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Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (Apolipoprotein E receptor) (APOER) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]

 LRP1_HUMAN              Reviewed;        4544 AA.
Q07954; Q2PP12; Q86SW0; Q8IVG8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
27-SEP-2017, entry version 196.
RecName: Full=Prolow-density lipoprotein receptor-related protein 1;
Short=LRP-1;
AltName: Full=Alpha-2-macroglobulin receptor {ECO:0000303|PubMed:26142438};
Short=A2MR;
AltName: Full=Apolipoprotein E receptor;
Short=APOER;
AltName: CD_antigen=CD91;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 85 kDa subunit;
Short=LRP-85;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 515 kDa subunit;
Short=LRP-515;
Contains:
RecName: Full=Low-density lipoprotein receptor-related protein 1 intracellular domain;
Short=LRPICD;
Flags: Precursor;
Name=LRP1; Synonyms=A2MR, APR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-2900.
TISSUE=Liver;
PubMed=3266596;
Herz J., Hamann U., Rogne S., Myklebost O., Gausepohl H.,
Stanley K.K.;
"Surface location and high affinity for calcium of a 500-kd liver
membrane protein closely related to the LDL-receptor suggest a
physiological role as lipoprotein receptor.";
EMBO J. 7:4119-4127(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7534747; DOI=10.1006/geno.1994.1584;
Van Leuven F., Stas L., Hilliker C., Lorent K., Umans L., Serneels L.,
Overbergh L., Torrekens S., Moechars D., De Strooper B.,
Van den Berghe H.;
"Structure of the gene (LRP1) coding for the human alpha 2-
macroglobulin receptor lipoprotein receptor-related protein.";
Genomics 24:78-89(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-2900.
PubMed=9782078; DOI=10.1006/geno.1998.5408;
Van Leuven F., Stas L., Thiry E., Nelissen B., Miyake Y.;
"Strategy to sequence the 89 exons of the human LRP1 gene coding for
the lipoprotein receptor related protein: identification of one
expressed mutation among 48 polymorphisms.";
Genomics 52:138-144(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-2900.
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=2597675;
Kutt H., Herz J., Stanley K.K.;
"Structure of the low-density lipoprotein receptor-related protein
(LRP) promoter.";
Biochim. Biophys. Acta 1009:229-236(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
TISSUE=Blood;
Glaeser C.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 150-166; 234-252; 685-695; 902-916; 1096-1109;
1743-1756; 2863-2874; 2949-2960; 3023-3039 AND 3277-3291.
TISSUE=Placenta;
PubMed=1698775;
Strickland D.K., Ashcom J.D., Williams S., Burgess W.H.,
Migliorini M., Argraves W.S.;
"Sequence identity between the alpha 2-macroglobulin receptor and low
density lipoprotein receptor-related protein suggests that this
molecule is a multifunctional receptor.";
J. Biol. Chem. 265:17401-17404(1990).
[10]
PROTEOLYTIC PROCESSING.
PubMed=2112085;
Herz J., Kowal R.C., Goldstein J.L., Brown M.S.;
"Proteolytic processing of the 600 kd low density lipoprotein
receptor-related protein (LRP) occurs in a trans-Golgi compartment.";
EMBO J. 9:1769-1776(1990).
[11]
FUNCTION.
PubMed=1702392; DOI=10.1016/0014-5793(90)80530-V;
Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O.,
Sottrup-Jensen L.;
"Evidence that the newly cloned low-density-lipoprotein receptor
related protein (LRP) is the alpha 2-macroglobulin receptor.";
FEBS Lett. 276:151-155(1990).
[12]
FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
PubMed=1618748;
Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J.,
Strickland D.K., Saelinger C.B.;
"The alpha 2-macroglobulin receptor/low density lipoprotein receptor-
related protein binds and internalizes Pseudomonas exotoxin A.";
J. Biol. Chem. 267:12420-12423(1992).
[13]
INTERACTION WITH GULP1, AND MUTAGENESIS OF ASN-4470 AND ASN-4504.
PubMed=11729193; DOI=10.1074/jbc.M109336200;
Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G.,
Henson P.M., Ravichandran K.S.;
"Interaction of CED-6/GULP, an adapter protein involved in engulfment
of apoptotic cells with CED-1 and CD91/low density lipoprotein
receptor-related protein (LRP).";
J. Biol. Chem. 277:11772-11779(2002).
[14]
PHOSPHORYLATION AT TYR-4507, MUTAGENESIS OF 4470-ASN--TYR-4473 AND
4504-ASN--TYR-4507, AND INTERACTION WITH PDGF.
PubMed=11854294; DOI=10.1074/jbc.M200427200;
Loukinova E., Ranganathan S., Kuznetsov S., Gorlatova N.,
Migliorini M.M., Loukinov D., Ulery P.G., Mikhailenko I.,
Lawrence D.A., Strickland D.K.;
"Platelet-derived growth factor (PDGF)-induced tyrosine
phosphorylation of the low density lipoprotein receptor-related
protein (LRP). Evidence for integrated co-receptor function between
LRP and the PDGF.";
J. Biol. Chem. 277:15499-15506(2002).
[15]
FUNCTION, AND PROTEOLYTIC PROCESSING.
PubMed=11907044; DOI=10.1074/jbc.M201979200;
May P., Reddy Y.K., Herz J.;
"Proteolytic processing of low density lipoprotein receptor-related
protein mediates regulated release of its intracellular domain.";
J. Biol. Chem. 277:18736-18743(2002).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12888553; DOI=10.1074/jbc.M306403200;
Kinoshita A., Shah T., Tangredi M.M., Strickland D.K., Hyman B.T.;
"The intracellular domain of the low density lipoprotein receptor-
related protein modulates transactivation mediated by amyloid
precursor protein and Fe65.";
J. Biol. Chem. 278:41182-41188(2003).
[17]
FUNCTION.
PubMed=12713657; DOI=10.1034/j.1600-0854.2003.00086_4_5.x;
May P., Herz J.;
"LDL receptor-related proteins in neurodevelopment.";
Traffic 4:291-301(2003).
[18]
PHOSPHORYLATION AT THR-4460; SER-4517; SER-4520 AND SER-4523,
MUTAGENESIS OF THR-4460; THR-4472; SER-4517; SER-4520 AND SER-4523,
AND INTERACTION WITH SHC1; GULP1 AND DAB1.
PubMed=15272003; DOI=10.1074/jbc.M407592200;
Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F.,
Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.;
"Serine and threonine phosphorylation of the low density lipoprotein
receptor-related protein by protein kinase Calpha regulates
endocytosis and association with adaptor molecules.";
J. Biol. Chem. 279:40536-40544(2004).
[19]
INTERACTION WITH SNX17.
