070-13075(1995).
[7]
INTERACTION WITH DAB2.
PubMed=10769163; DOI=10.1042/bj3470613;
Oleinikov A.V., Zhao J., Makker S.P.;
"Cytosolic adaptor protein Dab2 is an intracellular ligand of
endocytic receptor gp600/megalin.";
Biochem. J. 347:613-621(2000).
[8]
INTERACTION WITH LRP2BP.
PubMed=12508107; DOI=10.1242/jcs.00243;
Petersen H.H., Hilpert J., Militz D., Zandler V., Jacobsen C.,
Roebroek A.J.M., Willnow T.E.;
"Functional interaction of megalin with the megalin-binding protein
(MegBP), a novel tetratrico peptide repeat-containing adaptor
molecule.";
J. Cell Sci. 116:453-461(2003).
[9]
FUNCTION.
PubMed=15126248; DOI=10.1152/ajprenal.00233.2003;
Klassen R.B., Crenshaw K., Kozyraki R., Verroust P.J., Tio L.,
Atrian S., Allen P.L., Hammond T.G.;
"Megalin mediates renal uptake of heavy metal metallothionein
complexes.";
Am. J. Physiol. 287:F393-F403(2004).
[10]
INTERACTION WITH DAB2.
PubMed=15134832; DOI=10.1016/j.biochi.2004.03.001;
Gallagher H., Oleinikov A.V., Fenske C., Newman D.J.;
"The adaptor disabled-2 binds to the third psi xNPxY sequence on the
cytoplasmic tail of megalin.";
Biochimie 86:179-182(2004).
[11]
INTERACTION WITH SHBG.
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).
[12]
INTERACTION WITH CST3.
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).
[13]
DEVELOPMENTAL STAGE.
PubMed=17324488; DOI=10.1016/j.neurobiolaging.2007.01.008;
Dietrich M.O., Spuch C., Antequera D., Rodal I., de Yebenes J.G.,
Molina J.A., Bermejo F., Carro E.;
"Megalin mediates the transport of leptin across the blood-CSF
barrier.";
Neurobiol. Aging 29:902-912(2008).
[14]
FUNCTION, INTERACTION WITH BIRC5, AND SUBCELLULAR LOCATION.
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).
[15]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=27798286; DOI=10.1369/0022155416672210;
Storm T., Christensen E.I., Christensen J.N., Kjaergaard T.,
Uldbjerg N., Larsen A., Honore B., Madsen M.;
"Megalin is predominantly observed in vesicular structures in first
and third trimester cytotrophoblasts of the human placenta.";
J. Histochem. Cytochem. 64:769-784(2016).
[16]
STRUCTURE BY NMR OF 1103-1148 IN COMPLEX WITH CALCIUM, AND DISULFIDE
BONDS.
PubMed=23275343; DOI=10.1074/jbc.M112.434159;
Dagil R., O'Shea C., Nykjaer A., Bonvin A.M., Kragelund B.B.;
"Gentamicin binds to the megalin receptor as a competitive inhibitor
using the common ligand binding motif of complement type repeats:
insight from the NMR structure of the 10th complement type repeat
domain alone and in complex with gentamicin.";
J. Biol. Chem. 288:4424-4435(2013).
[17]
VARIANT [LARGE SCALE ANALYSIS] VAL-4272.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[18]
VARIANT DBS HIS-2522.
PubMed=17632512; DOI=10.1038/ng2063;
Kantarci S., Al-Gazali L., Hill R.S., Donnai D., Black G.C.M.,
Bieth E., Chassaing N., Lacombe D., Devriendt K., Teebi A.,
Loscertales M., Robson C., Liu T., MacLaughlin D.T., Noonan K.M.,
Russell M.K., Walsh C.A., Donahoe P.K., Pober B.R.;
"Mutations in LRP2, which encodes the multiligand receptor megalin,
cause Donnai-Barrow and facio-oculo-acoustico-renal syndromes.";
Nat. Genet. 39:957-959(2007).
[19]
VARIANT ARG-103.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
[20]
VARIANT GLY-3828.
PubMed=23992033; DOI=10.1111/cge.12265;
Schrauwen I., Sommen M., Claes C., Pinner J., Flaherty M., Collins F.,
Van Camp G.;
"Broadening the phenotype of LRP2 mutations: a new mutation in LRP2
causes a predominantly ocular phenotype suggestive of Stickler
syndrome.";
Clin. Genet. 86:282-286(2014).
[21]
VARIANT ASN-3779.
