A2ARV4 (LRP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name=LRP-2

Alternative name(s):
Glycoprotein 330
Short name=gp330
Megalin

Gene names

Name:

Lrp2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	4660 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts together with cubilin to mediate HDL endocytosis. Ref.4
Subunit structure	Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex together with a receptor-associated protein (RAP). Binds to ankyrin-repeat family A protein 2 (ANKRA2). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif. Ref.5
Subcellular location	Membrane; Single-pass type I membrane protein By similarity. Membrane › coated pit By similarity.
Sequence similarities	Belongs to the LDLR family. Contains 17 EGF-like domains. Contains 36 LDL-receptor class A domains. Contains 37 LDL-receptor class B repeats.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Coated pit Membrane
Domain	EGF-like domain Repeat SH3-binding Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Inferred from mutant phenotype PubMed 15623804. Source: MGI forebrain development Inferred from mutant phenotype PubMed 15623804. Source: MGI receptor-mediated endocytosis Inferred from mutant phenotype PubMed 10052453. Source: MGI vitamin metabolic process Inferred from mutant phenotype PubMed 10052453. Source: MGI
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 15616221. Source: MGI apical plasma membrane Inferred from direct assay PubMed 21938401. Source: UniProtKB brush border membrane Inferred from direct assay PubMed 10662735. Source: MGI coated pit Inferred from direct assay PubMed 15616221. Source: MGI endocytic vesicle Inferred from direct assay PubMed 15616221. Source: MGI endoplasmic reticulum Inferred from direct assay PubMed 15616221. Source: MGI endosome Inferred from direct assay Ref.4PubMed 12815097. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro receptor activity Inferred from sequence or structural similarity PubMed 10052453. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dab1	P97318	2	EBI-300875,EBI-81680
Dlg4	Q62108	2	EBI-300875,EBI-300895
Gipc1	Q9Z0G0	2	EBI-300875,EBI-300855
Mapk8ip1	Q9WVI9	2	EBI-300875,EBI-74515
Mapk8ip2	Q9ERE9	2	EBI-300875,EBI-74576
Synj2bp	Q9D6K5	2	EBI-300875,EBI-300910

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 4660	4635	Low-density lipoprotein receptor-related protein 2		PRO_0000309845
Regions
	Topological domain	26 – 4425	4400	Extracellular Potential
	Transmembrane	4426 – 4446	21	Helical; Potential
	Topological domain	4447 – 4660	214	Cytoplasmic Potential
	Domain	26 – 64	39	LDL-receptor class A 1
	Domain	65 – 105	41	LDL-receptor class A 2
	Domain	106 – 144	39	LDL-receptor class A 3
	Domain	145 – 181	37	LDL-receptor class A 4
	Domain	181 – 219	39	LDL-receptor class A 5
	Domain	220 – 258	39	LDL-receptor class A 6
	Domain	263 – 307	45	LDL-receptor class A 7
	Domain	308 – 346	39	EGF-like 1
	Domain	347 – 385	39	EGF-like 2
	Repeat	435 – 477	43	LDL-receptor class B 1
	Repeat	478 – 520	43	LDL-receptor class B 2
	Repeat	521 – 567	47	LDL-receptor class B 3
	Repeat	568 – 611	44	LDL-receptor class B 4
	Repeat	612 – 652	41	LDL-receptor class B 5
	Domain	658 – 704	47	EGF-like 3
	Repeat	752 – 794	43	LDL-receptor class B 6
	Repeat	795 – 836	42	LDL-receptor class B 7
	Repeat	837 – 880	44	LDL-receptor class B 8
	Repeat	881 – 924	44	LDL-receptor class B 9
	Domain	969 – 1013	45	EGF-like 4
	Domain	1023 – 1061	39	LDL-receptor class A 8
	Domain	1064 – 1103	40	LDL-receptor class A 9