PubMed=15769472; DOI=10.1016/j.jmb.2005.02.004;
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V.,
Schreckenberger S., Hahn H., Bohnensack R.;
"Functions of sorting nexin 17 domains and recognition motif for P-
selectin trafficking.";
J. Mol. Biol. 347:813-825(2005).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND
ASN-3048.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[21]
IDENTIFICATION IN A COMPLEX WITH CUBN AND PID1, AND INTERACTION WITH
CUBN AND PID1.
PubMed=17124247; DOI=10.1074/mcp.M600289-MCP200;
Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C.,
Scaloni A., Napolitano M., Russo T., Zambrano N.;
"Identification of the ligands of protein interaction domains through
a functional approach.";
Mol. Cell. Proteomics 6:333-345(2007).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-1511;
ASN-1575; ASN-1616; ASN-1645; ASN-1763; ASN-2127; ASN-2815; ASN-3048;
ASN-3089; ASN-3488; ASN-3788; ASN-3953; ASN-4075 AND ASN-4125.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[23]
GLYCOSYLATION AT ASN-729 AND ASN-1511.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4520, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, AND
DISULFIDE BONDS.
PubMed=10318830; DOI=10.1074/jbc.274.20.14130;
Huang W., Dolmer K., Gettins P.G.W.;
"NMR solution structure of complement-like repeat CR8 from the low
density lipoprotein receptor-related protein.";
J. Biol. Chem. 274:14130-14136(1999).
[27]
STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, AND
DISULFIDE BONDS.
PubMed=10652313; DOI=10.1074/jbc.275.5.3264;
Dolmer K., Huang W., Gettins P.G.W.;
"NMR solution structure of complement-like repeat CR3 from the low
density lipoprotein receptor-related protein. Evidence for specific
binding to the receptor binding domain of human alpha(2)-
macroglobulin.";
J. Biol. Chem. 275:3264-3269(2000).
[28]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1012-1054 IN COMPLEX WITH
CALCIUM IONS, AND DISULFIDE BONDS.
PubMed=11735395; DOI=10.1021/bi015688m;
Simonovic M., Dolmer K., Huang W., Strickland D.K., Volz K.,
Gettins P.G.;
"Calcium coordination and pH dependence of the calcium affinity of
ligand-binding repeat CR7 from the LRP. Comparison with related
domains from the LRP and the LDL receptor.";
Biochemistry 40:15127-15134(2001).
[29]
STRUCTURE BY NMR OF 932-1013 IN COMPLEX WITH LRPAP1 AND CALCIUM IONS,
AND DISULFIDE BONDS.
PubMed=16938309; DOI=10.1016/j.jmb.2006.07.013;
Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I.,
Etzerodt M., Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.;
"Binding site structure of one LRP-RAP complex: implications for a
common ligand-receptor binding motif.";
J. Mol. Biol. 362:700-716(2006).
[30]
VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
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).
[31]
VARIANT GLN-3258.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[32]
VARIANT KPA ARG-1245, CHARACTERIZATION OF VARIANT KPA ARG-1245,
FUNCTION, AND INVOLVEMENT IN KPA.
PubMed=26142438; DOI=10.1136/jmedgenet-2014-102931;
Klar J., Schuster J., Khan T.N., Jameel M., Maebert K., Forsberg L.,
Baig S.A., Baig S.M., Dahl N.;
"Whole exome sequencing identifies LRP1 as a pathogenic gene in
autosomal recessive keratosis pilaris atrophicans.";
J. Med. Genet. 52:599-606(2015).
-!- FUNCTION: Endocytic receptor involved in endocytosis and in
phagocytosis of apoptotic cells. Required for early embryonic
development. Involved in cellular lipid homeostasis. Involved in
the plasma clearance of chylomicron remnants and activated LRPAP1
(alpha 2-macroglobulin), as well as the local metabolism of
complexes between plasminogen activators and their endogenous
inhibitors. May modulate cellular events, such as APP metabolism,
kinase-dependent intracellular signaling, neuronal calcium
signaling as well as neurotransmission (PubMed:11907044,
PubMed:12888553, PubMed:12713657). Acts as an alpha-2-
macroglobulin receptor (PubMed:26142438).
{ECO:0000269|PubMed:11907044, ECO:0000269|PubMed:12713657,
ECO:0000269|PubMed:12888553, ECO:0000269|PubMed:26142438}.
-!- FUNCTION: (Microbial infection) Functions as a receptor for
Pseudomonas aeruginosa exotoxin A. {ECO:0000269|PubMed:1618748}.
-!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit
and a non-covalently attached 515-kDa N-terminal subunit.
Intracellular domain interacts with MAFB (By similarity). Found in
a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17,
PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with
SHC1, GULP1 and DAB1. Interacts with LRPAP1. Can weakly interact
(via NPXY motif) with DAB2 (via PID domain); the interaction is
enhanced by tyrosine phosphorylation of the NPXY motif. Interacts
with bacterial exotoxins. {ECO:0000250,
ECO:0000269|PubMed:10318830, ECO:0000269|PubMed:10652313,
ECO:0000269|PubMed:11729193, ECO:0000269|PubMed:11735395,
ECO:0000269|PubMed:11854294, ECO:0000269|PubMed:15272003,
ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:16938309,
ECO:0000269|PubMed:17124247}.
-!- INTERACTION:
O00213:APBB1; NbExp=3; IntAct=EBI-1046087, EBI-81694;
Q15485:FCN2; NbExp=2; IntAct=EBI-1046087, EBI-7468784;
Q63722:Jag1 (xeno); NbExp=4; IntAct=EBI-1046087, EBI-4567800;
P11226:MBL2; NbExp=5; IntAct=EBI-1046087, EBI-5325353;
Q03350:Thbs2 (xeno); NbExp=2; IntAct=EBI-1046087, EBI-4567830;
-!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
protein 1 85 kDa subunit: Cell membrane; Single-pass type I
membrane protein. Membrane, coated pit.
-!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
protein 1 515 kDa subunit: Cell membrane; Peripheral membrane
protein; Extracellular side. Membrane, coated pit.
-!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
protein 1 intracellular domain: Cytoplasm. Nucleus. Note=After
cleavage, the intracellular domain (LRPICD) is detected both in
the cytoplasm and in the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q07954-1; Sequence=Displayed;
Name=2;
IsoId=Q07954-2; Sequence=VSP_056919, VSP_056920;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Most abundant in liver, brain and lung.
-!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and
a 515 kDa large extracellular domain (LRP-515) that remains non-
covalently associated. Gamma-secretase-dependent cleavage of LRP-
85 releases the intracellular domain from the membrane.
{ECO:0000269|PubMed:11907044, ECO:0000269|PubMed:2112085}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Phosphorylated on serine and threonine residues.
-!- PTM: Phosphorylated on tyrosine residues upon stimulation with
PDGF. Tyrosine phosphorylation promotes interaction with SHC1.