PubMed=26529358; DOI=10.1097/YPG.0000000000000114;
Vasli N., Ahmed I., Mittal K., Ohadi M., Mikhailov A., Rafiq M.A.,
Bhatti A., Carter M.T., Andrade D.M., Ayub M., Vincent J.B., John P.;
"Identification of a homozygous missense mutation in LRP2 and a
hemizygous missense mutation in TSPYL2 in a family with mild
intellectual disability.";
Psychiatr. Genet. 26:66-73(2016).
-!- FUNCTION: Multiligand endocytic receptor (By similarity). Acts
together with CUBN to mediate endocytosis of high-density
lipoproteins (By similarity). 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 (By similarity). 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 (By
similarity). Mediates endocytosis and subsequent lysosomal
degradation of CST3 in kidney proximal tubule cells (By
similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in
complex with the vitamin D3 transporter GC/DBP (By similarity).
Mediates renal uptake of metallothionein-bound heavy metals
(PubMed:15126248). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). During neurulation, required
in neuroepithelial cells for uptake of folate bound to the folate
receptor FOLR1 which is necessary for neural tube closure (By
similarity). In the adult brain, negatively regulates BMP
signaling in the subependymal zone which enables neurogenesis to
proceed (By similarity). In astrocytes, mediates endocytosis of
ALB which is required for the synthesis of the neurotrophic factor
oleic acid (By similarity). Involved in neurite branching (By
similarity). During optic nerve development, required for SHH-
mediated migration and proliferation of oligodendrocyte precursor
cells (By similarity). Mediates endocytic uptake and clearance of
SHH in the retinal margin which protects retinal progenitor cells
from mitogenic stimuli and keeps them quiescent (By similarity).
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 (By similarity). Mediates endocytosis
of angiotensin-2 (By similarity). Also mediates endocytosis of
angiotensis 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 (By similarity). Required for normal hearing,
possibly through interaction with estrogen in the inner ear (By
similarity). {ECO:0000250|UniProtKB:A2ARV4,
ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98158,
ECO:0000269|PubMed:15126248, ECO:0000269|PubMed:23825075}.
-!- 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 (PubMed:7768901). Forms a
multimeric complex together with LRPAP1 (PubMed:1400426).
Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats)
(By similarity). Interacts with LRP2BP (PubMed:12508107).
Interacts (via NPXY motif) with DAB2; the interaction is not
affected by tyrosine phosphorylation of the NPXY motif
(PubMed:10769163, PubMed:15134832). Interacts with MB (By
similarity). Interacts with BMP4 (By similarity). Interacts with
the Sonic hedgehog protein N-product which is the active product
of SHH (By similarity). Interacts with CST3 in a calcium-dependent
manner (PubMed:17462596). Interacts with the vitamin-D binding
protein GC/DBP (By similarity). Interacts with sex hormone-binding
protein SHBG (PubMed:16143106). Interacts with angiotensin-2 (By
similarity). Also interacts with angiotensin 1-7 (By similarity).
Interacts with APOM (By similarity). Interacts with selenoprotein
SEPP1 (By similarity). Interacts with LEP (By similarity).
Interacts with ALB (By similarity). Interacts with the
antiapoptotic protein BIRC5/survivin (PubMed:23825075). Interacts
with matrix metalloproteinase MMP2 in complex with
metalloproteinase inhibitor TIMP1 (By similarity). In neurons,
forms a trimeric complex with APP and APPB1/FE65 (By similarity).
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:A2ARV4, ECO:0000250|UniProtKB:C0HL13,
ECO:0000250|UniProtKB:P98158, ECO:0000269|PubMed:10769163,
ECO:0000269|PubMed:12508107, ECO:0000269|PubMed:1400426,
ECO:0000269|PubMed:15134832, ECO:0000269|PubMed:16143106,
ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:23825075,
ECO:0000269|PubMed:7768901}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:23825075, ECO:0000269|PubMed:27798286};
Single-pass type I membrane protein {ECO:0000255}. Endosome lumen
{ECO:0000250|UniProtKB:P98158}. Membrane, coated pit
{ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite
{ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon
{ECO:0000250|UniProtKB:A2ARV4}. 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: Expressed in first and third trimester
cytotrophoblasts in the placenta (at protein level)
(PubMed:27798286). Absorptive epithelia, including renal proximal
tubules. {ECO:0000269|PubMed:27798286}.
-!- DEVELOPMENTAL STAGE: Expression in the choroid plexus of the brain
is markedly reduced in aging subjects when compared with younger
adults. {ECO:0000269|PubMed:17324488}.
-!- 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.
{ECO:0000250|UniProtKB:A2ARV4}.