	Domain	1108 – 1146	39	LDL-receptor class A 10
	Domain	1148 – 1186	39	LDL-receptor class A 11
	Domain	1186 – 1225	40	LDL-receptor class A 12
	Domain	1229 – 1269	41	LDL-receptor class A 13
	Domain	1270 – 1308	39	LDL-receptor class A 14
	Domain	1311 – 1351	41	LDL-receptor class A 15
	Domain	1350 – 1390	41	EGF-like 5
	Domain	1391 – 1430	40	EGF-like 6; calcium-binding Potential
	Repeat	1479 – 1521	43	LDL-receptor class B 10
	Repeat	1522 – 1564	43	LDL-receptor class B 11
	Repeat	1567 – 1610	44	LDL-receptor class B 12
	Repeat	1611 – 1654	44	LDL-receptor class B 13
	Repeat	1655 – 1696	42	LDL-receptor class B 14
	Domain	1701 – 1742	42	EGF-like 7
	Repeat	1791 – 1833	43	LDL-receptor class B 15
	Repeat	1834 – 1883	50	LDL-receptor class B 16
	Repeat	1884 – 1931	48	LDL-receptor class B 17
	Repeat	1932 – 1972	41	LDL-receptor class B 18
	Repeat	1973 – 2014	42	LDL-receptor class B 19
	Domain	2019 – 2060	42	EGF-like 8
	Repeat	2108 – 2157	50	LDL-receptor class B 20
	Repeat	2158 – 2202	45	LDL-receptor class B 21
	Repeat	2203 – 2246	44	LDL-receptor class B 22
	Repeat	2247 – 2290	44	LDL-receptor class B 23
	Repeat	2291 – 2332	42	LDL-receptor class B 24
	Domain	2343 – 2384	42	EGF-like 9
	Repeat	2433 – 2478	46	LDL-receptor class B 25
	Repeat	2479 – 2519	41	LDL-receptor class B 26
	Repeat	2520 – 2563	44	LDL-receptor class B 27
	Repeat	2564 – 2604	41	LDL-receptor class B 28
	Repeat	2605 – 2647	43	LDL-receptor class B 29
	Domain	2652 – 2694	43	EGF-like 10
	Domain	2699 – 2739	41	LDL-receptor class A 16
	Domain	2740 – 2778	39	LDL-receptor class A 17
	Domain	2779 – 2820	42	LDL-receptor class A 18
	Domain	2821 – 2862	42	LDL-receptor class A 19
	Domain	2863 – 2903	41	LDL-receptor class A 20
	Domain	2906 – 2947	42	LDL-receptor class A 21
	Domain	2948 – 2992	45	LDL-receptor class A 22
	Domain	2993 – 3031	39	LDL-receptor class A 23
	Domain	3032 – 3072	41	LDL-receptor class A 24
	Domain	3075 – 3112	38	LDL-receptor class A 25
	Domain	3113 – 3153	41	EGF-like 11
	Domain	3154 – 3194	41	EGF-like 12; calcium-binding Potential
	Repeat	3241 – 3283	43	LDL-receptor class B 30
	Repeat	3284 – 3326	43	LDL-receptor class B 31
	Repeat	3335 – 3378	44	LDL-receptor class B 32
	Repeat	3379 – 3420	42	LDL-receptor class B 33
	Repeat	3421 – 3462	42	LDL-receptor class B 34
	Domain	3467 – 3511	45	EGF-like 13
	Domain	3512 – 3552	41	LDL-receptor class A 26
	Domain	3553 – 3593	41	LDL-receptor class A 27
	Domain	3594 – 3634	41	LDL-receptor class A 28
	Domain	3635 – 3675	41	LDL-receptor class A 29
	Domain	3678 – 3718	41	LDL-receptor class A 30
	Domain	3719 – 3758	40	LDL-receptor class A 31
	Domain	3759 – 3797	39	LDL-receptor class A 32
	Domain	3798 – 3836	39	LDL-receptor class A 33
	Domain	3842 – 3882	41	LDL-receptor class A 34
	Domain	3883 – 3924	42	LDL-receptor class A 35
	Domain	3928 – 3966	39	LDL-receptor class A 36
	Domain	3968 – 4008	41	EGF-like 14
	Domain	4009 – 4050	42	EGF-like 15; calcium-binding Potential
	Repeat	4156 – 4198	43	LDL-receptor class B 35
	Repeat	4199 – 4242	44	LDL-receptor class B 36
	Repeat	4244 – 4285	42	LDL-receptor class B 37
	Domain	4332 – 4370	39	EGF-like 16
	Domain	4379 – 4413	35	EGF-like 17
	Region	4597 – 4610	14	Interaction with DAB2 By similarity
	Motif	1743 – 1745	3	Cell attachment site Potential
	Motif	4454 – 4463	10	SH3-binding Potential
	Motif	4522 – 4527	6	Endocytosis signal Potential
	Motif	4601 – 4606	6	NPXY motif
	Motif	4606 – 4609	4	SH2-binding Potential
	Motif	4619 – 4630	12	SH3-binding Potential
Sites