-!- DISEASE: Keratosis pilaris atrophicans (KPA) [MIM:604093]: A group
of rare genodermatoses characterized by keratotic follicular
papules, variable degrees of inflammation, and secondary atrophic
scarring. Most cases are associated with an atopic diathesis and
keratosis pilaris on the extensor extremities. KPA is comprised of
three distinct clinical subtypes: keratosis pilaris atrophicans
faciei, atrophoderma vermiculatum, and keratosis follicularis
spinulosa decalvans. Affected individuals may present with
features overlapping the 3 subtypes.
{ECO:0000269|PubMed:26142438}. 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; X13916; CAA32112.1; -; mRNA.
EMBL; AF058427; AAC64265.1; -; Genomic_DNA.
EMBL; DQ314873; ABC40732.1; -; Genomic_DNA.
EMBL; AC023237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC045107; AAH45107.1; -; mRNA.
EMBL; X15424; CAA33464.1; -; Genomic_DNA.
EMBL; Y18524; CAD57169.1; -; Genomic_DNA.
CCDS; CCDS8932.1; -. [Q07954-1]
PIR; S02392; S02392.
RefSeq; NP_002323.2; NM_002332.2. [Q07954-1]
UniGene; Hs.162757; -.
PDB; 1CR8; NMR; -; A=1059-1100.
PDB; 1D2L; NMR; -; A=851-893.
PDB; 1J8E; X-ray; 1.85 A; A=1011-1054.
PDB; 2FYJ; NMR; -; A=932-1013.
PDB; 2FYL; NMR; -; B=932-1013.
PDB; 2KNX; NMR; -; A=2770-2817.
PDB; 2KNY; NMR; -; A=2770-2817.
PDBsum; 1CR8; -.
PDBsum; 1D2L; -.
PDBsum; 1J8E; -.
PDBsum; 2FYJ; -.
PDBsum; 2FYL; -.
PDBsum; 2KNX; -.
PDBsum; 2KNY; -.
ProteinModelPortal; Q07954; -.
SMR; Q07954; -.
BioGrid; 110215; 122.
CORUM; Q07954; -.
DIP; DIP-50613N; -.
ELM; Q07954; -.
IntAct; Q07954; 25.
MINT; MINT-5004471; -.
STRING; 9606.ENSP00000243077; -.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB00031; Tenecteplase.
iPTMnet; Q07954; -.
PhosphoSitePlus; Q07954; -.
BioMuta; LRP1; -.
DMDM; 317373384; -.
EPD; Q07954; -.
MaxQB; Q07954; -.
PaxDb; Q07954; -.
PeptideAtlas; Q07954; -.
PRIDE; Q07954; -.
Ensembl; ENST00000243077; ENSP00000243077; ENSG00000123384. [Q07954-1]
Ensembl; ENST00000338962; ENSP00000341264; ENSG00000123384. [Q07954-2]
GeneID; 4035; -.
KEGG; hsa:4035; -.
UCSC; uc001snd.4; human. [Q07954-1]
CTD; 4035; -.
DisGeNET; 4035; -.
EuPathDB; HostDB:ENSG00000123384.13; -.
GeneCards; LRP1; -.
HGNC; HGNC:6692; LRP1.
HPA; CAB018621; -.
HPA; HPA004182; -.
HPA; HPA022903; -.
MalaCards; LRP1; -.
MIM; 107770; gene.
MIM; 604093; phenotype.
neXtProt; NX_Q07954; -.
OpenTargets; ENSG00000123384; -.
PharmGKB; PA233; -.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XP34; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000230574; -.
HOVERGEN; HBG006292; -.
InParanoid; Q07954; -.
KO; K04550; -.
OMA; SHRYVIL; -.
OrthoDB; EOG091G000N; -.
PhylomeDB; Q07954; -.
TreeFam; TF315253; -.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; Q07954; -.
ChiTaRS; LRP1; human.
EvolutionaryTrace; Q07954; -.
GeneWiki; LRP1; -.
GenomeRNAi; 4035; -.
PRO; PR:Q07954; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123384; -.
CleanEx; HS_LRP1; -.
ExpressionAtlas; Q07954; baseline and differential.
Genevisible; Q07954; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; NAS:ARUK-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0098797; C:plasma membrane protein complex; TAS:ARUK-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0016964; F:alpha-2 macroglobulin receptor activity; IMP:UniProtKB.
GO; GO:0034185; F:apolipoprotein binding; IDA:UniProtKB.
GO; GO:0030226; F:apolipoprotein receptor activity; TAS:ARUK-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0032050; F:clathrin heavy chain binding; IPI:ARUK-UCL.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; TAS:ARUK-UCL.
GO; GO:0070325; F:lipoprotein particle receptor binding; IC:BHF-UCL.
GO; GO:0042954; F:lipoprotein transporter activity; NAS:UniProtKB.
GO; GO:0005041; F:low-density lipoprotein receptor activity; TAS:ARUK-UCL.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IDA:BHF-UCL.
GO; GO:0004872; F:receptor activity; TAS:ARUK-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0097242; P:amyloid-beta clearance; TAS:BHF-UCL.
GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0043277; P:apoptotic cell clearance; ISS:BHF-UCL.
GO; GO:0002265; P:astrocyte activation involved in immune response; ISS:ARUK-UCL.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ARUK-UCL.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
GO; GO:0042953; P:lipoprotein transport; NAS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISS:BHF-UCL.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISS:BHF-UCL.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:BHF-UCL.
GO; GO:0006909; P:phagocytosis; NAS:ARUK-UCL.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IMP:ARUK-UCL.
GO; GO:0010942; P:positive regulation of cell death; IGI:ARUK-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:BHF-UCL.
GO; GO:0045807; P:positive regulation of endocytosis; IGI:ARUK-UCL.
GO; GO:0032370; P:positive regulation of lipid transport; ISS:BHF-UCL.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IMP:ARUK-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IGI:ARUK-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:ARUK-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IGI:ARUK-UCL.
GO; GO:0051222; P:positive regulation of protein transport; IEA:Ensembl.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; TAS:ARUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:BHF-UCL.
GO; GO:0032374; P:regulation of cholesterol transport; ISS:BHF-UCL.
GO; GO:0010715; P:regulation of extracellular matrix disassembly; TAS:ParkinsonsUK-UCL.
GO; GO:0032429; P:regulation of phospholipase A2 activity; ISS:BHF-UCL.
GO; GO:0051246; P:regulation of protein metabolic process; ISS:ARUK-UCL.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0045056; P:transcytosis; IMP:ARUK-UCL.
Gene3D; 2.120.10.30; -; 8.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR032485; DUF5050.
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_.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF12662; cEGF; 1.
Pfam; PF16472; DUF5050; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00057; Ldl_recept_a; 29.
Pfam; PF00058; Ldl_recept_b; 12.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 26.
SMART; SM00179; EGF_CA; 7.
SMART; SM00192; LDLa; 31.
SMART; SM00135; LY; 35.
SUPFAM; SSF57184; SSF57184; 9.
SUPFAM; SSF57424; SSF57424; 30.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS00022; EGF_1; 5.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS01209; LDLRA_1; 27.
PROSITE; PS50068; LDLRA_2; 31.