-!- DISEASE: Donnai-Barrow syndrome (DBS) [MIM:222448]: Rare autosomal
recessive disorder characterized by major malformations including
agenesis of the corpus callosum, congenital diaphragmatic hernia,
facial dysmorphology, ocular anomalies, sensorineural hearing loss
and developmental delay. The FOAR syndrome was first described as
comprising facial anomalies, ocular anomalies, sensorineural
hearing loss, and proteinuria. DBS and FOAR were first described
as distinct disorders but the classic distinguishing features
between the 2 disorders were presence of proteinuria and absence
of diaphragmatic hernia and corpus callosum anomalies in FOAR.
Early reports noted that the 2 disorders shared many phenotypic
features and may be identical. Although there is variability in
the expression of some features (e.g., agenesis of the corpus
callosum and proteinuria), DBS and FOAR are now considered to
represent the same entity. {ECO:0000269|PubMed:17632512}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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EMBL; U33837; AAB41649.1; -; mRNA.
EMBL; AC007556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U04441; AAB02882.1; -; mRNA.
EMBL; S73145; AAB30825.1; -; mRNA.
CCDS; CCDS2232.1; -.
PIR; I38467; I38467.
PIR; I53413; I53413.
RefSeq; NP_004516.2; NM_004525.2.
UniGene; Hs.657729; -.
PDB; 2M0P; NMR; -; A=1103-1148.
PDBsum; 2M0P; -.
ProteinModelPortal; P98164; -.
SMR; P98164; -.
BioGrid; 110216; 82.
IntAct; P98164; 10.
MINT; MINT-2860496; -.
STRING; 9606.ENSP00000263816; -.
DrugBank; DB00798; Gentamicin.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00071; Insulin Pork.
DrugBank; DB00013; Urokinase.
iPTMnet; P98164; -.
PhosphoSitePlus; P98164; -.
BioMuta; LRP2; -.
DMDM; 160332309; -.
EPD; P98164; -.
MaxQB; P98164; -.
PaxDb; P98164; -.
PeptideAtlas; P98164; -.
PRIDE; P98164; -.
Ensembl; ENST00000263816; ENSP00000263816; ENSG00000081479.
GeneID; 4036; -.
KEGG; hsa:4036; -.
UCSC; uc002ues.4; human.
CTD; 4036; -.
DisGeNET; 4036; -.
EuPathDB; HostDB:ENSG00000081479.12; -.
GeneCards; LRP2; -.
GeneReviews; LRP2; -.
H-InvDB; HIX0029894; -.
HGNC; HGNC:6694; LRP2.
HPA; HPA005980; -.
HPA; HPA064792; -.
MalaCards; LRP2; -.
MIM; 222448; phenotype.
MIM; 600073; gene.
neXtProt; NX_P98164; -.
OpenTargets; ENSG00000081479; -.
Orphanet; 2143; Donnai-Barrow syndrome.
PharmGKB; PA30452; -.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XP34; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000230574; -.
HOVERGEN; HBG097941; -.
InParanoid; P98164; -.
KO; K06233; -.
OMA; PNGDCSH; -.
OrthoDB; EOG091G000N; -.
PhylomeDB; P98164; -.
TreeFam; TF315253; -.
Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SignaLink; P98164; -.
ChiTaRS; LRP2; human.
GeneWiki; LRP2; -.
GenomeRNAi; 4036; -.
PRO; PR:P98164; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000081479; -.
CleanEx; HS_LRP2; -.
ExpressionAtlas; P98164; baseline and differential.
Genevisible; P98164; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0042954; F:lipoprotein transporter activity; TAS:Reactome.
GO; GO:0005041; F:low-density lipoprotein receptor activity; TAS:Reactome.
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; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; TAS:ProtInc.
GO; GO:1904447; P:folic acid import across plasma membrane; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0030001; P:metal ion transport; IDA:UniProtKB.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
GO; GO:0140058; P:neuron projection arborization; ISS:UniProtKB.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
GO; GO:0061156; P:pulmonary artery morphogenesis; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0060068; P:vagina development; ISS:UniProtKB.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:UniProtKB.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
GO; GO:0042359; P:vitamin D metabolic process; TAS:Reactome.
CDD; cd00112; LDLa; 34.
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.
InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
Pfam; PF12662; cEGF; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00057; Ldl_recept_a; 34.
Pfam; PF00058; Ldl_recept_b; 14.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 26.
SMART; SM00179; EGF_CA; 10.
SMART; SM00192; LDLa; 36.
