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Q9JI18

- LRP1B_MOUSE

UniProt

Q9JI18 - LRP1B_MOUSE

Protein

Low-density lipoprotein receptor-related protein 1B

Gene

Lrp1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. low-density lipoprotein particle receptor binding Source: MGI
    3. low-density lipoprotein receptor activity Source: MGI
    4. protein binding Source: IntAct

    GO - Biological processi

    1. receptor-mediated endocytosis Source: GOC

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Lrp1b
    Synonyms:Lrpdit
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2151136. Lrp1b.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: MGI
    3. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 45994579Low-density lipoprotein receptor-related protein 1BPRO_0000017320Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 45By similarity
    Disulfide bondi39 ↔ 58By similarity
    Disulfide bondi52 ↔ 69By similarity
    Disulfide bondi77 ↔ 90By similarity
    Disulfide bondi84 ↔ 103By similarity
    Disulfide bondi97 ↔ 113By similarity
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi159 ↔ 169By similarity
    Disulfide bondi165 ↔ 178By similarity
    Disulfide bondi180 ↔ 193By similarity
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi725 – 7251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi798 ↔ 809By similarity
    Disulfide bondi805 ↔ 818By similarity
    Disulfide bondi820 ↔ 833By similarity
    Glycosylationi829 – 8291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi845 ↔ 857By similarity
    Disulfide bondi852 ↔ 870By similarity
    Disulfide bondi864 ↔ 881By similarity
    Glycosylationi883 – 8831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi886 ↔ 898By similarity
    Disulfide bondi893 ↔ 911By similarity
    Disulfide bondi905 ↔ 922By similarity
    Glycosylationi919 – 9191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi927 ↔ 939By similarity
    Disulfide bondi934 ↔ 952By similarity
    Disulfide bondi946 ↔ 962By similarity
    Disulfide bondi967 ↔ 980By similarity
    Disulfide bondi975 ↔ 993By similarity
    Disulfide bondi987 ↔ 1002By similarity
    Disulfide bondi1006 ↔ 1018By similarity
    Disulfide bondi1013 ↔ 1031By similarity
    Disulfide bondi1025 ↔ 1042By similarity
    Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1053 ↔ 1066By similarity
    Disulfide bondi1060 ↔ 1079By similarity
    Disulfide bondi1073 ↔ 1088By similarity
    Glycosylationi1089 – 10891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1095 ↔ 1109By similarity
    Disulfide bondi1103 ↔ 1122By similarity
    Disulfide bondi1116 ↔ 1131By similarity
    Disulfide bondi1136 ↔ 1150By similarity
    Disulfide bondi1143 ↔ 1163By similarity
    Glycosylationi1145 – 11451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1157 ↔ 1173By similarity
    Disulfide bondi1176 ↔ 1187By similarity
    Disulfide bondi1183 ↔ 1197By similarity
    Disulfide bondi1199 ↔ 1212By similarity
    Glycosylationi1209 – 12091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1298 – 12981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1502 – 15021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1531 ↔ 1544By similarity
    Disulfide bondi1540 ↔ 1554By similarity
    Glycosylationi1549 – 15491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1556 ↔ 1569By similarity
    Glycosylationi1636 – 16361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1754 – 17541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1816 – 18161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1838 ↔ 1849By similarity
    Disulfide bondi1845 ↔ 1859By similarity
    Disulfide bondi1861 ↔ 1874By similarity
    Glycosylationi1921 – 19211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1983 – 19831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2105 – 21051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2147 ↔ 2158By similarity
    Disulfide bondi2154 ↔ 2168By similarity
    Disulfide bondi2170 ↔ 2182By similarity
    Glycosylationi2458 – 24581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2488 – 24881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2507 – 25071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2510 ↔ 2523By similarity
    Disulfide bondi2518 ↔ 2536By similarity
    Disulfide bondi2530 ↔ 2547By similarity
    Glycosylationi2549 – 25491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2552 ↔ 2564By similarity
    Disulfide bondi2559 ↔ 2577By similarity
    Disulfide bondi2571 ↔ 2586By similarity
    Disulfide bondi2591 ↔ 2603By similarity
    Disulfide bondi2598 ↔ 2616By similarity
    Disulfide bondi2610 ↔ 2625By similarity
    Glycosylationi2626 – 26261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2630 ↔ 2652By similarity
    Disulfide bondi2646 ↔ 2665By similarity