PROSITE; PS51120; LDLRB; 34.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Calcium;
Cell membrane; Coated pit; Complete proteome; Cytoplasm;
Developmental protein; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 4544 Prolow-density lipoprotein receptor-
related protein 1.
/FTId=PRO_0000017317.
CHAIN 20 ?3943 Low-density lipoprotein receptor-related
protein 1 515 kDa subunit.
/FTId=PRO_0000302750.
CHAIN ?3944 4544 Low-density lipoprotein receptor-related
protein 1 85 kDa subunit.
/FTId=PRO_0000302751.
CHAIN ?4441 4544 Low-density lipoprotein receptor-related
protein 1 intracellular domain.
/FTId=PRO_0000302752.
TOPO_DOM 20 4419 Extracellular. {ECO:0000255}.
TRANSMEM 4420 4444 Helical. {ECO:0000255}.
TOPO_DOM 4445 4544 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 66 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 70 110 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 111 149 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 150 189 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 292 334 LDL-receptor class B 1.
REPEAT 335 378 LDL-receptor class B 2.
REPEAT 379 422 LDL-receptor class B 3.
DOMAIN 474 520 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 571 613 LDL-receptor class B 4.
REPEAT 614 659 LDL-receptor class B 5.
REPEAT 660 710 LDL-receptor class B 6.
REPEAT 711 754 LDL-receptor class B 7.
DOMAIN 803 843 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 852 892 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 893 933 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 934 973 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 974 1013 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1013 1053 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1060 1099 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1102 1142 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1143 1182 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1183 1222 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1223 1262 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1309 1355 LDL-receptor class B 8.
REPEAT 1356 1398 LDL-receptor class B 9.
REPEAT 1399 1445 LDL-receptor class B 10.
REPEAT 1446 1490 LDL-receptor class B 11.
REPEAT 1491 1531 LDL-receptor class B 12.
DOMAIN 1536 1579 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1627 1669 LDL-receptor class B 13.
REPEAT 1670 1713 LDL-receptor class B 14.
REPEAT 1714 1753 LDL-receptor class B 15.
REPEAT 1754 1798 LDL-receptor class B 16.
DOMAIN 1846 1887 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1934 1976 LDL-receptor class B 17.
REPEAT 1977 2019 LDL-receptor class B 18.
REPEAT 2020 2063 LDL-receptor class B 19.
REPEAT 2064 2107 LDL-receptor class B 20.
DOMAIN 2155 2195 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2253 2294 LDL-receptor class B 21.
REPEAT 2295 2343 LDL-receptor class B 22.
REPEAT 2344 2388 LDL-receptor class B 23.
REPEAT 2389 2431 LDL-receptor class B 24.
REPEAT 2432 2473 LDL-receptor class B 25.
DOMAIN 2478 2518 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2522 2563 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2564 2602 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2603 2641 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2642 2690 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2694 2732 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2732 2771 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2772 2814 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2816 2855 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2856 2899 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2902 2940 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2941 2981 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2982 3022 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3069 3113 LDL-receptor class B 26.
REPEAT 3114 3156 LDL-receptor class B 27.
REPEAT 3157 3200 LDL-receptor class B 28.
REPEAT 3201 3243 LDL-receptor class B 29.
REPEAT 3244 3284 LDL-receptor class B 30.
DOMAIN 3290 3331 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3332 3371 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3372 3410 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3411 3450 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3451 3491 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3492 3533 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3534 3572 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3573 3611 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3611 3649 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3652 3692 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3693 3733 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3739 3778 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3781 3823 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3824 3861 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 3912 3954 LDL-receptor class B 31.
REPEAT 3970 4012 LDL-receptor class B 32.
REPEAT 4013 4056 LDL-receptor class B 33.
REPEAT 4057 4101 LDL-receptor class B 34.
DOMAIN 4147 4183 EGF-like 16. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4196 4232 EGF-like 17. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4232 4268 EGF-like 18. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4268 4304 EGF-like 19. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4304 4340 EGF-like 20. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4340 4375 EGF-like 21. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4373 4409 EGF-like 22. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4445 4544 Interaction with MAFB. {ECO:0000250}.
MOTIF 3940 3943 Recognition site for proteolytical
processing. {ECO:0000255}.
MOTIF 4502 4507 NPXY motif.
METAL 871 871 Calcium 1; via carbonyl oxygen.
METAL 874 874 Calcium 1.
METAL 876 876 Calcium 1; via carbonyl oxygen.
METAL 878 878 Calcium 1.
METAL 884 884 Calcium 1.
METAL 885 885 Calcium 1.
METAL 1032 1032 Calcium 2; via carbonyl oxygen.
METAL 1035 1035 Calcium 2.
METAL 1037 1037 Calcium 2; via carbonyl oxygen.
METAL 1039 1039 Calcium 2.
METAL 1045 1045 Calcium 2.
METAL 1046 1046 Calcium 2.
METAL 1080 1080 Calcium 3; via carbonyl oxygen.
METAL 1083 1083 Calcium 3.
METAL 1085 1085 Calcium 3; via carbonyl oxygen.
METAL 1087 1087 Calcium 3.
METAL 1093 1093 Calcium 3.
METAL 1094 1094 Calcium 3.
MOD_RES 2009 2009 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91ZX7}.
MOD_RES 4460 4460 Phosphothreonine.
{ECO:0000305|PubMed:15272003}.
MOD_RES 4507 4507 Phosphotyrosine.
{ECO:0000269|PubMed:11854294}.
MOD_RES 4517 4517 Phosphoserine.
{ECO:0000305|PubMed:15272003}.
MOD_RES 4520 4520 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 4523 4523 Phosphoserine.
{ECO:0000305|PubMed:15272003}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 729 729 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 928 928 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1050 1050 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1154 1154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1155 1155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1195 1195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1218 1218 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1511 1511 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 1558 1558 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1575 1575 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1616 1616 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1645 1645 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1723 1723 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1733 1733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1763 1763 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1825 1825 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1933 1933 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1995 1995 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2048 2048 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2117 2117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2127 2127 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 2472 2472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2502 2502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2521 2521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2539 2539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2601 2601 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2620 2620 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2638 2638 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2815 2815 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 2905 2905 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3048 3048 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 3089 3089 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3264 3264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3333 3333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3488 3488 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3662 3662 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3788 3788 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3839 3839 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3953 3953 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 4075 4075 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 4125 4125 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 4179 4179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4278 4278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4279 4279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4364 4364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 40 {ECO:0000250}.
DISULFID 34 53 {ECO:0000250}.
DISULFID 47 64 {ECO:0000250}.
DISULFID 72 85 {ECO:0000250}.
DISULFID 79 98 {ECO:0000250}.
DISULFID 92 108 {ECO:0000250}.
DISULFID 115 124 {ECO:0000250}.
DISULFID 120 133 {ECO:0000250}.
DISULFID 135 148 {ECO:0000250}.