	Metal binding	1206	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1209	1	Calcium By similarity
	Metal binding	1211	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1213	1	Calcium By similarity
	Metal binding	1219	1	Calcium By similarity
	Metal binding	1220	1	Calcium By similarity
Amino acid modifications
	Modified residue	4464	1	Phosphoserine Ref.6
	Modified residue	4472	1	Phosphoserine Ref.6
	Glycosylation	159	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	299	1	N-linked (GlcNAc...) Potential
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Glycosylation	387	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	399	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	462	1	N-linked (GlcNAc...) Potential
	Glycosylation	657	1	N-linked (GlcNAc...) Potential
	Glycosylation	865	1	N-linked (GlcNAc...) Potential
	Glycosylation	1063	1	N-linked (GlcNAc...) Potential
	Glycosylation	1187	1	N-linked (GlcNAc...) Potential
	Glycosylation	1328	1	N-linked (GlcNAc...) Potential
	Glycosylation	1341	1	N-linked (GlcNAc...) Potential
	Glycosylation	1384	1	N-linked (GlcNAc...) Potential
	Glycosylation	1451	1	N-linked (GlcNAc...) Potential
	Glycosylation	1497	1	N-linked (GlcNAc...) Potential
	Glycosylation	1551	1	N-linked (GlcNAc...) Potential
	Glycosylation	1676	1	N-linked (GlcNAc...) Potential
	Glycosylation	1733	1	N-linked (GlcNAc...) Potential
	Glycosylation	1811	1	N-linked (GlcNAc...) Potential
	Glycosylation	2131	1	N-linked (GlcNAc...) Potential
	Glycosylation	2134	1	N-linked (GlcNAc...) Potential
	Glycosylation	2178	1	N-linked (GlcNAc...) Potential
	Glycosylation	2225	1	N-linked (GlcNAc...) Potential
	Glycosylation	2396	1	N-linked (GlcNAc...) Potential
	Glycosylation	2488	1	N-linked (GlcNAc...) Potential
	Glycosylation	2548	1	N-linked (GlcNAc...) Potential
	Glycosylation	2782	1	N-linked (GlcNAc...) Potential
	Glycosylation	2810	1	N-linked (GlcNAc...) Potential
	Glycosylation	2949	1	N-linked (GlcNAc...) Potential
	Glycosylation	2989	1	N-linked (GlcNAc...) Potential
	Glycosylation	3127	1	N-linked (GlcNAc...) Potential
	Glycosylation	3213	1	N-linked (GlcNAc...) Potential
	Glycosylation	3259	1	N-linked (GlcNAc...) Potential
	Glycosylation	3317	1	N-linked (GlcNAc...) Potential
	Glycosylation	3357	1	N-linked (GlcNAc...) Potential
	Glycosylation	3448	1	N-linked (GlcNAc...) Potential
	Glycosylation	3566	1	N-linked (GlcNAc...) Potential
	Glycosylation	3682	1	N-linked (GlcNAc...) Potential
	Glycosylation	3840	1	N-linked (GlcNAc...) Potential
	Glycosylation	3969	1	N-linked (GlcNAc...) Potential
	Glycosylation	3980	1	N-linked (GlcNAc...) Potential
	Glycosylation	4070	1	N-linked (GlcNAc...) Potential
	Glycosylation	4329	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 40		By similarity
	Disulfide bond	35 ↔ 53		By similarity
	Disulfide bond	47 ↔ 62		By similarity
	Disulfide bond	67 ↔ 80		By similarity
	Disulfide bond	74 ↔ 93		By similarity
	Disulfide bond	87 ↔ 103		By similarity
	Disulfide bond	108 ↔ 120		By similarity
	Disulfide bond	115 ↔ 133		By similarity
	Disulfide bond	127 ↔ 142		By similarity
	Disulfide bond	147 ↔ 157		By similarity
	Disulfide bond	152 ↔ 170		By similarity
	Disulfide bond	164 ↔ 179		By similarity
	Disulfide bond	183 ↔ 195		By similarity
	Disulfide bond	190 ↔ 208		By similarity
	Disulfide bond	202 ↔ 217		By similarity
	Disulfide bond	222 ↔ 234		By similarity
	Disulfide bond	229 ↔ 247		By similarity
	Disulfide bond	241 ↔ 256		By similarity
	Disulfide bond	265 ↔ 278		By similarity
	Disulfide bond	272 ↔ 291		By similarity
	Disulfide bond	285 ↔ 306		By similarity