    Glycosylationi2647 – 26471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2659 ↔ 2674By similarity
    Disulfide bondi2682 ↔ 2694By similarity
    Disulfide bondi2689 ↔ 2707By similarity
    Disulfide bondi2701 ↔ 2716By similarity
    Disulfide bondi2720 ↔ 2732By similarity
    Disulfide bondi2727 ↔ 2745By similarity
    Disulfide bondi2739 ↔ 2756By similarity
    Disulfide bondi2761 ↔ 2774By similarity
    Disulfide bondi2768 ↔ 2787By similarity
    Disulfide bondi2781 ↔ 2799By similarity
    Glycosylationi2802 – 28021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2805 ↔ 2817By similarity
    Disulfide bondi2812 ↔ 2830By similarity
    Disulfide bondi2824 ↔ 2840By similarity
    Disulfide bondi2845 ↔ 2857By similarity
    Disulfide bondi2852 ↔ 2871By similarity
    Disulfide bondi2865 ↔ 2884By similarity
    Disulfide bondi2891 ↔ 2903By similarity
    Glycosylationi2892 – 28921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2898 ↔ 2916By similarity
    Disulfide bondi2910 ↔ 2925By similarity
    Disulfide bondi2930 ↔ 2942By similarity
    Disulfide bondi2938 ↔ 2951By similarity
    Disulfide bondi2953 ↔ 2966By similarity
    Disulfide bondi2972 ↔ 2982By similarity
    Disulfide bondi2978 ↔ 2991By similarity
    Disulfide bondi2993 ↔ 3007By similarity
    Glycosylationi3034 – 30341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3066 – 30661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3076 – 30761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3164 – 31641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3310 – 33101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3316 – 33161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3317 ↔ 3329By similarity
    Disulfide bondi3324 ↔ 3342By similarity
    Disulfide bondi3336 ↔ 3352By similarity
    Disulfide bondi3357 ↔ 3369By similarity
    Disulfide bondi3364 ↔ 3382By similarity
    Disulfide bondi3376 ↔ 3391By similarity
    Disulfide bondi3396 ↔ 3409By similarity
    Disulfide bondi3403 ↔ 3422By similarity
    Disulfide bondi3416 ↔ 3431By similarity
    Disulfide bondi3436 ↔ 3449By similarity
    Disulfide bondi3443 ↔ 3462By similarity
    Disulfide bondi3456 ↔ 3471By similarity
    Disulfide bondi3476 ↔ 3488By similarity
    Disulfide bondi3483 ↔ 3501By similarity
    Disulfide bondi3495 ↔ 3510By similarity
    Disulfide bondi3515 ↔ 3527By similarity
    Disulfide bondi3522 ↔ 3540By similarity
    Disulfide bondi3534 ↔ 3549By similarity
    Disulfide bondi3553 ↔ 3565By similarity
    Disulfide bondi3560 ↔ 3578By similarity
    Disulfide bondi3572 ↔ 3587By similarity
    Disulfide bondi3594 ↔ 3606By similarity
    Disulfide bondi3601 ↔ 3619By similarity
    Disulfide bondi3613 ↔ 3628By similarity
    Disulfide bondi3632 ↔ 3645By similarity
    Disulfide bondi3639 ↔ 3658By similarity
    Disulfide bondi3652 ↔ 3667By similarity
    Disulfide bondi3674 ↔ 3686By similarity
    Disulfide bondi3681 ↔ 3699By similarity
    Glycosylationi3682 – 36821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3693 ↔ 3710By similarity
    Disulfide bondi3715 ↔ 3729By similarity
    Disulfide bondi3723 ↔ 3742By similarity
    Disulfide bondi3736 ↔ 3751By similarity
    Disulfide bondi3762 ↔ 3774By similarity
    Disulfide bondi3769 ↔ 3787By similarity
    Disulfide bondi3781 ↔ 3796By similarity
    Disulfide bondi3805 ↔ 3818By similarity
    Disulfide bondi3812 ↔ 3827By similarity
    Disulfide bondi3829 ↔ 3842By similarity
    Disulfide bondi3848 ↔ 3858By similarity
    Disulfide bondi3854 ↔ 3867By similarity
    Glycosylationi3877 – 38771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3894 – 38941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3906 – 39061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4017 – 40171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4204 – 42041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4217 ↔ 4227By similarity
    Disulfide bondi4221 ↔ 4237By similarity
    Disulfide bondi4239 ↔ 4248By similarity
    Disulfide bondi4253 ↔ 4263By similarity
    Disulfide bondi4257 ↔ 4273By similarity
    Disulfide bondi4275 ↔ 4284By similarity
    Disulfide bondi4289 ↔ 4299By similarity
    Disulfide bondi4293 ↔ 4309By similarity
    Disulfide bondi4311 ↔ 4320By similarity
    Disulfide bondi4325 ↔ 4335By similarity
    Disulfide bondi4329 ↔ 4345By similarity
    Disulfide bondi4347 ↔ 4356By similarity
    Glycosylationi4381 – 43811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4394 ↔ 4404By similarity
    Disulfide bondi4398 ↔ 4415By similarity
    Disulfide bondi4417 ↔ 4426By similarity
    Glycosylationi4420 – 44201N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9JI18.
    PRIDEiQ9JI18.

    PTM databases

    PhosphoSiteiQ9JI18.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9JI18.