DISULFID 154 164 {ECO:0000250}.
DISULFID 160 173 {ECO:0000250}.
DISULFID 175 188 {ECO:0000250}.
DISULFID 478 493 {ECO:0000250}.
DISULFID 489 504 {ECO:0000250}.
DISULFID 506 519 {ECO:0000250}.
DISULFID 807 818 {ECO:0000250}.
DISULFID 814 827 {ECO:0000250}.
DISULFID 829 842 {ECO:0000250}.
DISULFID 854 866
DISULFID 861 879
DISULFID 873 890
DISULFID 895 907 {ECO:0000250}.
DISULFID 902 920 {ECO:0000250}.
DISULFID 914 931 {ECO:0000250}.
DISULFID 936 948
DISULFID 943 961
DISULFID 955 971
DISULFID 976 989
DISULFID 984 1002
DISULFID 996 1011
DISULFID 1015 1027
DISULFID 1022 1040
DISULFID 1034 1051
DISULFID 1062 1075
DISULFID 1069 1088
DISULFID 1082 1097
DISULFID 1104 1118 {ECO:0000250}.
DISULFID 1112 1131 {ECO:0000250}.
DISULFID 1125 1140 {ECO:0000250}.
DISULFID 1145 1159 {ECO:0000250}.
DISULFID 1152 1172 {ECO:0000250}.
DISULFID 1166 1182 {ECO:0000250}.
DISULFID 1185 1196 {ECO:0000250}.
DISULFID 1192 1206 {ECO:0000250}.
DISULFID 1208 1221 {ECO:0000250}.
DISULFID 1227 1237 {ECO:0000250}.
DISULFID 1233 1246 {ECO:0000250}.
DISULFID 1248 1261 {ECO:0000250}.
DISULFID 1540 1553 {ECO:0000250}.
DISULFID 1549 1563 {ECO:0000250}.
DISULFID 1565 1578 {ECO:0000250}.
DISULFID 1850 1861 {ECO:0000250}.
DISULFID 1857 1871 {ECO:0000250}.
DISULFID 1873 1886 {ECO:0000250}.
DISULFID 2159 2170 {ECO:0000250}.
DISULFID 2166 2180 {ECO:0000250}.
DISULFID 2182 2194 {ECO:0000250}.
DISULFID 2482 2493 {ECO:0000250}.
DISULFID 2489 2503 {ECO:0000250}.
DISULFID 2505 2517 {ECO:0000250}.
DISULFID 2524 2537 {ECO:0000250}.
DISULFID 2532 2550 {ECO:0000250}.
DISULFID 2544 2561 {ECO:0000250}.
DISULFID 2566 2578 {ECO:0000250}.
DISULFID 2573 2591 {ECO:0000250}.
DISULFID 2585 2600 {ECO:0000250}.
DISULFID 2605 2617 {ECO:0000250}.
DISULFID 2612 2630 {ECO:0000250}.
DISULFID 2624 2639 {ECO:0000250}.
DISULFID 2644 2666 {ECO:0000250}.
DISULFID 2660 2679 {ECO:0000250}.
DISULFID 2673 2688 {ECO:0000250}.
DISULFID 2696 2708 {ECO:0000250}.
DISULFID 2703 2721 {ECO:0000250}.
DISULFID 2715 2730 {ECO:0000250}.
DISULFID 2734 2746 {ECO:0000250}.
DISULFID 2741 2759 {ECO:0000250}.
DISULFID 2753 2769 {ECO:0000250}.
DISULFID 2774 2787 {ECO:0000250}.
DISULFID 2781 2800 {ECO:0000250}.
DISULFID 2794 2812 {ECO:0000250}.
DISULFID 2818 2830 {ECO:0000250}.
DISULFID 2825 2843 {ECO:0000250}.
DISULFID 2837 2853 {ECO:0000250}.
DISULFID 2858 2870 {ECO:0000250}.
DISULFID 2865 2884 {ECO:0000250}.
DISULFID 2878 2897 {ECO:0000250}.
DISULFID 2904 2917 {ECO:0000250}.
DISULFID 2912 2930 {ECO:0000250}.
DISULFID 2924 2939 {ECO:0000250}.
DISULFID 2944 2956 {ECO:0000250}.
DISULFID 2952 2965 {ECO:0000250}.
DISULFID 2967 2980 {ECO:0000250}.
DISULFID 2986 2996 {ECO:0000250}.
DISULFID 2992 3005 {ECO:0000250}.
DISULFID 3007 3021 {ECO:0000250}.
DISULFID 3294 3305 {ECO:0000250}.
DISULFID 3301 3315 {ECO:0000250}.
DISULFID 3317 3330 {ECO:0000250}.
DISULFID 3334 3346 {ECO:0000250}.
DISULFID 3341 3359 {ECO:0000250}.
DISULFID 3353 3369 {ECO:0000250}.
DISULFID 3374 3386 {ECO:0000250}.
DISULFID 3381 3399 {ECO:0000250}.
DISULFID 3393 3408 {ECO:0000250}.
DISULFID 3413 3426 {ECO:0000250}.
DISULFID 3420 3439 {ECO:0000250}.
DISULFID 3433 3448 {ECO:0000250}.
DISULFID 3453 3466 {ECO:0000250}.
DISULFID 3460 3479 {ECO:0000250}.
DISULFID 3473 3489 {ECO:0000250}.
DISULFID 3494 3507 {ECO:0000250}.
DISULFID 3501 3520 {ECO:0000250}.
DISULFID 3514 3531 {ECO:0000250}.
DISULFID 3536 3548 {ECO:0000250}.
DISULFID 3543 3561 {ECO:0000250}.
DISULFID 3555 3570 {ECO:0000250}.
DISULFID 3575 3587 {ECO:0000250}.
DISULFID 3582 3600 {ECO:0000250}.
DISULFID 3594 3609 {ECO:0000250}.
DISULFID 3613 3625 {ECO:0000250}.
DISULFID 3620 3638 {ECO:0000250}.
DISULFID 3632 3647 {ECO:0000250}.
DISULFID 3654 3666 {ECO:0000250}.
DISULFID 3661 3679 {ECO:0000250}.
DISULFID 3673 3690 {ECO:0000250}.
DISULFID 3695 3709 {ECO:0000250}.
DISULFID 3703 3722 {ECO:0000250}.
DISULFID 3716 3731 {ECO:0000250}.
DISULFID 3741 3754 {ECO:0000250}.
DISULFID 3749 3767 {ECO:0000250}.
DISULFID 3761 3776 {ECO:0000250}.
DISULFID 3785 3798 {ECO:0000250}.
DISULFID 3792 3807 {ECO:0000250}.
DISULFID 3809 3822 {ECO:0000250}.
DISULFID 3828 3838 {ECO:0000250}.
DISULFID 3834 3847 {ECO:0000250}.
DISULFID 3849 3860 {ECO:0000250}.
DISULFID 4151 4160 {ECO:0000250}.