	Disulfide bond	311 ↔ 320		By similarity
	Disulfide bond	316 ↔ 329		By similarity
	Disulfide bond	331 ↔ 345		By similarity
	Disulfide bond	351 ↔ 361		By similarity
	Disulfide bond	357 ↔ 370		By similarity
	Disulfide bond	372 ↔ 384		By similarity
	Disulfide bond	662 ↔ 673		By similarity
	Disulfide bond	669 ↔ 688		By similarity
	Disulfide bond	690 ↔ 703		By similarity
	Disulfide bond	973 ↔ 987		By similarity
	Disulfide bond	983 ↔ 997		By similarity
	Disulfide bond	999 ↔ 1012		By similarity
	Disulfide bond	1025 ↔ 1037		By similarity
	Disulfide bond	1032 ↔ 1050		By similarity
	Disulfide bond	1044 ↔ 1059		By similarity
	Disulfide bond	1066 ↔ 1079		By similarity
	Disulfide bond	1073 ↔ 1092		By similarity
	Disulfide bond	1086 ↔ 1101		By similarity
	Disulfide bond	1110 ↔ 1122		By similarity
	Disulfide bond	1117 ↔ 1135		By similarity
	Disulfide bond	1129 ↔ 1144		By similarity
	Disulfide bond	1150 ↔ 1162		By similarity
	Disulfide bond	1157 ↔ 1175		By similarity
	Disulfide bond	1169 ↔ 1184		By similarity
	Disulfide bond	1188 ↔ 1201		By similarity
	Disulfide bond	1195 ↔ 1214		By similarity
	Disulfide bond	1208 ↔ 1223		By similarity
	Disulfide bond	1231 ↔ 1244		By similarity
	Disulfide bond	1238 ↔ 1257		By similarity
	Disulfide bond	1251 ↔ 1267		By similarity
	Disulfide bond	1272 ↔ 1284		By similarity
	Disulfide bond	1279 ↔ 1297		By similarity
	Disulfide bond	1291 ↔ 1306		By similarity
	Disulfide bond	1313 ↔ 1326		By similarity
	Disulfide bond	1320 ↔ 1339		By similarity
	Disulfide bond	1333 ↔ 1349		By similarity
	Disulfide bond	1354 ↔ 1365		By similarity
	Disulfide bond	1361 ↔ 1374		By similarity
	Disulfide bond	1376 ↔ 1389		By similarity
	Disulfide bond	1395 ↔ 1405		By similarity
	Disulfide bond	1401 ↔ 1414		By similarity
	Disulfide bond	1416 ↔ 1429		By similarity
	Disulfide bond	1705 ↔ 1714		By similarity
	Disulfide bond	1710 ↔ 1726		By similarity
	Disulfide bond	1728 ↔ 1741		By similarity
	Disulfide bond	2023 ↔ 2034		By similarity
	Disulfide bond	2030 ↔ 2044		By similarity
	Disulfide bond	2046 ↔ 2059		By similarity
	Disulfide bond	2347 ↔ 2358		By similarity
	Disulfide bond	2354 ↔ 2369		By similarity
	Disulfide bond	2371 ↔ 2383		By similarity
	Disulfide bond	2656 ↔ 2667		By similarity
	Disulfide bond	2663 ↔ 2676		By similarity
	Disulfide bond	2678 ↔ 2693		By similarity
	Disulfide bond	2701 ↔ 2713		By similarity
	Disulfide bond	2708 ↔ 2726		By similarity
	Disulfide bond	2720 ↔ 2737		By similarity
	Disulfide bond	2742 ↔ 2754		By similarity
	Disulfide bond	2749 ↔ 2767		By similarity
	Disulfide bond	2761 ↔ 2776		By similarity
	Disulfide bond	2781 ↔ 2794		By similarity
	Disulfide bond	2789 ↔ 2807		By similarity
	Disulfide bond	2801 ↔ 2818		By similarity
	Disulfide bond	2823 ↔ 2836		By similarity
	Disulfide bond	2830 ↔ 2849		By similarity
	Disulfide bond	2843 ↔ 2860		By similarity
	Disulfide bond	2865 ↔ 2878		By similarity
	Disulfide bond	2872 ↔ 2891		By similarity
	Disulfide bond	2885 ↔ 2901		By similarity
	Disulfide bond	2908 ↔ 2920		By similarity
	Disulfide bond	2915 ↔ 2933		By similarity
	Disulfide bond	2927 ↔ 2945		By similarity
	Disulfide bond	2950 ↔ 2967		By similarity
	Disulfide bond	2957 ↔ 2980		By similarity
	Disulfide bond	2974 ↔ 2990		By similarity
	Disulfide bond	2995 ↔ 3007		By similarity
	Disulfide bond	3002 ↔ 3020		By similarity
	Disulfide bond	3014 ↔ 3029		By similarity
	Disulfide bond	3034 ↔ 3046		By similarity
	Disulfide bond	3041 ↔ 3059		By similarity
	Disulfide bond	3053 ↔ 3070		By similarity
