Q9JI18 (LRP1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low-density lipoprotein receptor-related protein 1B
Short name=LRP-1B

Alternative name(s):
Low-density lipoprotein receptor-related protein-deleted in tumor
Short name=LRP-DIT

Gene names

Name:	Lrp1b
Synonyms:	Lrpdit

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	4599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis.
Subunit structure	Binds LRPAP1, PLAU, PLAT and SERPINE1; binding is followed by internalization and degradation of the ligands By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Sequence similarities	Belongs to the LDLR family. Contains 17 EGF-like domains. Contains 32 LDL-receptor class A domains. Contains 35 LDL-receptor class B repeats.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Membrane
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 15082773. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro low-density lipoprotein particle receptor binding Inferred from direct assay PubMed 15082773. Source: MGI low-density lipoprotein receptor activity Inferred from direct assay PubMed 15082773. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 4599	4579	Low-density lipoprotein receptor-related protein 1B		PRO_0000017320
Regions
	Topological domain	21 – 4444	4424	Extracellular Potential
	Transmembrane	4445 – 4467	23	Helical; Potential
	Topological domain	4468 – 4599	132	Cytoplasmic Potential
	Domain	31 – 70	40	LDL-receptor class A 1
	Domain	76 – 114	39	LDL-receptor class A 2
	Domain	120 – 154	35	EGF-like 1
	Domain	155 – 194	40	EGF-like 2; calcium-binding Potential
	Repeat	295 – 337	43	LDL-receptor class B 1
	Repeat	338 – 381	44	LDL-receptor class B 2
	Repeat	382 – 425	44	LDL-receptor class B 3
	Repeat	568 – 610	43	LDL-receptor class B 4
	Repeat	611 – 656	46	LDL-receptor class B 5
	Repeat	657 – 706	50	LDL-receptor class B 6
	Repeat	707 – 750	44	LDL-receptor class B 7
	Domain	794 – 834	41	EGF-like 3
	Domain	844 – 882	39	LDL-receptor class A 3
	Domain	885 – 923	39	LDL-receptor class A 4
	Domain	926 – 963	38	LDL-receptor class A 5
	Domain	966 – 1003	38	LDL-receptor class A 6
	Domain	1005 – 1043	39	LDL-receptor class A 7
	Domain	1052 – 1089	38	LDL-receptor class A 8
	Domain	1094 – 1132	39	LDL-receptor class A 9
	Domain	1135 – 1174	40	LDL-receptor class A 10
	Domain	1172 – 1213	42	EGF-like 4
	Repeat	1300 – 1346	47	LDL-receptor class B 8
	Repeat	1347 – 1389	43	LDL-receptor class B 9
	Repeat	1390 – 1436	47	LDL-receptor class B 10
	Repeat	1437 – 1480	44	LDL-receptor class B 11
	Repeat	1481 – 1522	42	LDL-receptor class B 12
	Domain	1527 – 1570	44	EGF-like 5
	Repeat	1618 – 1660	43	LDL-receptor class B 13
	Repeat	1661 – 1704	44	LDL-receptor class B 14
	Repeat	1705 – 1744	40	LDL-receptor class B 15
	Repeat	1745 – 1787	43	LDL-receptor class B 16
	Repeat	1788 – 1830	43	LDL-receptor class B 17
	Domain	1834 – 1875	42	EGF-like 6
	Repeat	1922 – 1964	43	LDL-receptor class B 18