DISULFID 4156 4169 {ECO:0000250}.
DISULFID 4171 4182 {ECO:0000250}.
DISULFID 4200 4210 {ECO:0000250}.
DISULFID 4204 4220 {ECO:0000250}.
DISULFID 4222 4231 {ECO:0000250}.
DISULFID 4236 4246 {ECO:0000250}.
DISULFID 4240 4256 {ECO:0000250}.
DISULFID 4258 4267 {ECO:0000250}.
DISULFID 4272 4282 {ECO:0000250}.
DISULFID 4276 4292 {ECO:0000250}.
DISULFID 4294 4303 {ECO:0000250}.
DISULFID 4308 4318 {ECO:0000250}.
DISULFID 4312 4328 {ECO:0000250}.
DISULFID 4330 4339 {ECO:0000250}.
DISULFID 4344 4352 {ECO:0000250}.
DISULFID 4347 4363 {ECO:0000250}.
DISULFID 4365 4374 {ECO:0000250}.
DISULFID 4377 4387 {ECO:0000250}.
DISULFID 4381 4397 {ECO:0000250}.
DISULFID 4399 4408 {ECO:0000250}.
VAR_SEQ 281 292 HVEQMAIDWLTG -> LCVFSKSQQEMG (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_056919.
VAR_SEQ 293 4544 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056920.
VARIANT 166 166 N -> D (in dbSNP:rs2306691).
/FTId=VAR_021885.
VARIANT 217 217 A -> V (in dbSNP:rs1800127).
/FTId=VAR_014725.
VARIANT 869 869 E -> K (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035994.
VARIANT 1245 1245 K -> R (in KPA; reduced alpha-2
macroglobulin receptor activity; reduced
protein abundance; dbSNP:rs483353013).
{ECO:0000269|PubMed:26142438}.
/FTId=VAR_077982.
VARIANT 2059 2059 V -> L (in dbSNP:rs2229278).
/FTId=VAR_029181.
VARIANT 2080 2080 D -> N (in dbSNP:rs34577247).
/FTId=VAR_047525.
VARIANT 2900 2900 Q -> P (in dbSNP:rs7397167).
{ECO:0000269|PubMed:3266596,
ECO:0000269|PubMed:9782078,
ECO:0000269|Ref.4}.
/FTId=VAR_047526.
VARIANT 3258 3258 H -> Q (found in a patient with severe
mental retardation, seizures, stereotypic
behavior, high pain threshold and sleep
disturbances).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069388.
VARIANT 3760 3760 R -> H (in a colorectal cancer sample;
somatic mutation; dbSNP:rs569866427).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035995.
VARIANT 4536 4536 E -> G (in dbSNP:rs17357542).
/FTId=VAR_047527.
MUTAGEN 4460 4460 T->A: Strongly reduced phosphorylation
and loss of interaction with SHC1; when
associated with A-4517; A-4520 and A-
4523. {ECO:0000269|PubMed:15272003}.
MUTAGEN 4470 4473 NPTY->APTA: No effect on tyrosine
phosphorylation.
{ECO:0000269|PubMed:11854294}.
MUTAGEN 4470 4470 N->A: No effect on interaction with
GULP1. {ECO:0000269|PubMed:11729193}.
MUTAGEN 4472 4472 T->A: No detectable effect on
phosphorylation.
{ECO:0000269|PubMed:15272003}.
MUTAGEN 4504 4507 NPVY->APVA: Loss of tyrosine
phosphorylation. Abolishes interaction
with SHC1 and GULP1.
{ECO:0000269|PubMed:11854294}.
MUTAGEN 4504 4504 N->A: Loss of interaction with GULP1.
{ECO:0000269|PubMed:11729193}.
MUTAGEN 4517 4517 S->A: Strongly reduced phosphorylation
and loss of interaction with SHC1; when
associated with A-4460; A-4520 and A-
4523. {ECO:0000269|PubMed:15272003}.
MUTAGEN 4520 4520 S->A: Strongly reduced phosphorylation
and loss of interaction with SHC1; when
associated with A-4460; A-4517 and A-
4523. {ECO:0000269|PubMed:15272003}.
MUTAGEN 4523 4523 S->A: Strongly reduced phosphorylation
and loss of interaction with SHC1; when
associated with A-4460; A-4517 and A-
4520. {ECO:0000269|PubMed:15272003}.
CONFLICT 685 685 D -> G (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 1743 1743 G -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 2871 2872 LS -> IA (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 3036 3036 R -> M (in Ref. 9; AA sequence).
{ECO:0000305}.
TURN 853 857 {ECO:0000244|PDB:1D2L}.
STRAND 859 861 {ECO:0000244|PDB:1D2L}.
TURN 862 864 {ECO:0000244|PDB:1D2L}.
STRAND 865 867 {ECO:0000244|PDB:1D2L}.
HELIX 869 871 {ECO:0000244|PDB:1D2L}.
STRAND 874 876 {ECO:0000244|PDB:1D2L}.
TURN 878 881 {ECO:0000244|PDB:1D2L}.
STRAND 934 936 {ECO:0000244|PDB:2FYJ}.
STRAND 940 942 {ECO:0000244|PDB:2FYJ}.
TURN 944 946 {ECO:0000244|PDB:2FYL}.
STRAND 948 950 {ECO:0000244|PDB:2FYJ}.
STRAND 953 956 {ECO:0000244|PDB:2FYJ}.
STRAND 958 961 {ECO:0000244|PDB:2FYJ}.
TURN 964 968 {ECO:0000244|PDB:2FYJ}.
TURN 969 971 {ECO:0000244|PDB:2FYL}.
STRAND 974 976 {ECO:0000244|PDB:2FYJ}.
STRAND 978 983 {ECO:0000244|PDB:2FYJ}.
TURN 985 987 {ECO:0000244|PDB:2FYL}.
STRAND 989 991 {ECO:0000244|PDB:2FYJ}.
STRAND 995 1000 {ECO:0000244|PDB:2FYJ}.
STRAND 1003 1007 {ECO:0000244|PDB:2FYJ}.
STRAND 1009 1011 {ECO:0000244|PDB:2FYL}.
STRAND 1013 1015 {ECO:0000244|PDB:1J8E}.
STRAND 1019 1021 {ECO:0000244|PDB:1J8E}.
STRAND 1027 1029 {ECO:0000244|PDB:1J8E}.
HELIX 1030 1032 {ECO:0000244|PDB:1J8E}.
STRAND 1035 1037 {ECO:0000244|PDB:1J8E}.
STRAND 1040 1043 {ECO:0000244|PDB:1J8E}.
HELIX 1044 1046 {ECO:0000244|PDB:1J8E}.
HELIX 1048 1051 {ECO:0000244|PDB:1J8E}.
TURN 1070 1072 {ECO:0000244|PDB:1CR8}.
HELIX 1078 1080 {ECO:0000244|PDB:1CR8}.