SMART; SM00135; LY; 38.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF57424; SSF57424; 36.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 9.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS01209; LDLRA_1; 31.
PROSITE; PS50068; LDLRA_2; 36.
PROSITE; PS51120; LDLRB; 35.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Cell projection; Coated pit;
Complete proteome; Disease mutation; Disulfide bond; EGF-like domain;
Endocytosis; Endosome; Glycoprotein; Hearing; Membrane; Metal-binding;
Neurogenesis; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; SH3-binding; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 4655 Low-density lipoprotein receptor-related
protein 2.
/FTId=PRO_0000017321.
TOPO_DOM 26 4423 Extracellular. {ECO:0000255}.
TRANSMEM 4424 4446 Helical. {ECO:0000255}.
TOPO_DOM 4447 4655 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 265 308 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REPEAT 436 478 LDL-receptor class B 1.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 479 521 LDL-receptor class B 2.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 522 568 LDL-receptor class B 3.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 569 613 LDL-receptor class B 4.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 753 795 LDL-receptor class B 5.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 796 837 LDL-receptor class B 6.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 838 881 LDL-receptor class B 7.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 882 925 LDL-receptor class B 8.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 1025 1061 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1066 1102 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1108 1144 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1148 1184 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1186 1223 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1229 1267 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1270 1306 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1304 1349 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1390 1429 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 1478 1520 LDL-receptor class B 9.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1521 1563 LDL-receptor class B 10.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1566 1609 LDL-receptor class B 11.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1610 1654 LDL-receptor class B 12.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1655 1695 LDL-receptor class B 13.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 1700 1741 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1790 1832 LDL-receptor class B 14.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1833 1882 LDL-receptor class B 15.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1883 1930 LDL-receptor class B 16.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1931 1972 LDL-receptor class B 17.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 1973 2013 LDL-receptor class B 18.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2107 2156 LDL-receptor class B 19.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2157 2201 LDL-receptor class B 20.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2202 2245 LDL-receptor class B 21.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2246 2289 LDL-receptor class B 22.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2431 2477 LDL-receptor class B 23.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2478 2518 LDL-receptor class B 24.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2519 2562 LDL-receptor class B 25.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2563 2604 LDL-receptor class B 26.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 2605 2646 LDL-receptor class B 27.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 2699 2737 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2740 2776 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2779 2818 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2821 2860 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2863 2900 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2905 2944 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2947 2989 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2992 3028 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3031 3069 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3074 3110 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3110 3151 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3152 3192 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3239 3281 LDL-receptor class B 28.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3282 3324 LDL-receptor class B 29.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3333 3376 LDL-receptor class B 30.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3377 3419 LDL-receptor class B 31.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 3420 3460 LDL-receptor class B 32.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 3511 3549 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3552 3590 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3593 3631 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3634 3672 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3677 3715 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3718 3755 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3758 3794 LDL-receptor class A 32.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3797 3833 LDL-receptor class A 33.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3841 3879 LDL-receptor class A 34.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3882 3921 LDL-receptor class A 35.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3927 3963 LDL-receptor class A 36.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 4007 4048 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 4154 4196 LDL-receptor class B 33.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4197 4240 LDL-receptor class B 34.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 4242 4283 LDL-receptor class B 35.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
DOMAIN 4377 4411 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4589 4602 Interaction with DAB2.
{ECO:0000269|PubMed:10769163}.
MOTIF 4453 4462 SH3-binding. {ECO:0000255}.
MOTIF 4456 4461 PxLPxI/L motif 1; mediates interaction
with ANKRA2.
{ECO:0000250|UniProtKB:P98158}.
MOTIF 4459 4464 PxLPxI/L motif 2; mediates interaction
with ANKRA2.
{ECO:0000250|UniProtKB:P98158}.
MOTIF 4521 4526 Endocytosis signal. {ECO:0000255}.
MOTIF 4595 4598 NPXY motif.
MOTIF 4598 4601 SH2-binding. {ECO:0000255}.
MOTIF 4611 4622 SH3-binding. {ECO:0000255}.
METAL 1126 1126 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2M0P,
ECO:0000269|PubMed:23275343}.
METAL 1129 1129 Calcium. {ECO:0000244|PDB:2M0P,
ECO:0000269|PubMed:23275343}.
METAL 1131 1131 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:2M0P,
ECO:0000269|PubMed:23275343}.
METAL 1133 1133 Calcium. {ECO:0000244|PDB:2M0P,
ECO:0000269|PubMed:23275343}.
METAL 1139 1139 Calcium. {ECO:0000244|PDB:2M0P,
ECO:0000269|PubMed:23275343}.