	Repeat	1965 – 2007	43	LDL-receptor class B 19
	Repeat	2008 – 2051	44	LDL-receptor class B 20
	Repeat	2052 – 2095	44	LDL-receptor class B 21
	Domain	2143 – 2183	41	EGF-like 7
	Repeat	2239 – 2280	42	LDL-receptor class B 22
	Repeat	2281 – 2329	49	LDL-receptor class B 23
	Repeat	2330 – 2374	45	LDL-receptor class B 24
	Repeat	2375 – 2416	42	LDL-receptor class B 25
	Repeat	2417 – 2459	43	LDL-receptor class B 26
	Domain	2509 – 2548	40	LDL-receptor class A 11
	Domain	2551 – 2587	37	LDL-receptor class A 12
	Domain	2590 – 2626	37	LDL-receptor class A 13
	Domain	2629 – 2675	47	LDL-receptor class A 14
	Domain	2681 – 2717	37	LDL-receptor class A 15
	Domain	2719 – 2757	39	LDL-receptor class A 16
	Domain	2760 – 2800	41	LDL-receptor class A 17
	Domain	2804 – 2841	38	LDL-receptor class A 18
	Domain	2844 – 2885	42	LDL-receptor class A 19
	Domain	2890 – 2926	37	LDL-receptor class A 20
	Domain	2926 – 2967	42	EGF-like 8
	Domain	2968 – 3008	41	EGF-like 9
	Repeat	3055 – 3098	44	LDL-receptor class B 27
	Repeat	3099 – 3141	43	LDL-receptor class B 28
	Repeat	3142 – 3185	44	LDL-receptor class B 29
	Repeat	3186 – 3224	39	LDL-receptor class B 30
	Repeat	3225 – 3267	43	LDL-receptor class B 31
	Domain	3274 – 3314	41	EGF-like 10
	Domain	3316 – 3353	38	LDL-receptor class A 21
	Domain	3356 – 3392	37	LDL-receptor class A 22
	Domain	3395 – 3432	38	LDL-receptor class A 23
	Domain	3435 – 3472	38	LDL-receptor class A 24
	Domain	3475 – 3511	37	LDL-receptor class A 25
	Domain	3514 – 3550	37	LDL-receptor class A 26
	Domain	3552 – 3588	37	LDL-receptor class A 27
	Domain	3593 – 3629	37	LDL-receptor class A 28
	Domain	3631 – 3668	38	LDL-receptor class A 29
	Domain	3673 – 3711	39	LDL-receptor class A 30
	Domain	3714 – 3752	39	LDL-receptor class A 31
	Domain	3761 – 3797	37	LDL-receptor class A 32
	Domain	3801 – 3843	43	EGF-like 11
	Domain	3844 – 3881	38	EGF-like 12
	Repeat	3933 – 3980	48	LDL-receptor class B 32
	Repeat	3981 – 4037	57	LDL-receptor class B 33
	Repeat	4039 – 4082	44	LDL-receptor class B 34
	Repeat	4083 – 4127	45	LDL-receptor class B 35
	Domain	4213 – 4249	37	EGF-like 13
	Domain	4249 – 4290	42	EGF-like 14
	Domain	4286 – 4326	41	EGF-like 15
	Domain	4321 – 4363	43	EGF-like 16
	Domain	4392 – 4430	39	EGF-like 17
	Motif	4492 – 4495	4	Endocytosis signal Potential
	Motif	4559 – 4562	4	Endocytosis signal Potential
Amino acid modifications
	Glycosylation	134	1	N-linked (GlcNAc...) Potential
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Glycosylation	220	1	N-linked (GlcNAc...) Potential
	Glycosylation	313	1	N-linked (GlcNAc...) Potential
	Glycosylation	360	1	N-linked (GlcNAc...) Potential
	Glycosylation	443	1	N-linked (GlcNAc...) Potential
	Glycosylation	725	1	N-linked (GlcNAc...) Potential
	Glycosylation	758	1	N-linked (GlcNAc...) Potential
	Glycosylation	829	1	N-linked (GlcNAc...) Potential
	Glycosylation	883	1	N-linked (GlcNAc...) Potential