	Disulfide bond	3077 ↔ 3089		By similarity
	Disulfide bond	3084 ↔ 3102		By similarity
	Disulfide bond	3096 ↔ 3111		By similarity
	Disulfide bond	3116 ↔ 3128		By similarity
	Disulfide bond	3124 ↔ 3137		By similarity
	Disulfide bond	3139 ↔ 3152		By similarity
	Disulfide bond	3158 ↔ 3169		By similarity
	Disulfide bond	3165 ↔ 3178		By similarity
	Disulfide bond	3180 ↔ 3193		By similarity
	Disulfide bond	3471 ↔ 3482		By similarity
	Disulfide bond	3478 ↔ 3493		By similarity
	Disulfide bond	3495 ↔ 3510		By similarity
	Disulfide bond	3514 ↔ 3527		By similarity
	Disulfide bond	3521 ↔ 3540		By similarity
	Disulfide bond	3534 ↔ 3550		By similarity
	Disulfide bond	3555 ↔ 3567		By similarity
	Disulfide bond	3562 ↔ 3580		By similarity
	Disulfide bond	3574 ↔ 3591		By similarity
	Disulfide bond	3596 ↔ 3608		By similarity
	Disulfide bond	3603 ↔ 3621		By similarity
	Disulfide bond	3615 ↔ 3632		By similarity
	Disulfide bond	3637 ↔ 3649		By similarity
	Disulfide bond	3644 ↔ 3662		By similarity
	Disulfide bond	3656 ↔ 3673		By similarity
	Disulfide bond	3680 ↔ 3694		By similarity
	Disulfide bond	3688 ↔ 3707		By similarity
	Disulfide bond	3701 ↔ 3716		By similarity
	Disulfide bond	3721 ↔ 3734		By similarity
	Disulfide bond	3729 ↔ 3747		By similarity
	Disulfide bond	3741 ↔ 3756		By similarity
	Disulfide bond	3761 ↔ 3773		By similarity
	Disulfide bond	3768 ↔ 3786		By similarity
	Disulfide bond	3780 ↔ 3795		By similarity
	Disulfide bond	3800 ↔ 3812		By similarity
	Disulfide bond	3807 ↔ 3825		By similarity
	Disulfide bond	3819 ↔ 3834		By similarity
	Disulfide bond	3844 ↔ 3856		By similarity
	Disulfide bond	3851 ↔ 3869		By similarity
	Disulfide bond	3863 ↔ 3880		By similarity
	Disulfide bond	3885 ↔ 3898		By similarity
	Disulfide bond	3893 ↔ 3911		By similarity
	Disulfide bond	3905 ↔ 3922		By similarity
	Disulfide bond	3930 ↔ 3942		By similarity
	Disulfide bond	3937 ↔ 3955		By similarity
	Disulfide bond	3949 ↔ 3964		By similarity
	Disulfide bond	3972 ↔ 3981		By similarity
	Disulfide bond	3977 ↔ 3991		By similarity
	Disulfide bond	3993 ↔ 4007		By similarity
	Disulfide bond	4013 ↔ 4023		By similarity
	Disulfide bond	4019 ↔ 4032		By similarity
	Disulfide bond	4034 ↔ 4049		By similarity
	Disulfide bond	4336 ↔ 4344		By similarity
	Disulfide bond	4340 ↔ 4353		By similarity
	Disulfide bond	4355 ↔ 4369		By similarity
	Disulfide bond	4383 ↔ 4391		By similarity
	Disulfide bond	4385 ↔ 4401		By similarity
	Disulfide bond	4403 ↔ 4412		By similarity
Experimental info
	Sequence conflict	4198	1	L → F in CAA69877. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	A2ARV4 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 4CF399C24DF2FAA4	FASTA	4,660	519,208
	10 20 30 40 50 60 MERGAAAAAW MLLLAIAACL APVSGQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI 70 80 90 100 110 120 GCPPRSCGSG FFLCPAEGTC IPSSWVCDQD KDCSDGADEQ QNCPGTTCSS QQLTCSNGQC 130 140 150 160 170 180 VPIEYRCDHV SDCPDGSDER NCYYPTCDQL TCANGACYNT SQKCDHKVDC RDSSDEANCT 190 200 210 220 230 240 TLCSQKEFQC GSGECILRAY VCDHDNDCED NSDEHNCNYD TCGGHQFTCS NGQCINQNWV 250 260 270 280 290 300 CDGDDDCQDS GDEDGCESNQ RHHTCYPREW ACPGSGRCIS MDKVCDGVPD CPEGEDENNA 310 320 330 340 350 360 TSGRYCGTGL CSILNCEYQC HQTPYGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK 370 380 390 400 410 420 CESRQGRHQC LCEEGYILER GQHCKSNDSF SAASIIFSNG RDLLVGDLHG RNFRILAESK 430 440 450 460 470 480 NRGIVMGVDF HYQKHRVFWT DPMQAKVFST DINGLNTQEI LNVSIDAPEN LAVDWINNKL 490 500 510 520 530 540 YLVETRVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA 550 560 570 