METAL 1140 1140 Calcium. {ECO:0000244|PDB:2M0P,
ECO:0000269|PubMed:23275343}.
METAL 1208 1208 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1210 1210 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P98158}.
METAL 1212 1212 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1218 1218 Calcium. {ECO:0000250|UniProtKB:P98158}.
METAL 1219 1219 Calcium. {ECO:0000250|UniProtKB:P98158}.
MOD_RES 4463 4463 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4466 4466 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4569 4569 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4616 4616 Phosphoserine.
{ECO:0000250|UniProtKB:P98158}.
MOD_RES 4632 4632 Phosphothreonine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4653 4653 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
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 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 866 866 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1064 1064 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1144 1144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1186 1186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1327 1327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1340 1340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1383 1383 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1464 1464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1496 1496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1550 1550 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1675 1675 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1810 1810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2055 2055 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2177 2177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2224 2224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2499 2499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2547 2547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2781 2781 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2809 2809 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2810 2810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2947 2947 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2987 2987 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3125 3125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3211 3211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3257 3257 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3315 3315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3355 3355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3446 3446 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3564 3564 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3680 3680 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3978 3978 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4068 4068 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4327 4327 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 266 279 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 273 292 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 286 307 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1026 1038 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1033 1051 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1045 1060 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1067 1079 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1074 1092 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1086 1101 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1109 1121 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:23275343}.
DISULFID 1116 1134 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:23275343}.
DISULFID 1128 1143 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:23275343}.
DISULFID 1149 1161 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1156 1174 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1168 1183 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1187 1200 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1194 1213 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1207 1222 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1230 1243 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1237 1256 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1250 1266 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1271 1283 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1278 1296 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1290 1305 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1305 1325 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1312 1338 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1332 1348 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1394 1404 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1400 1413 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1415 1428 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1704 1713 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1709 1725 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1727 1740 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2700 2712 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2707 2725 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2719 2736 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2741 2753 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2748 2766 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2760 2775 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2780 2793 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2788 2806 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2800 2817 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2822 2835 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2829 2848 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2842 2859 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2864 2876 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2871 2889 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2883 2899 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2906 2918 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2913 2931 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2925 2943 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2948 2965 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2955 2978 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2972 2988 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 2993 3005 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3000 3018 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3012 3027 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3032 3044 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3039 3057 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3051 3068 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3075 3087 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3082 3100 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3094 3109 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3114 3126 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3122 3135 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3137 3150 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3156 3167 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3163 3176 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3178 3191 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 3512 3525 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3519 3538 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3532 3548 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3553 3565 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3560 3578 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3572 3589 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3594 3606 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3601 3619 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3613 3630 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3635 3647 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3642 3660 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3654 3671 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3678 3692 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3686 3705 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3699 3714 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3719 3732 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3727 3745 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3739 3754 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3759 3771 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3766 3784 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3778 3793 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3798 3810 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3805 3823 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3817 3832 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3842 3854 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3849 3867 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3861 3878 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3883 3896 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3891 3909 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3903 3920 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3928 3940 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3935 3953 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 3947 3962 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 4011 4021 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4017 4030 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4032 4047 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4381 4389 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4383 4399 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 4401 4410 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VARIANT 83 83 N -> S (in dbSNP:rs2229263).
{ECO:0000269|PubMed:8706697}.
/FTId=VAR_037009.
VARIANT 103 103 C -> R (found in a renal cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064727.
VARIANT 259 259 G -> R (in dbSNP:rs34693334).
/FTId=VAR_061294.
VARIANT 669 669 G -> D (in dbSNP:rs34291900).
/FTId=VAR_037010.
VARIANT 909 909 H -> R (in dbSNP:rs36082715).
/FTId=VAR_037011.
VARIANT 1083 1083 H -> Q (in dbSNP:rs2302691).
/FTId=VAR_037012.
VARIANT 1279 1279 D -> A (in dbSNP:rs17848149).
/FTId=VAR_029182.
VARIANT 1287 1287 A -> P.
/FTId=VAR_005421.
VARIANT 2012 2012 R -> K (in dbSNP:rs4667596).
/FTId=VAR_029183.
VARIANT 2065 2065 I -> T (in dbSNP:rs2228168).
/FTId=VAR_020218.
VARIANT 2522 2522 Y -> H (in DBS; dbSNP:rs80338747).
{ECO:0000269|PubMed:17632512}.
/FTId=VAR_037013.
VARIANT 2632 2632 N -> D (in dbSNP:rs17848169).
/FTId=VAR_029184.