	Glycosylation	919	1	N-linked (GlcNAc...) Potential
	Glycosylation	1041	1	N-linked (GlcNAc...) Potential
	Glycosylation	1089	1	N-linked (GlcNAc...) Potential
	Glycosylation	1145	1	N-linked (GlcNAc...) Potential
	Glycosylation	1209	1	N-linked (GlcNAc...) Potential
	Glycosylation	1298	1	N-linked (GlcNAc...) Potential
	Glycosylation	1502	1	N-linked (GlcNAc...) Potential
	Glycosylation	1549	1	N-linked (GlcNAc...) Potential
	Glycosylation	1636	1	N-linked (GlcNAc...) Potential
	Glycosylation	1754	1	N-linked (GlcNAc...) Potential
	Glycosylation	1816	1	N-linked (GlcNAc...) Potential
	Glycosylation	1921	1	N-linked (GlcNAc...) Potential
	Glycosylation	1983	1	N-linked (GlcNAc...) Potential
	Glycosylation	2105	1	N-linked (GlcNAc...) Potential
	Glycosylation	2458	1	N-linked (GlcNAc...) Potential
	Glycosylation	2488	1	N-linked (GlcNAc...) Potential
	Glycosylation	2507	1	N-linked (GlcNAc...) Potential
	Glycosylation	2549	1	N-linked (GlcNAc...) Potential
	Glycosylation	2626	1	N-linked (GlcNAc...) Potential
	Glycosylation	2647	1	N-linked (GlcNAc...) Potential
	Glycosylation	2802	1	N-linked (GlcNAc...) Potential
	Glycosylation	2892	1	N-linked (GlcNAc...) Potential
	Glycosylation	3034	1	N-linked (GlcNAc...) Potential
	Glycosylation	3066	1	N-linked (GlcNAc...) Potential
	Glycosylation	3076	1	N-linked (GlcNAc...) Potential
	Glycosylation	3164	1	N-linked (GlcNAc...) Potential
	Glycosylation	3310	1	N-linked (GlcNAc...) Potential
	Glycosylation	3316	1	N-linked (GlcNAc...) Potential
	Glycosylation	3682	1	N-linked (GlcNAc...) Potential
	Glycosylation	3877	1	N-linked (GlcNAc...) Potential
	Glycosylation	3894	1	N-linked (GlcNAc...) Potential
	Glycosylation	3906	1	N-linked (GlcNAc...) Potential
	Glycosylation	4017	1	N-linked (GlcNAc...) Potential
	Glycosylation	4204	1	N-linked (GlcNAc...) Potential
	Glycosylation	4381	1	N-linked (GlcNAc...) Potential
	Glycosylation	4420	1	N-linked (GlcNAc...) Potential
	Disulfide bond	32 ↔ 45		By similarity
	Disulfide bond	39 ↔ 58		By similarity
	Disulfide bond	52 ↔ 69		By similarity
	Disulfide bond	77 ↔ 90		By similarity
	Disulfide bond	84 ↔ 103		By similarity
	Disulfide bond	97 ↔ 113		By similarity
	Disulfide bond	159 ↔ 169		By similarity
	Disulfide bond	165 ↔ 178		By similarity
	Disulfide bond	180 ↔ 193		By similarity
	Disulfide bond	798 ↔ 809		By similarity
	Disulfide bond	805 ↔ 818		By similarity
	Disulfide bond	820 ↔ 833		By similarity
	Disulfide bond	845 ↔ 857		By similarity
	Disulfide bond	852 ↔ 870		By similarity
	Disulfide bond	864 ↔ 881		By similarity
	Disulfide bond	886 ↔ 898		By similarity
	Disulfide bond	893 ↔ 911		By similarity
	Disulfide bond	905 ↔ 922		By similarity
	Disulfide bond	927 ↔ 939		By similarity
	Disulfide bond	934 ↔ 952		By similarity
	Disulfide bond	946 ↔ 962		By similarity
	Disulfide bond	967 ↔ 980		By similarity
	Disulfide bond	975 ↔ 993		By similarity
	Disulfide bond	987 ↔ 1002		By similarity
	Disulfide bond	1006 ↔ 1018		By similarity