STRAND 1081 1085 {ECO:0000244|PDB:1CR8}.
STRAND 1088 1091 {ECO:0000244|PDB:1CR8}.
TURN 1092 1096 {ECO:0000244|PDB:1CR8}.
STRAND 2778 2781 {ECO:0000244|PDB:2KNX}.
TURN 2782 2785 {ECO:0000244|PDB:2KNX}.
STRAND 2786 2789 {ECO:0000244|PDB:2KNX}.
TURN 2790 2794 {ECO:0000244|PDB:2KNX}.
STRAND 2795 2797 {ECO:0000244|PDB:2KNX}.
STRAND 2800 2803 {ECO:0000244|PDB:2KNY}.
HELIX 2804 2806 {ECO:0000244|PDB:2KNX}.
HELIX 2808 2810 {ECO:0000244|PDB:2KNX}.
STRAND 2813 2816 {ECO:0000244|PDB:2KNY}.
SEQUENCE 4544 AA; 504606 MW; 5A11CC02FAB127BE CRC64;
MLTPPLLLLL PLLSALVAAA IDAPKTCSPK QFACRDQITC ISKGWRCDGE RDCPDGSDEA
PEICPQSKAQ RCQPNEHNCL GTELCVPMSR LCNGVQDCMD GSDEGPHCRE LQGNCSRLGC
QHHCVPTLDG PTCYCNSSFQ LQADGKTCKD FDECSVYGTC SQLCTNTDGS FICGCVEGYL
LQPDNRSCKA KNEPVDRPPV LLIANSQNIL ATYLSGAQVS TITPTSTRQT TAMDFSYANE
TVCWVHVGDS AAQTQLKCAR MPGLKGFVDE HTINISLSLH HVEQMAIDWL TGNFYFVDDI
DDRIFVCNRN GDTCVTLLDL ELYNPKGIAL DPAMGKVFFT DYGQIPKVER CDMDGQNRTK
LVDSKIVFPH GITLDLVSRL VYWADAYLDY IEVVDYEGKG RQTIIQGILI EHLYGLTVFE
NYLYATNSDN ANAQQKTSVI RVNRFNSTEY QVVTRVDKGG ALHIYHQRRQ PRVRSHACEN
DQYGKPGGCS DICLLANSHK ARTCRCRSGF SLGSDGKSCK KPEHELFLVY GKGRPGIIRG
MDMGAKVPDE HMIPIENLMN PRALDFHAET GFIYFADTTS YLIGRQKIDG TERETILKDG
IHNVEGVAVD WMGDNLYWTD DGPKKTISVA RLEKAAQTRK TLIEGKMTHP RAIVVDPLNG
WMYWTDWEED PKDSRRGRLE RAWMDGSHRD IFVTSKTVLW PNGLSLDIPA GRLYWVDAFY
DRIETILLNG TDRKIVYEGP ELNHAFGLCH HGNYLFWTEY RSGSVYRLER GVGGAPPTVT
LLRSERPPIF EIRMYDAQQQ QVGTNKCRVN NGGCSSLCLA TPGSRQCACA EDQVLDADGV
TCLANPSYVP PPQCQPGEFA CANSRCIQER WKCDGDNDCL DNSDEAPALC HQHTCPSDRF
KCENNRCIPN RWLCDGDNDC GNSEDESNAT CSARTCPPNQ FSCASGRCIP ISWTCDLDDD
CGDRSDESAS CAYPTCFPLT QFTCNNGRCI NINWRCDNDN DCGDNSDEAG CSHSCSSTQF
KCNSGRCIPE HWTCDGDNDC GDYSDETHAN CTNQATRPPG GCHTDEFQCR LDGLCIPLRW
RCDGDTDCMD SSDEKSCEGV THVCDPSVKF GCKDSARCIS KAWVCDGDND CEDNSDEENC
ESLACRPPSH PCANNTSVCL PPDKLCDGND DCGDGSDEGE LCDQCSLNNG GCSHNCSVAP
GEGIVCSCPL GMELGPDNHT CQIQSYCAKH LKCSQKCDQN KFSVKCSCYE GWVLEPDGES
CRSLDPFKPF IIFSNRHEIR RIDLHKGDYS VLVPGLRNTI ALDFHLSQSA LYWTDVVEDK
IYRGKLLDNG ALTSFEVVIQ YGLATPEGLA VDWIAGNIYW VESNLDQIEV AKLDGTLRTT
LLAGDIEHPR AIALDPRDGI LFWTDWDASL PRIEAASMSG AGRRTVHRET GSGGWPNGLT
VDYLEKRILW IDARSDAIYS ARYDGSGHME VLRGHEFLSH PFAVTLYGGE VYWTDWRTNT
LAKANKWTGH NVTVVQRTNT QPFDLQVYHP SRQPMAPNPC EANGGQGPCS HLCLINYNRT
VSCACPHLMK LHKDNTTCYE FKKFLLYARQ MEIRGVDLDA PYYNYIISFT VPDIDNVTVL
DYDAREQRVY WSDVRTQAIK RAFINGTGVE TVVSADLPNA HGLAVDWVSR NLFWTSYDTN
KKQINVARLD GSFKNAVVQG LEQPHGLVVH PLRGKLYWTD GDNISMANMD GSNRTLLFSG
QKGPVGLAID FPESKLYWIS SGNHTINRCN LDGSGLEVID AMRSQLGKAT ALAIMGDKLW
WADQVSEKMG TCSKADGSGS VVLRNSTTLV MHMKVYDESI QLDHKGTNPC SVNNGDCSQL
CLPTSETTRS CMCTAGYSLR SGQQACEGVG SFLLYSVHEG IRGIPLDPND KSDALVPVSG
TSLAVGIDFH AENDTIYWVD MGLSTISRAK RDQTWREDVV TNGIGRVEGI AVDWIAGNIY
WTDQGFDVIE VARLNGSFRY VVISQGLDKP RAITVHPEKG YLFWTEWGQY PRIERSRLDG
TERVVLVNVS ISWPNGISVD YQDGKLYWCD ARTDKIERID LETGENREVV LSSNNMDMFS
VSVFEDFIYW SDRTHANGSI KRGSKDNATD SVPLRTGIGV QLKDIKVFNR DRQKGTNVCA
VANGGCQQLC LYRGRGQRAC ACAHGMLAED GASCREYAGY LLYSERTILK SIHLSDERNL
NAPVQPFEDP EHMKNVIALA FDYRAGTSPG TPNRIFFSDI HFGNIQQIND DGSRRITIVE
NVGSVEGLAY HRGWDTLYWT SYTTSTITRH TVDQTRPGAF ERETVITMSG DDHPRAFVLD
ECQNLMFWTN WNEQHPSIMR AALSGANVLT LIEKDIRTPN GLAIDHRAEK LYFSDATLDK
IERCEYDGSH RYVILKSEPV HPFGLAVYGE HIFWTDWVRR AVQRANKHVG SNMKLLRVDI
PQQPMGIIAV ANDTNSCELS PCRINNGGCQ DLCLLTHQGH VNCSCRGGRI LQDDLTCRAV
NSSCRAQDEF ECANGECINF SLTCDGVPHC KDKSDEKPSY CNSRRCKKTF RQCSNGRCVS
NMLWCNGADD CGDGSDEIPC NKTACGVGEF RCRDGTCIGN SSRCNQFVDC EDASDEMNCS
ATDCSSYFRL GVKGVLFQPC ERTSLCYAPS WVCDGANDCG DYSDERDCPG VKRPRCPLNY
FACPSGRCIP MSWTCDKEDD CEHGEDETHC NKFCSEAQFE CQNHRCISKQ WLCDGSDDCG
DGSDEAAHCE GKTCGPSSFS CPGTHVCVPE RWLCDGDKDC ADGADESIAA GCLYNSTCDD