VARIANT 2872 2872 A -> T (in dbSNP:rs2228171).
/FTId=VAR_005422.
VARIANT 3011 3011 R -> M (in dbSNP:rs11674973).
/FTId=VAR_037014.
VARIANT 3305 3305 R -> H (in dbSNP:rs3213760).
/FTId=VAR_020219.
VARIANT 3779 3779 D -> N (found in patients with mild
intellectual disability, unknown
pathological significance;
dbSNP:rs199583537).
{ECO:0000269|PubMed:26529358}.
/FTId=VAR_075534.
VARIANT 3828 3828 D -> G (found in patients with a
phenotype suggestive of Stickler
syndrome; unknown pathological
significance).
{ECO:0000269|PubMed:23992033}.
/FTId=VAR_075535.
VARIANT 4094 4094 K -> E (in dbSNP:rs2075252).
{ECO:0000269|PubMed:7959795}.
/FTId=VAR_005423.
VARIANT 4210 4210 I -> L (in dbSNP:rs4667591).
{ECO:0000269|PubMed:7959795}.
/FTId=VAR_005424.
VARIANT 4272 4272 M -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035996.
CONFLICT 2724 2724 D -> G (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2773 2773 A -> T (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2827 2827 T -> P (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2880 2882 HWY -> TFGI (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2897 2897 A -> S (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2908 2908 A -> S (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2921 2921 S -> N (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2954 2954 L -> P (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2971 2972 VC -> PP (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2982 2982 Y -> H (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 2985 2985 N -> I (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 3615 3615 T -> S (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 3738 3738 Q -> K (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 3784 3784 C -> LW (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 3810 3810 C -> R (in Ref. 3; AAB02882).
{ECO:0000305}.
CONFLICT 4220 4220 R -> P (in Ref. 3; AAB02882).
{ECO:0000305}.
STRAND 1111 1115 {ECO:0000244|PDB:2M0P}.
STRAND 1121 1123 {ECO:0000244|PDB:2M0P}.
STRAND 1129 1131 {ECO:0000244|PDB:2M0P}.
STRAND 1133 1136 {ECO:0000244|PDB:2M0P}.
HELIX 1138 1141 {ECO:0000244|PDB:2M0P}.
SEQUENCE 4655 AA; 521958 MW; C73C4206B8B28CE0 CRC64;
MDRGPAAVAC TLLLALVACL APASGQECDS AHFRCGSGHC IPADWRCDGT KDCSDDADEI
GCAVVTCQQG YFKCQSEGQC IPNSWVCDQD QDCDDGSDER QDCSQSTCSS HQITCSNGQC
IPSEYRCDHV RDCPDGADEN DCQYPTCEQL TCDNGACYNT SQKCDWKVDC RDSSDEINCT
EICLHNEFSC GNGECIPRAY VCDHDNDCQD GSDEHACNYP TCGGYQFTCP SGRCIYQNWV