	Disulfide bond	1013 ↔ 1031		By similarity
	Disulfide bond	1025 ↔ 1042		By similarity
	Disulfide bond	1053 ↔ 1066		By similarity
	Disulfide bond	1060 ↔ 1079		By similarity
	Disulfide bond	1073 ↔ 1088		By similarity
	Disulfide bond	1095 ↔ 1109		By similarity
	Disulfide bond	1103 ↔ 1122		By similarity
	Disulfide bond	1116 ↔ 1131		By similarity
	Disulfide bond	1136 ↔ 1150		By similarity
	Disulfide bond	1143 ↔ 1163		By similarity
	Disulfide bond	1157 ↔ 1173		By similarity
	Disulfide bond	1176 ↔ 1187		By similarity
	Disulfide bond	1183 ↔ 1197		By similarity
	Disulfide bond	1199 ↔ 1212		By similarity
	Disulfide bond	1531 ↔ 1544		By similarity
	Disulfide bond	1540 ↔ 1554		By similarity
	Disulfide bond	1556 ↔ 1569		By similarity
	Disulfide bond	1838 ↔ 1849		By similarity
	Disulfide bond	1845 ↔ 1859		By similarity
	Disulfide bond	1861 ↔ 1874		By similarity
	Disulfide bond	2147 ↔ 2158		By similarity
	Disulfide bond	2154 ↔ 2168		By similarity
	Disulfide bond	2170 ↔ 2182		By similarity
	Disulfide bond	2510 ↔ 2523		By similarity
	Disulfide bond	2518 ↔ 2536		By similarity
	Disulfide bond	2530 ↔ 2547		By similarity
	Disulfide bond	2552 ↔ 2564		By similarity
	Disulfide bond	2559 ↔ 2577		By similarity
	Disulfide bond	2571 ↔ 2586		By similarity
	Disulfide bond	2591 ↔ 2603		By similarity
	Disulfide bond	2598 ↔ 2616		By similarity
	Disulfide bond	2610 ↔ 2625		By similarity
	Disulfide bond	2630 ↔ 2652		By similarity
	Disulfide bond	2646 ↔ 2665		By similarity
	Disulfide bond	2659 ↔ 2674		By similarity
	Disulfide bond	2682 ↔ 2694		By similarity
	Disulfide bond	2689 ↔ 2707		By similarity
	Disulfide bond	2701 ↔ 2716		By similarity
	Disulfide bond	2720 ↔ 2732		By similarity
	Disulfide bond	2727 ↔ 2745		By similarity
	Disulfide bond	2739 ↔ 2756		By similarity
	Disulfide bond	2761 ↔ 2774		By similarity
	Disulfide bond	2768 ↔ 2787		By similarity
	Disulfide bond	2781 ↔ 2799		By similarity
	Disulfide bond	2805 ↔ 2817		By similarity
	Disulfide bond	2812 ↔ 2830		By similarity
	Disulfide bond	2824 ↔ 2840		By similarity
	Disulfide bond	2845 ↔ 2857		By similarity
	Disulfide bond	2852 ↔ 2871		By similarity
	Disulfide bond	2865 ↔ 2884		By similarity
	Disulfide bond	2891 ↔ 2903		By similarity
	Disulfide bond	2898 ↔ 2916		By similarity
	Disulfide bond	2910 ↔ 2925		By similarity
	Disulfide bond	2930 ↔ 2942		By similarity
	Disulfide bond	2938 ↔ 2951		By similarity
	Disulfide bond	2953 ↔ 2966		By similarity
	Disulfide bond	2972 ↔ 2982		By similarity
	Disulfide bond	2978 ↔ 2991		By similarity
	Disulfide bond	2993 ↔ 3007		By similarity
	Disulfide bond	3317 ↔ 3329		By similarity
	Disulfide bond	3324 ↔ 3342		By similarity
	Disulfide bond	3336 ↔ 3352		By similarity
	Disulfide bond	3357 ↔ 3369		By similarity
	Disulfide bond	3364 ↔ 3382		By similarity
	Disulfide bond	3376 ↔ 3391		By similarity
	Disulfide bond	3396 ↔ 3409		By similarity
	Disulfide bond	3403 ↔ 3422		By similarity