REFMCQNRQC IPKHFVCDHD RDCADGSDES PECEYPTCGP SEFRCANGRC LSSRQWECDG
ENDCHDQSDE APKNPHCTSQ EHKCNASSQF LCSSGRCVAE ALLCNGQDDC GDSSDERGCH
INECLSRKLS GCSQDCEDLK IGFKCRCRPG FRLKDDGRTC ADVDECSTTF PCSQRCINTH
GSYKCLCVEG YAPRGGDPHS CKAVTDEEPF LIFANRYYLR KLNLDGSNYT LLKQGLNNAV
ALDFDYREQM IYWTDVTTQG SMIRRMHLNG SNVQVLHRTG LSNPDGLAVD WVGGNLYWCD
KGRDTIEVSK LNGAYRTVLV SSGLREPRAL VVDVQNGYLY WTDWGDHSLI GRIGMDGSSR
SVIVDTKITW PNGLTLDYVT ERIYWADARE DYIEFASLDG SNRHVVLSQD IPHIFALTLF
EDYVYWTDWE TKSINRAHKT TGTNKTLLIS TLHRPMDLHV FHALRQPDVP NHPCKVNNGG
CSNLCLLSPG GGHKCACPTN FYLGSDGRTC VSNCTASQFV CKNDKCIPFW WKCDTEDDCG
DHSDEPPDCP EFKCRPGQFQ CSTGICTNPA FICDGDNDCQ DNSDEANCDI HVCLPSQFKC
TNTNRCIPGI FRCNGQDNCG DGEDERDCPE VTCAPNQFQC SITKRCIPRV WVCDRDNDCV
DGSDEPANCT QMTCGVDEFR CKDSGRCIPA RWKCDGEDDC GDGSDEPKEE CDERTCEPYQ
FRCKNNRCVP GRWQCDYDND CGDNSDEESC TPRPCSESEF SCANGRCIAG RWKCDGDHDC
ADGSDEKDCT PRCDMDQFQC KSGHCIPLRW RCDADADCMD GSDEEACGTG VRTCPLDEFQ
CNNTLCKPLA WKCDGEDDCG DNSDENPEEC ARFVCPPNRP FRCKNDRVCL WIGRQCDGTD
NCGDGTDEED CEPPTAHTTH CKDKKEFLCR NQRCLSSSLR CNMFDDCGDG SDEEDCSIDP
KLTSCATNAS ICGDEARCVR TEKAAYCACR SGFHTVPGQP GCQDINECLR FGTCSQLCNN
TKGGHLCSCA RNFMKTHNTC KAEGSEYQVL YIADDNEIRS LFPGHPHSAY EQAFQGDESV
RIDAMDVHVK AGRVYWTNWH TGTISYRSLP PAAPPTTSNR HRRQIDRGVT HLNISGLKMP
RGIAIDWVAG NVYWTDSGRD VIEVAQMKGE NRKTLISGMI DEPHAIVVDP LRGTMYWSDW
GNHPKIETAA MDGTLRETLV QDNIQWPTGL AVDYHNERLY WADAKLSVIG SIRLNGTDPI
VAADSKRGLS HPFSIDVFED YIYGVTYINN RVFKIHKFGH SPLVNLTGGL SHASDVVLYH
QHKQPEVTNP CDRKKCEWLC LLSPSGPVCT CPNGKRLDNG TCVPVPSPTP PPDAPRPGTC
NLQCFNGGSC FLNARRQPKC RCQPRYTGDK CELDQCWEHC RNGGTCAASP SGMPTCRCPT
GFTGPKCTQQ VCAGYCANNS TCTVNQGNQP QCRCLPGFLG DRCQYRQCSG YCENFGTCQM
AADGSRQCRC TAYFEGSRCE VNKCSRCLEG ACVVNKQSGD VTCNCTDGRV APSCLTCVGH
CSNGGSCTMN SKMMPECQCP PHMTGPRCEE HVFSQQQPGH IASILIPLLL LLLLVLVAGV
VFWYKRRVQG AKGFQHQRMT NGAMNVEIGN PTYKMYEGGE PDDVGGLLDA DFALDPDKPT
NFTNPVYATL YMGGHGSRHS LASTDEKREL LGRGPEDEIG DPLA


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CSB-EL013091CH Chicken Prolow-density lipoprotein receptor-related protein 1(LRP1) ELISA kit SpeciesChicken 96T
CSB-EL013091MO Mouse Prolow-density lipoprotein receptor-related protein 1(LRP1) ELISA kit SpeciesMouse 96T
GWB-6B9E5F Anti- LRP1 (low density lipoprotein-related protein 1 (alpha-2-macroglobulin receptor)) Antibody
E2072m ELISA Kit FOR Prolow-density lipoprotein receptor-related protein 1; organism: Mouse; gene name: Lrp1 96T
E2072h ELISA Kit FOR Prolow-density lipoprotein receptor-related protein 1; organism: Human; gene name: LRP1 96T
CSB-EL013103HU Human low density lipoprotein receptor-related protein 8, apolipoprotein e receptor (LRP8) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL013103MO Mouse low density lipoprotein receptor-related protein 8, apolipoprotein e receptor (LRP8) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL013103CH Chicken low density lipoprotein receptor-related protein 8, apolipoprotein e receptor (LRP8) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
E02L0278 Rat low-density lipoprotein receptor-related protein 1 96 Tests/kit
E02L0279 Rat low-density lipoprotein-receptor-related protein 6 96 Tests/kit
YHB0684Ra Rat low-density lipoprotein-receptor-related protein,LRP-1 ELISA Kit 48T
EH1110 Low-density lipoprotein receptor-related protein 8 Elisa Kit 96T
201-11-0210 Rat low-density lipoprotein-receptor-related protein,LRP-1 ELISA Kit 96T
C389 Low-Density Lipoprotein Receptor-Related Protein 12 LRP12 500
EH1247 Low-density lipoprotein receptor-related protein 4 Elisa Kit 96T
E02L0278 Rat Low-density lipoprotein receptor-related protein 1 ELISA 96T/kit


 

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