580 590 600 FMDGSNRKDL VTTKLGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV 610 620 630 640 650 660 PHPFGISLFE EHVFFTDWTK MAVMKANKFT DTNPQVYHQS SLTPFGVTVY HALRQPNATN 670 680 690 700 710 720 PCGNNNGGCA QICVLSHRTD NGGLGYRCKC EFGFELDADE HHCVAVKNFL LFSSQTAVRG 730 740 750 760 770 780 IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTIFYSDLS KNIIYQQKID GTGKEVITAN 790 800 810 820 830 840 RLQNVECLSF DWISRNLYWT DGGSKSVTVM KLADKSRRQI ISNLNNPRSI VVHPAAGYMF 850 860 870 880 890 900 LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWST SRLYWVDAFF DKIEHSNLDG 910 920 930 940 950 960 LDRKRLGHVD QMTHPFGLTV FKDNVFLTDW RLGAIIRVRK SDGGDMTVVR RGISSIMHVK 970 980 990 1000 1010 1020 AYDADLQTGT NYCSQTTHPN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP 1030 1040 1050 1060 1070 1080 PTQQCGSSSF PCNNGKCVPS IFRCDGVDDC HDNSDEHQCG ALNNTCSSSA FTCVHGGQCI 1090 1100 1110 1120 1130 1140 PGQWRCDKQN DCLDGSDEQN CPTRSPSSTC PPTSFTCDNH MCIPKEWVCD TDNDCSDGSD 1150 1160 1170 1180 1190 1200 EKNCQASGTC HPTQFRCPDH RCISPLYVCD GDKDCVDGSD EAGCVLNCTS SQFKCADGSS 1210 1220 1230 1240 1250 1260 CINSRYRCDG VYDCKDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIQG 1270 1280 1290 1300 1310 1320 SDEHNGCVPK TCSPSHFLCD NGNCIYNSWV CDGDNDCRDM SDEKDCPTQP FHCPSSQWQC 1330 1340 1350 1360 1370 1380 PGYSICVNLS ALCDGVFDCP NGTDESPLCN QDSCLHFNGG CTHRCIQGPF GATCVCPIGY 1390 1400 1410 1420 1430 1440 QLANDTKTCE DVNECDIPGF CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTASENLLLV 1450 1460 1470 1480 1490 1500 VASRDKIIMD NITAHTHNIY SLVQDVSFVV ALDFDSVTGR VFWSDLLEGK TWSAFQNGTD 1510 1520 1530 1540 1550 1560 KRVVHDSGLS LTEMIAVDWI GRNIYWTDYT LETIEVSKID GSHRTVLISK NVTKPRGLAL 1570 1580 1590 1600 1610 1620 DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW PCGLSIDYPN RLIYFMDAYL 1630 1640 1650 1660 1670 1680 DYIEFCDYDG QNRRQVIASD LVLHHPHALT LFEDSVFWTD RGTHQVMQAN KWHGRNQSVV 1690 1700 1710 1720 1730 1740 MYSVPQPLGI IAIHPSRQPS SPNPCASATC SHLCLLSAQE PRHYSCACPS GWNLSDDSVN 1750 1760 1770 1780 1790 1800 CVRGDQPFLI SVRENVIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG 1810 1820 1830 1840 1850 1860 EIHRVKTDGS NRTAFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT LRGDTRYGKT 1870 1880 1890 1900 1910 1920 LITNDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK IASANMDGTS LKILFTGNME 1930 1940 1950 1960 1970 1980 HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD GTERMILVHH LAHPWGLVVH GSFLYYSDEQ 1990 2000 2010 2020 2030 2040 YEVIERVDKS SGSNKVVFRD NIPYLRGLRV YHHRNAADSS NGCSNNPNAC QQICLPVPGG 2050 2060 2070 2080 2090 2100 MFSCACASGF KLSPDGRSCS PYNSFIVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH 2110 2120 2130 2140 2150 2160 ADVDVANGFI YWCDFSSSVR SSNGIRRIKP NGSNFTNIVT YGIGANGIRG VAVDWVAGNL 2170 2180 2190 2200 2210 2220 YFTNAFVYET LIEVIRINTT YRRVLLKVSV DMPRHIVVDP KHRYLFWADY GQKPKIERSF 2230 2240 2250 2260 2270 2280 LDCTNRTVLV SEGIVTPRGL AVDHDTGYIY WVDDSLDIIA RIHRDGGESQ VVRYGSRYPT 2290 2300 2310 2320 2330 2340 PYGITVFGES IIWVDRNLRK VFQASKQPGN TDPPTVIRDS INLLRDVTIF DEHVQPLSPA 2350 2360 2370 2380 2390 2400 ELNNNPCLQS NGGCSHFCFA LPELPTPKCG CAFGTLEDDG KNCATSREDF LIYSLNNSLR 2410 2420 2430 2440 2450 2460 SLHFDPQDHN LPFQAISVEG MAIALDYDRR NNRIFFTQKL NPIRGQISYV NLYSGASSPT 2470 2480 2490 2500 2510 2520 ILLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN RAVIARVSKP RAIVLDPCRG 2530 2540 2550 2560 2570 2580 YMYWTDWGTN AKIERATLGG NFRVPIVNTS LVWPNGLTLD LETDLLYWAD ASLQKIERST 2590 2600 2610 2620 2630 2640 LTGSNREVVI STAFHSFGLT VYGQYIYWTD FYTKKIYRAN KYDGSDLIAM TTRLPTQPSG 2650 