	Disulfide bond	3416 ↔ 3431		By similarity
	Disulfide bond	3436 ↔ 3449		By similarity
	Disulfide bond	3443 ↔ 3462		By similarity
	Disulfide bond	3456 ↔ 3471		By similarity
	Disulfide bond	3476 ↔ 3488		By similarity
	Disulfide bond	3483 ↔ 3501		By similarity
	Disulfide bond	3495 ↔ 3510		By similarity
	Disulfide bond	3515 ↔ 3527		By similarity
	Disulfide bond	3522 ↔ 3540		By similarity
	Disulfide bond	3534 ↔ 3549		By similarity
	Disulfide bond	3553 ↔ 3565		By similarity
	Disulfide bond	3560 ↔ 3578		By similarity
	Disulfide bond	3572 ↔ 3587		By similarity
	Disulfide bond	3594 ↔ 3606		By similarity
	Disulfide bond	3601 ↔ 3619		By similarity
	Disulfide bond	3613 ↔ 3628		By similarity
	Disulfide bond	3632 ↔ 3645		By similarity
	Disulfide bond	3639 ↔ 3658		By similarity
	Disulfide bond	3652 ↔ 3667		By similarity
	Disulfide bond	3674 ↔ 3686		By similarity
	Disulfide bond	3681 ↔ 3699		By similarity
	Disulfide bond	3693 ↔ 3710		By similarity
	Disulfide bond	3715 ↔ 3729		By similarity
	Disulfide bond	3723 ↔ 3742		By similarity
	Disulfide bond	3736 ↔ 3751		By similarity
	Disulfide bond	3762 ↔ 3774		By similarity
	Disulfide bond	3769 ↔ 3787		By similarity
	Disulfide bond	3781 ↔ 3796		By similarity
	Disulfide bond	3805 ↔ 3818		By similarity
	Disulfide bond	3812 ↔ 3827		By similarity
	Disulfide bond	3829 ↔ 3842		By similarity
	Disulfide bond	3848 ↔ 3858		By similarity
	Disulfide bond	3854 ↔ 3867		By similarity
	Disulfide bond	4217 ↔ 4227		By similarity
	Disulfide bond	4221 ↔ 4237		By similarity
	Disulfide bond	4239 ↔ 4248		By similarity
	Disulfide bond	4253 ↔ 4263		By similarity
	Disulfide bond	4257 ↔ 4273		By similarity
	Disulfide bond	4275 ↔ 4284		By similarity
	Disulfide bond	4289 ↔ 4299		By similarity
	Disulfide bond	4293 ↔ 4309		By similarity
	Disulfide bond	4311 ↔ 4320		By similarity
	Disulfide bond	4325 ↔ 4335		By similarity
	Disulfide bond	4329 ↔ 4345		By similarity
	Disulfide bond	4347 ↔ 4356		By similarity
	Disulfide bond	4394 ↔ 4404		By similarity
	Disulfide bond	4398 ↔ 4415		By similarity
	Disulfide bond	4417 ↔ 4426		By similarity
Experimental info
	Sequence conflict	4521 – 4553	33	Missing in BAC29188. Ref.2
	Sequence conflict	4552	1	F → S in BAC28594. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9JI18 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 11462A3354FFB200	FASTA	4,599	513,634
	10 20 30 40 50 60 MSQLLLAILT LSGLLPNAEV LIVGANQDQH LCDPGEFLCH DHVTCVSQSW LCDGDPDCPD 70 80 90 100 110 120 QSDESLDTCP EEVEIKCPLN HIACHGSSAC VHLSKLCNGV VDCPDGFDEG GHCQELLPSC 130 140 150 160 170 180 QQLNCQFKCA MVRNATRCYC EDGFEVAEDG RSCKDQDECS IYGICSQTCK NTYGSYACSC 190 200 210 220 230 240 VEGYIMQSDN RSCKVKHEPT DKAPMLLISS LETIELFYIN GSKMTTLSSA NRNEIHTLDF 250 260 270 280 290 300 IYSEEMICWI ESRESSNQLK CGQITKAGRL TDQRIINSLQ SFQNVEQMAF DWLTRNIYFV 310 320 330 340 350 360 DHVSDRIFVC NFNGSVCVTL IESELHNPKA IAADPIAGKL FFTDYGNVPK IERCDLDGMN 370 380 390 400 410 420 RTRIVYSKAE QPSALALDLV