CDGEDDCKDN GDEDGCESGP HDVHKCSPRE WSCPESGRCI SIYKVCDGIL DCPGREDENN
TSTGKYCSMT LCSALNCQYQ CHETPYGGAC FCPPGYIINH NDSRTCVEFD DCQIWGICDQ
KCESRPGRHL CHCEEGYILE RGQYCKANDS FGEASIIFSN GRDLLIGDIH GRSFRILVES
QNRGVAVGVA FHYHLQRVFW TDTVQNKVFS VDINGLNIQE VLNVSVETPE NLAVDWVNNK
IYLVETKVNR IDMVNLDGSY RVTLITENLG HPRGIAVDPT VGYLFFSDWE SLSGEPKLER
AFMDGSNRKD LVKTKLGWPA GVTLDMISKR VYWVDSRFDY IETVTYDGIQ RKTVVHGGSL
IPHPFGVSLF EGQVFFTDWT KMAVLKANKF TETNPQVYYQ ASLRPYGVTV YHSLRQPYAT
NPCKDNNGGC EQVCVLSHRT DNDGLGFRCK CTFGFQLDTD ERHCIAVQNF LIFSSQVAIR
GIPFTLSTQE DVMVPVSGNP SFFVGIDFDA QDSTIFFSDM SKHMIFKQKI DGTGREILAA
NRVENVESLA FDWISKNLYW TDSHYKSISV MRLADKTRRT VVQYLNNPRS VVVHPFAGYL
FFTDWFRPAK IMRAWSDGSH LLPVINTTLG WPNGLAIDWA ASRLYWVDAY FDKIEHSTFD
GLDRRRLGHI EQMTHPFGLA IFGEHLFFTD WRLGAIIRVR KADGGEMTVI RSGIAYILHL
KSYDVNIQTG SNACNQPTHP NGDCSHFCFP VPNFQRVCGC PYGMRLASNH LTCEGDPTNE
PPTEQCGLFS FPCKNGRCVP NYYLCDGVDD CHDNSDEQLC GTLNNTCSSS AFTCGHGECI
PAHWRCDKRN DCVDGSDEHN CPTHAPASCL DTQYTCDNHQ CISKNWVCDT DNDCGDGSDE
KNCNSTETCQ PSQFNCPNHR CIDLSFVCDG DKDCVDGSDE VGCVLNCTAS QFKCASGDKC
IGVTNRCDGV FDCSDNSDEA GCPTRPPGMC HSDEFQCQED GICIPNFWEC DGHPDCLYGS
DEHNACVPKT CPSSYFHCDN GNCIHRAWLC DRDNDCGDMS DEKDCPTQPF RCPSWQWQCL
GHNICVNLSV VCDGIFDCPN GTDESPLCNG NSCSDFNGGC THECVQEPFG AKCLCPLGFL
LANDSKTCED IDECDILGSC SQHCYNMRGS FRCSCDTGYM LESDGRTCKV TASESLLLLV
ASQNKIIADS VTSQVHNIYS LVENGSYIVA VDFDSISGRI FWSDATQGKT WSAFQNGTDR
RVVFDSSIIL TETIAIDWVG RNLYWTDYAL ETIEVSKIDG SHRTVLISKN LTNPRGLALD
PRMNEHLLFW SDWGHHPRIE RASMDGSMRT VIVQDKIFWP CGLTIDYPNR LLYFMDSYLD
YMDFCDYNGH HRRQVIASDL IIRHPYALTL FEDSVYWTDR ATRRVMRANK WHGGNQSVVM
YNIQWPLGIV AVHPSKQPNS VNPCAFSRCS HLCLLSSQGP HFYSCVCPSG WSLSPDLLNC
LRDDQPFLIT VRQHIIFGIS LNPEVKSNDA MVPIAGIQNG LDVEFDDAEQ YIYWVENPGE
IHRVKTDGTN RTVFASISMV GPSMNLALDW ISRNLYSTNP RTQSIEVLTL HGDIRYRKTL
IANDGTALGV GFPIGITVDP ARGKLYWSDQ GTDSGVPAKI ASANMDGTSV KTLFTGNLEH
LECVTLDIEE QKLYWAVTGR GVIERGNVDG TDRMILVHQL SHPWGIAVHD SFLYYTDEQY
EVIERVDKAT GANKIVLRDN VPNLRGLQVY HRRNAAESSN GCSNNMNACQ QICLPVPGGL
FSCACATGFK LNPDNRSCSP YNSFIVVSML SAIRGFSLEL SDHSETMVPV AGQGRNALHV
DVDVSSGFIY WCDFSSSVAS DNAIRRIKPD GSSLMNIVTH GIGENGVRGI AVDWVAGNLY
FTNAFVSETL IEVLRINTTY RRVLLKVTVD MPRHIVVDPK NRYLFWADYG QRPKIERSFL
DCTNRTVLVS EGIVTPRGLA VDRSDGYVYW VDDSLDIIAR IRINGENSEV IRYGSRYPTP
YGITVFENSI IWVDRNLKKI FQASKEPENT EPPTVIRDNI NWLRDVTIFD KQVQPRSPAE
VNNNPCLENN GGCSHLCFAL PGLHTPKCDC AFGTLQSDGK NCAISTENFL IFALSNSLRS
LHLDPENHSP PFQTINVERT VMSLDYDSVS DRIYFTQNLA SGVGQISYAT LSSGIHTPTV