2660 2670 2680 2690 2700 ISTVVKTQQQ QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGSWYLANDN KYCVVDTGAR 2710 2720 2730 2740 2750 2760 CNQFQFTCLN GRCISQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCA NGRCVPYHYR 2770 2780 2790 2800 2810 2820 CDFYNDCGDN SDEAGCLFRS CNSTTEFTCS NGRCIPLSYV CNGINNCHDN DTSDEKNCPP 2830 2840 2850 2860 2870 2880 ITCQPDFAKC QTTNICVPRA FLCDGDNDCG DGSDENPIYC ASHTCRSNEF QCVSPHRCIP 2890 2900 2910 2920 2930 2940 SYWFCDGEAD CVDSSDEPDT CGHSLNSCSA NQFHCDNGRC ISSSWVCDGD NDCGDMSDED 2950 2960 2970 2980 2990 3000 QRHHCELQNC SSTEFTCINS RPPNRRCIPQ HWVCDGDADC ADALDELQNC TMRACSTGEF 3010 3020 3030 3040 3050 3060 SCANGRCIRQ SFRCDRRNDC GDYSDERGCS YPPCRDDQFT CQNGQCITKL YVCDEDNDCG 3070 3080 3090 3100 3110 3120 DGSDEQEHLC HTPEPTCPPH QFRCDNGHCI EMGTVCNHVD DCSDNSDEKG CGINECQDSS 3130 3140 3150 3160 3170 3180 ISHCDHNCTD TITSFYCSCL PGYKLMSDKR TCVDIDECKE TPQLCSQKCE NVIGSYICKC 3190 3200 3210 3220 3230 3240 APGYIREPDG KSCRQNSNIE PYLVFSNRYY IRNLTIDGTS YSLILQGLGN VVALDFDRVE 3250 3260 3270 3280 3290 3300 ERLYWIDAEK QIIERMFLNK TNQETIISHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD 3310 3320 3330 3340 3350 3360 LEGRQRKMLA QHCVDANNTF CFENPRGIVL HPQRGYVYWA DWGDHAYIAR IGMDGTNKTV 3370 3380 3390 3400 3410 3420 IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH RHTVYDGTLP HPFALTIFED 3430 3440 3450 3460 3470 3480 TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT HKPFDIHVLH PYRQPIMSNP CATNNGGCSH 3490 3500 3510 3520 3530 3540 LCLIKAGGRG FTCECPDDFQ TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC 3550 3560 3570 3580 3590 3600 SDGSDESDLC PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCEANE 3610 3620 3630 3640 3650 3660 WQCANKRCIP EYWQCDSVDD CLDNSDEDPS HCASRTCRPG QFKCNNGRCI PQSWKCDVDN 3670 3680 3690 3700 3710 3720 DCGDYSDEPI HECMTAAYNC DNHTEFSCKT NYRCIPQWAV CNGFDDCRDN SDEQGCESVP 3730 3740 3750 3760 3770 3780 CHPSGDFRCG NHHCIPLRWK CDGIDDCGDN SDEESCVPRE CTESEFRCAD QQCIPSRWVC 3790 3800 3810 3820 3830 3840 DQENDCGDNS DERDCEMKTC HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN 3850 3860 3870 3880 3890 3900 GTYCPAAMFE CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNVPCESPQR FRCDNSRCIY 3910 3920 3930 3940 3950 3960 GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCVSQHYVCD NVDDCGDLSD 3970 3980 3990 4000 4010 4020 ETGCNLGENR TCAEKICEQN CTQLSNGGFI CSCRPGFKPS TLDKNSCQDI NECEEFGICP 4030 4040 4050 4060 4070 4080 QSCRNSKGSY ECFCVDGFKS MSTHYGERCA ADGSPPLLLL PENVRIRKYN ISSEKFSEYL 4090 4100 4110 4120 4130 4140 EEEEHIQAID YDWDPEGIGL SVVYYTVLSQ GSQFGAIKRA YLPDFESGSN NPVREVDLGL 4150 4160 4170 4180 4190 4200 KYLMQPDGLA VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL 4210 4220 4230 4240 4250 4260 MFWTDQGKQP KIESAWMNGE HRSVLASANL GWPNGLSIDY LNGDRIYWSD SKEDVIESIK 4270 4280 4290 4300 4310 4320 YDGTDRRLII NDAMKPFSLD IFEDQLYWVA KEKGEVWRQN KFGKGNKEKL LVVNPWLTQV 4330 4340 4350 4360 4370 4380 RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG YSCACPQGSD FVTGSTVECD AASELPITMP 4390 4400 4410 4420 4430 4440 SPCRCMHGGS CYFDENDLPK CKCSSGYSGE YCEIGLSRGI PPGTTMALLL TFAMVIIVGA 4450 4460 4470 4480 4490 4500 LVLVGFFHYR KTGSLLPSLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI 4510 4520 4530 4540 4550 4560 IDRSMAMNEQ FVMEVGKQPV IFENPMYAAK DSTSKVGLAV QGPSVSSQVT VPENVENQNY 4570 4580 4590 4600 4610 4620 GRSIDPSEIV PEPKPASPGA DETQGTKWNI FKRKPKQTTN FENPIYAEMD TEQKEAVAVA 4630 4640 4650 4660 PPPSPSLPAK ASKRSSTPGY TATEDTFKDT ANLVKEDSDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4054-4660. Strain: C57BL/6J.