NRLVYWVDLY LDYVGVVDYQ GKNRHTIVQG RQVKHLYGIT 430 440 450 460 470 480 VFEDYLYATS SDNFNIIRIN RFNGTDIHSI IKMESARGIR TYQKRTQPTV RSHACEVDAY 490 500 510 520 530 540 GMPGGCSHIC LLSSSYKTRT CRCRTGFNMG SDGRSCKRPK NELFLFYGKG RPGIVRGMDL 550 560 570 580 590 600 NTKIADECMI PIENLVNPRA LDFHAEANYI YFADTTSFLI GRQKIDGTER ETILKDDLDN 610 620 630 640 650 660 VEGIAVDWIG NNLYWTNDGH RKTINVARLE KASQSRKTLL EGGMSHPRAI VVDPVNGWMY 670 680 690 700 710 720 WTDWKEDKID DSVGRIEKAW MDGVNRQVFV TSKMLWPNGL TLDFHTSTLY WCDAYYDHIE 730 740 750 760 770 780 KVFLNGTHRK VVYSGKELNH PFGLSHHGNY VFWTDYMNGS IFQLDLMTNE VTLLRHERAP 790 800 810 820 830 840 LFGLQIYDPR KQQGDNMCRI NNGGCGTLCL AIPAGRVCAC ADNQLLDENG TTCTFNPEEI 850 860 870 880 890 900 RFHICKPGEF RCKNKHCIQA RWKCDGDDDC LDGSDEDSVT CFNHSCPDDQ FKCQNNRCIP 910 920 930 940 950 960 KRWLCDGAND CGSNEDESNQ TCTARTCQAD QFSCGNGRCI PTAWLCDRED DCGDQTDEVA 970 980 990 1000 1010 1020 SCEFPTCEPL TQFICKSGRC ISNKWHCDTD DDCGDRSDEV GCVHSCLDDQ FRCSSGRCIP 1030 1040 1050 1060 1070 1080 GHWACDGDND CGDFSDETHI NCTKEEARSP AGCIGNEFQC RPDGNCIPDL WRCDGEKDCE 1090 1100 1110 1120 1130 1140 DGSDEKGCNG TIRLCDHKTK FSCRSTGRCI NNAWVCDGDV DCEDQSDEED CDSFLCGPPK 1150 1160 1170 1180 1190 1200 YPCANDTSVC LQPEKLCNGR KDCPDGSDEG DLCDECSLNN GGCSNHCSVV PGRGIVCSCP 1210 1220 1230 1240 1250 1260 EGHQLKKDNR TCEIVDYCAS HLRCSQVCEQ QKHMVKCSCY EGWALGTDGE SCTSVDSFEA 1270 1280 1290 1300 1310 1320 FIIFSIRHEI RRIDLHKGDY SLLVPGLRNT IALDFHFNQS LLYWTDVVED RIYRGKLSES 1330 1340 1350 1360 1370 1380 GGVSAIEVVV EHGLATPEGL TVDWIAGNIY WIDSNLDQIE VSKLDGSLRA TLIAGAMEHP 1390 1400 1410 1420 1430 1440 RAIALDPRYG ILFWTDWDAN FPRIESASMS GAGRKTIYKD MKTGAWPNGL TVDHFERRIV 1450 1460 1470 1480 1490 1500 WTDARSDAIY SAFYDGTNMI EIIRGHEYLS HPFAVSLYGS EVYWTDWRTN TLAKANKWTG 1510 1520 1530 1540 1550 1560 QNVSVIQKTS AQPFDLQIYH PSRQPQAPNP CAANEGRGPC SHLCLINHNR SAACACPHLM 1570 1580 1590 1600 1610 1620 KLSSDKKTCY EMKKFLLYAR RSEIRGVDID NPYVNFITAF TVPDIDDVAV IDFDASEERL 1630 1640 1650 1660 1670 1680 YWTDIKTQTI TRAFINGTGL ETVISRDIQS IRGLAVDWVS RNLYWISSEF DETQINVARL 1690 1700 1710 1720 1730 1740 DGSLKTSIIH GIDKPQCLAA HPVRGKLYWT DGNTINMANM DGSNSKILFQ NQKEPVGLSI 1750 1760 1770 1780 1790 1800 DYVENKLYWI SSGNGTINRC NLDGGNLEVI ESMKEELTKA TALTIMDKKL WWADQNLAQL 1810 1820 1830 1840 1850 1860 GTCNKRDGRN PSILRNKTSG VVHMKVYDKE AQQGSNSCQV NNGGCSQLCL PTSETTRTCM 1870 1880 1890 1900 1910 1920 CTVGYYLQKN RMSCQGIESF LMYSVHEGIR GIPLEPRDKV DALMPISGAA FAVGIDFHAE 1930 1940 1950 1960 1970 1980 NDTIYWTDMG LNKISRAKRD QTWKEDVVTN GLGRVEGIAV DWIAGNIYWT DHGFNLIEVA 1990 2000 2010 2020 2030 2040 RLNGSFRYVI ISQGLDQPRS IAVHPEKGFL FWTEWGQVPC IGKARLDGSE KVMIVSVGIT 2050 2060 2070 2080 2090 2100 WPNGISIDYE ENKLYWCDAR SDKIERIDLD TGANREVLLS GSNVDLFSVA VFGAYIYWSD 2110 2120 2130 2140 2150 2160 RAHANGSVRR GHKNDATETV TMRTGLGVNL KEIKIFNRVR EKGTNVCAKE NGGCQQLCLY 2170 2180 2190 2200 2210 2220 RGNSRRTCAC AHGYLAGDGV TCLRHEGYLL YSGRTILKSI HLSDETNLNS PVRPYENPNY 2230 2240 2250 2260 2270 2280 