IASGIGTADG IAFDWITRRI YYSDYLNQMI NSMAEDGSNR TVIARVPKPR AIVLDPCQGY
LYWADWDTHA KIERATLGGN FRVPIVNSSL VMPSGLTLDY EEDLLYWVDA SLQRIERSTL
TGVDREVIVN AAVHAFGLTL YGQYIYWTDL YTQRIYRANK YDGSGQIAMT TNLLSQPRGI
NTVVKNQKQQ CNNPCEQFNG GCSHICAPGP NGAECQCPHE GNWYLANNRK HCIVDNGERC
GASSFTCSNG RCISEEWKCD NDNDCGDGSD EMESVCALHT CSPTAFTCAN GRCVQYSYRC
DYYNDCGDGS DEAGCLFRDC NATTEFMCNN RRCIPREFIC NGVDNCHDNN TSDEKNCPDR
TCQSGYTKCH NSNICIPRVY LCDGDNDCGD NSDENPTYCT THTCSSSEFQ CASGRCIPQH
WYCDQETDCF DASDEPASCG HSERTCLADE FKCDGGRCIP SEWICDGDND CGDMSDEDKR
HQCQNQNCSD SEFLCVNDRP PDRRCIPQSW VCDGDVDCTD GYDENQNCTR RTCSENEFTC
GYGLCIPKIF RCDRHNDCGD YSDERGCLYQ TCQQNQFTCQ NGRCISKTFV CDEDNDCGDG
SDELMHLCHT PEPTCPPHEF KCDNGRCIEM MKLCNHLDDC LDNSDEKGCG INECHDPSIS
GCDHNCTDTL TSFYCSCRPG YKLMSDKRTC VDIDECTEMP FVCSQKCENV IGSYICKCAP
GYLREPDGKT CRQNSNIEPY LIFSNRYYLR NLTIDGYFYS LILEGLDNVV ALDFDRVEKR
LYWIDTQRQV IERMFLNKTN KETIINHRLP AAESLAVDWV SRKLYWLDAR LDGLFVSDLN
GGHRRMLAQH CVDANNTFCF DNPRGLALHP QYGYLYWADW GHRAYIGRVG MDGTNKSVII
STKLEWPNGI TIDYTNDLLY WADAHLGYIE YSDLEGHHRH TVYDGALPHP FAITIFEDTI
YWTDWNTRTV EKGNKYDGSN RQTLVNTTHR PFDIHVYHPY RQPIVSNPCG TNNGGCSHLC
LIKPGGKGFT CECPDDFRTL QLSGSTYCMP MCSSTQFLCA NNEKCIPIWW KCDGQKDCSD
GSDELALCPQ RFCRLGQFQC SDGNCTSPQT LCNAHQNCPD GSDEDRLLCE NHHCDSNEWQ
CANKRCIPES WQCDTFNDCE DNSDEDSSHC ASRTCRPGQF RCANGRCIPQ AWKCDVDNDC
GDHSDEPIEE CMSSAHLCDN FTEFSCKTNY RCIPKWAVCN GVDDCRDNSD EQGCEERTCH
PVGDFRCKNH HCIPLRWQCD GQNDCGDNSD EENCAPRECT ESEFRCVNQQ CIPSRWICDH
YNDCGDNSDE RDCEMRTCHP EYFQCTSGHC VHSELKCDGS ADCLDASDEA DCPTRFPDGA
YCQATMFECK NHVCIPPYWK CDGDDDCGDG SDEELHLCLD VPCNSPNRFR CDNNRCIYSH
EVCNGVDDCG DGTDETEEHC RKPTPKPCTE YEYKCGNGHC IPHDNVCDDA DDCGDWSDEL
GCNKGKERTC AENICEQNCT QLNEGGFICS CTAGFETNVF DRTSCLDINE CEQFGTCPQH
CRNTKGSYEC VCADGFTSMS DRPGKRCAAE GSSPLLLLPD NVRIRKYNLS SERFSEYLQD
EEYIQAVDYD WDPKDIGLSV VYYTVRGEGS RFGAIKRAYI PNFESGRNNL VQEVDLKLKY
VMQPDGIAVD WVGRHIYWSD VKNKRIEVAK LDGRYRKWLI STDLDQPAAI AVNPKLGLMF
WTDWGKEPKI ESAWMNGEDR NILVFEDLGW PTGLSIDYLN NDRIYWSDFK EDVIETIKYD
GTDRRVIAKE AMNPYSLDIF EDQLYWISKE KGEVWKQNKF GQGKKEKTLV VNPWLTQVRI
FHQLRYNKSV PNLCKQICSH LCLLRPGGYS CACPQGSSFI EGSTTECDAA IELPINLPPP
CRCMHGGNCY FDETDLPKCK CPSGYTGKYC EMAFSKGISP GTTAVAVLLT ILLIVVIGAL
AIAGFFHYRR TGSLLPALPK LPSLSSLVKP SENGNGVTFR SGADLNMDIG VSGFGPETAI
DRSMAMSEDF VMEMGKQPII FENPMYSARD SAVKVVQPIQ VTVSENVDNK NYGSPINPSE
IVPETNPTSP AADGTQVTKW NLFKRKSKQT TNFENPIYAQ MENEQKESVA ATPPPSPSLP
AKPKPPSRRD PTPTYSATED TFKDTANLVK EDSEV


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