[3]	"Tubular modulation of clusterin in lupus-like glomerulonephritis." Moll S., Menoud P.A., Izui S. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4198-4320. Strain: NMRI. Tissue: Kidney.
[4]	"Megalin acts in concert with cubilin to mediate endocytosis of high density lipoproteins." Hammad S.M., Barth J.L., Knaak C., Argraves W.S. J. Biol. Chem. 275:12003-12008(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4465-4660, FUNCTION.
[5]	"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2." Morris S.M., Cooper J.A. Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAB2.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4464 AND SER-4472, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-387 AND ASN-399, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL845489 Genomic DNA. Translation: CAM20178.1. AK166702 mRNA. Translation: BAE38957.1. Y08566 mRNA. Translation: CAA69877.1. AF197160 mRNA. Translation: AAF61488.1.
IPI	IPI00349520.
RefSeq	NP_001074557.1. NM_001081088.1.
UniGene	Mm.23847.
3D structure databases
ProteinModelPortal	A2ARV4.
SMR	A2ARV4. Positions 26-1347, 1352-2695, 2701-4375.
ModBase	Search...
Protein-protein interaction databases
IntAct	A2ARV4. 9 interactions.
Protein family/group databases
TCDB	9.B.87.1.1. selenoprotein P receptor (SelP-receptor) family.
PTM databases
PhosphoSite	A2ARV4.
Proteomic databases
PaxDb	A2ARV4.
PRIDE	A2ARV4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070.
GeneID	14725.
KEGG	mmu:14725.
UCSC	uc008jyc.1. mouse.
Organism-specific databases
CTD	4036.
MGI	MGI:95794. Lrp2.
Phylogenomic databases
eggNOG	NOG235850.
GeneTree	ENSGT00700000104463.
HOGENOM	HOG000230574.
HOVERGEN	HBG097941.
InParanoid	A2ARV4.
KO	K06233.
OMA	TRPPGMC.
OrthoDB	EOG4WQ11K.
Gene expression databases
ArrayExpress	A2ARV4.
Bgee	A2ARV4.
Genevestigator	A2ARV4.
Family and domain databases
Gene3D	2.120.10.30. 8 hits. 4.10.400.10. 35 hits.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR026823. cEGF. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR009030. Growth_fac_rcpt. IPR023415. LDLR_class-A_CS. IPR000033. LDLR_classB_rpt. IPR002172. LDrepeatLR_classA_rpt. [Graphical view]
Pfam	PF12662. cEGF. 2 hits. PF07645. EGF_CA. 1 hit. PF00057. Ldl_recept_a. 34 hits. PF00058. Ldl_recept_b. 18 hits. [Graphical view]
SMART	SM00181. EGF. 14 hits. SM00179. EGF_CA. 3 hits. SM00192. LDLa. 36 hits. SM00135. LY. 37 hits. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 2 hits. SSF57424. LDL_rcpt_classA_cys-rich. 35 hits.
PROSITE	PS00010. ASX_HYDROXYL. 4 hits. PS00022. EGF_1. 1 hit. PS01186. EGF_2. 8 hits. PS50026. EGF_3. 6 hits. PS01187. EGF_CA. 3 hits. PS01209. LDLRA_1. 31 hits. PS50068. LDLRA_2. 36 hits. PS51120. LDLRB. 36 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	286749.
SOURCE	Search...

Entry information

Entry name

LRP2_MOUSE

Accession

Primary (citable) accession number: A2ARV4
Secondary accession number(s): P70215, Q3TL35, Q9JLB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program