FKNIIALAFD YNQRREGTNR IFYSDAHFGN IQLIKDNWED RQVIVENVGS VEGLAYHRAW 2290 2300 2310 2320 2330 2340 DTLYWTSSST SSITRHTVDQ TRPGAIDREA VITMSEDDHP HVLALDECQN LMFWTNWNEQ 2350 2360 2370 2380 2390 2400 HPSIMRATLT GKNAHVVVST DILTPNGLTI DHRAEKLYFS DGSLGKIERC EYDGSQRHVI 2410 2420 2430 2440 2450 2460 VKSGPGTFLS LAVYDSYIFW SDWGRRAILR SNKYTGGETK ILRSDIPHQP MGIIAVANDT 2470 2480 2490 2500 2510 2520 NSCELSPCAL LNGGCHDLCL LTPDGRVNCS CRGDRVLLAN NRCVTKNSSC NIYSEFECGN 2530 2540 2550 2560 2570 2580 GDCVDYVLTC DGIPHCKDKS DEKLLYCENR SCRSGFKPCY NRRCVPHGKL CDGTNDCGDS 2590 2600 2610 2620 2630 2640 SDELDCKVST CSTVEFRCAD GTCIPRSARC NQNMDCSDAS DEKGCNNTDC THFYKLGVKS 2650 2660 2670 2680 2690 2700 TGFIRCNSTS LCVLPSWICD GSNDCGDYSD ELKCPVQNKH KCEENYFGCP SGRCILNTWV 2710 2720 2730 2740 2750 2760 CDGQKDCEDG LDELHCDSSC SWNQFACSVK KCISKHWICD GEDDCGDSLD ESDSICGAVT 2770 2780 2790 2800 2810 2820 CAADMFSCQG SHACVPQHWL CDGERDCPDG SDELSSAGCA PNNTCDENAF MCHNKVCIPK 2830 2840 2850 2860 2870 2880 QFVCDHDDDC GDGSDEFLQC GYRQCGPEEF RCADGRCLVN TLWQCDGDFD CPDSSDEAPI 2890 2900 2910 2920 2930 2940 NPRCRSAEHS CNSSFFMCKN GRCIPSDGLC DIRDDCGDGS DETNCHINEC LSKKISGCSQ 2950 2960 2970 2980 2990 3000 DCQDLPVSYK CKCWPGFQLK DDGKTCVDID ECSSGFPCSQ QCINTYGTYK CHCAEGYETQ 3010 3020 3030 3040 3050 3060 PDNPNGCRSL SDEEPFLILA DQHEIRKIST DGSNYTLLKQ GLNNVIALDF DYREEFIYWI 3070 3080 3090 3100 3110 3120 DSSRPNGSRI NRMCLNGSDI KVVHNTAVPN ALAVDWIGKN LYWSDTEKRI IEVSKLNGLY 3130 3140 3150 3160 3170 3180 PTVLVSKRLK FPRDLSLDPR AGNLYWIDCC EYPHIGRVGM DGTNQSVVIE TKISRPMALT 3190 3200 3210 3220 3230 3240 IDYVNHRLYW ADENHIEFSN MDGSHRHKVP NQDIPGVIAL TLFEDYIYWT DGKTKSLSRV 3250 3260 3270 3280 3290 3300 HKTSGADRLS LINSWHAITD IQVYHSYRQP DVSKHLCTVN NGGCSHLCLL GPGKTHTCAC 3310 3320 3330 3340 3350 3360 PTNFYLAADN RTCLSNCTAS QFRCKTDKCI PFWWKCDTVD DCGDGSDEPD DCPEFKCQPG 3370 3380 3390 3400 3410 3420 RFQCGTGLCA LPAFICDGEN DCGDNSDELN CDTHVCLAGQ FKCTKNKKCI PVNLRCNGQD 3430 3440 3450 3460 3470 3480 DCGDEEDEKD CPENSCSPDY FQCKTTKHCI SKLWVCDEDP DCADASDEAN CDKKTCGPHE 3490 3500 3510 3520 3530 3540 FQCKNNNCIP DHWRCDNQND CSDNSDEDNC KPQTCTLKDF LCSNGDCVSS RFWCDGEFDC 3550 3560 3570 3580 3590 3600 ADGSDEKNCE TSCSKDQFQC SNGQCLSAKW KCDGHEDCKY GEDEKNCEPA FPVCSSSEYM 3610 3620 3630 3640 3650 3660 CASGGCLSAS LKCNGEPDCV DGSDEMDCVI ECKEDQFQCK NKAYCIPIRW LCDGIYDCVD 3670 3680 3690 3700 3710 3720 GSDEETCGRG GSICRDDEFL CNNSLCKLHF WVCDGEDDCG DNSDEAPDMC VKFLCPPTRP 3730 3740 3750 3760 3770 3780 YRCRNDRICL QLEKICNGIN DCGDNSDEEH CSGKLSLKSK PCKKDEFTCS NRNCIPMELQ 3790 3800 3810 3820 3830 3840 CDSLDDCGDG SDEQGCLKTP IEHTCENNGN PCGDDAYCNQ IKTSVFCRCK PGFQRNMKGR 3850 3860 3870 3880 3890 3900 ECADLNECLL FGICSHHCLN TRGSYKCVCD QNFQEKNNSC IAKGSEDQAL YIANDTDILG 3910 3920 3930 3940 3950 3960 FVYPFNYSGG HQQISHVEHN SRITGMDVHY QRNVIVWSTQ FNPGGIFYKM IDAREKRQAN 3970 3980 3990 4000 4010 4020 SGLICPEFKR PRDIAVDWVA GNVYWTDHSR MHWFSYYTTH WTSLRYSINV GQLNGPNCTR 4030 4040 4050 4060 4070 4080 LLTNMAGEPY AIAVNPKRGM MYWTVIGDHS HIEEAAMDGT LRRVLVQKNL QRPTGLTVDH 4090 4100 4110 4120 4130 4140 FGERIYWADF ELSIIGSVLY DGSSPVVSVS SKQGLLHPHR IDVFEDYIYG AGPKNGIFRV 4150 4160 4170 4180 4190 4200 QKFGHGSVEV LALGVDKTKS ILVSHRYKQL NLPNPCLDLS CDFLCLLNPS GATCICPEGK 4210 4220 4230 4240 4250 4260 YMMNGTCHDD SLLDDSCKLT CENGGRCILN EKGDLRCHCW PSYSGGRCEV NHCSNYCQNG 4270 4280 4290 4300 4310 4320 GTCIPSTLGR PTCICALGFT GPNCGKAVCE DSCHNGGSCV VTAGNQPYCH CQADYTGDRC 4330 4340 4350 4360 4370 4380 QYYVCHHYCV NSESCTIGND GSVECVCPTR YEGPKCEIDK CVRCHGGHCI INKDNEDIFC 4390 4400 4410 4420 4430 4440 NCTNGKIASS CQLCDGYCYN GGTCQLDPET SIPVCVCSTN WSGTQCERPA PKSSKSEHIS 4450 4460 4470 4480 4490 4500 TRSIAIIVPL VLLVTLVTTL VIGLVVCKRK RRTKTIRRQP IINGGINVEI GNPSYNMYEV 4510 4520 4530 4540 4550 4560 DHDHSDGGLL EPSFMIDPVK SRYIGGGSSA FKLPHTAPPI YLNSDLKGPL TFGPTNYSNP 4570 4580 4590 VYAKLYMDGQ NCRNSLASVD ERKELLPKKI EIGIRETVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure of the mouse homologue of the human candidate tumor suppressor gene LRP1B/LRP-DIT." Yaklichkin S., Lisitsyn N. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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 3770-4599. Strain: C57BL/6J. Tissue: Cerebellum.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF270884 mRNA. Translation: AAF81758.1. AK035795 mRNA. Translation: BAC29188.1. AK034122 mRNA. Translation: BAC28594.1.
IPI	IPI00119787.
UniGene	Mm.441398.
3D structure databases
ProteinModelPortal	Q9JI18.
SMR	Q9JI18. Positions 32-111, 129-833, 845-4205, 4215-4438.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1951413.
STRING	10090.ENSMUSP00000054275.
PTM databases
PhosphoSite	Q9JI18.
Proteomic databases
PaxDb	Q9JI18.
PRIDE	Q9JI18.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:2151136. Lrp1b.
Phylogenomic databases
eggNOG	NOG235850.
HOVERGEN	HBG006292.
InParanoid	Q9JI18.
OrthoDB	EOG42BX7K.
Gene expression databases
Genevestigator	Q9JI18.
GermOnline	ENSMUSG00000049252. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 8 hits. 4.10.400.10. 31 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. 1 hit. PF00008. EGF. 1 hit. PF07645. EGF_CA. 2 hits. PF00057. Ldl_recept_a. 30 hits. PF00058. Ldl_recept_b. 11 hits. [Graphical view]
SMART	SM00181. EGF. 16 hits. SM00179. EGF_CA. 4 hits. SM00192. LDLa. 32 hits. SM00135. LY. 36 hits. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 3 hits. SSF57424. LDL_rcpt_classA_cys-rich. 30 hits.
PROSITE	PS00010. ASX_HYDROXYL. 4 hits. PS00022. EGF_1. 5 hits. PS01186. EGF_2. 9 hits. PS50026. EGF_3. 9 hits. PS01187. EGF_CA. 3 hits. PS01209. LDLRA_1. 27 hits. PS50068. LDLRA_2. 32 hits. PS51120. LDLRB. 36 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LRP1B. mouse.
SOURCE	Search...

Entry information

Entry name

LRP1B_MOUSE

Accession

Primary (citable) accession number: Q9JI18
Secondary accession number(s): Q8BZD3, Q8BZM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program