    Interactioni

    Subunit structurei

    Binds LRPAP1, PLAU, PLAT and SERPINE1; binding is followed by internalization and degradation of the ligands.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Mapk8ip1Q9WVI9-13EBI-8294317,EBI-288461
    Pick1Q80VC84EBI-8294317,EBI-8521477
    Ranbp9P695662EBI-8294317,EBI-772305

    Protein-protein interaction databases

    IntActiQ9JI18. 7 interactions.
    MINTiMINT-4998267.
    STRINGi10090.ENSMUSP00000054275.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JI18.
    SMRiQ9JI18. Positions 32-111, 129-833, 845-4430.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 44444424ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini4468 – 4599132CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4445 – 446723HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 7040LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini76 – 11439LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini116 – 15439EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini155 – 19440EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati295 – 33743LDL-receptor class B 1Add
    BLAST
    Repeati338 – 38144LDL-receptor class B 2Add
    BLAST
    Repeati382 – 42544LDL-receptor class B 3Add
    BLAST
    Domaini471 – 51747EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati568 – 61043LDL-receptor class B 4Add
    BLAST
    Repeati611 – 65646LDL-receptor class B 5Add
    BLAST
    Repeati657 – 70650LDL-receptor class B 6Add
    BLAST
    Repeati707 – 75044LDL-receptor class B 7Add
    BLAST
    Domaini794 – 83441EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini844 – 88239LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini885 – 92339LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini926 – 96338LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini966 – 100338LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1005 – 104339LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1052 – 108938LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1094 – 113239LDL-receptor class A 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1135 – 117440LDL-receptor class A 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1174 – 121340EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1214 – 125340EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Repeati1300 – 134647LDL-receptor class B 8Add
    BLAST
    Repeati1347 – 138943LDL-receptor class B 9Add
    BLAST
    Repeati1390 – 143647LDL-receptor class B 10Add
    BLAST
    Repeati1437 – 148044LDL-receptor class B 11Add
    BLAST
    Repeati1481 – 152242LDL-receptor class B 12Add
    BLAST
    Domaini1527 – 157044EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Repeati1618 – 166043LDL-receptor class B 13Add
    BLAST
    Repeati1661 – 170444LDL-receptor class B 14Add
    BLAST
    Repeati1705 – 174440LDL-receptor class B 15Add
    BLAST
    Repeati1745 – 178743LDL-receptor class B 16Add
    BLAST
    Domaini1834 – 187542EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Repeati1922 – 196443LDL-receptor class B 17Add
    BLAST
    Repeati1965 – 200743LDL-receptor class B 28Add
    BLAST
    Repeati2008 – 205144LDL-receptor class B 19Add
    BLAST
    Repeati2052 – 209544LDL-receptor class B 20Add
    BLAST
    Domaini2143 – 218341EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Repeati2239 – 228042LDL-receptor class B 21Add
    BLAST
    Repeati2281 – 232949LDL-receptor class B 22Add
    BLAST
    Repeati2330 – 237445LDL-receptor class B 23Add
    BLAST
    Repeati2375 – 241642LDL-receptor class B 24Add
    BLAST
    Repeati2417 – 245943LDL-receptor class B 25Add
    BLAST
    Domaini2464 – 250441EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2509 – 254840LDL-receptor class A 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2551 – 258737LDL-receptor class A 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini2590 – 262637LDL-receptor class A 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini2629 – 267547LDL-receptor class A 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini2681 – 271737LDL-receptor class A 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2719 – 275739LDL-receptor class A 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2760 – 280041LDL-receptor class A 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2804 – 284138LDL-receptor class A 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2844 – 288542LDL-receptor class A 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2890 – 292637LDL-receptor class A 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2927 – 296741EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2968 – 300841EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati3055 – 309844LDL-receptor class B 26Add
    BLAST
    Repeati3099 – 314143LDL-receptor class B 27Add
    BLAST
    Repeati3142 – 318544LDL-receptor class B 28Add
    BLAST
    Repeati3186 – 322439LDL-receptor class B 29Add
    BLAST
    Repeati3225 – 326844LDL-receptor class B 30Add
    BLAST
    Domaini3273 – 331442EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini3316 – 335338LDL-receptor class A 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini3356 – 339237LDL-receptor class A 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini3395 – 343238LDL-receptor class A 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini3435 – 347238LDL-receptor class A 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini3475 – 351137LDL-receptor class A 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini3514 – 355037LDL-receptor class A 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3552 – 358837LDL-receptor class A 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini3593 – 362937LDL-receptor class A 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini3631 – 366838LDL-receptor class A 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini3673 – 371139LDL-receptor class A 30PROSITE-ProRule annotationAdd
    BLAST
    Domaini3714 – 375239LDL-receptor class A 31PROSITE-ProRule annotationAdd
    BLAST
    Domaini3761 – 379737LDL-receptor class A 32PROSITE-ProRule annotationAdd
    BLAST
    Domaini3801 – 384343EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini3844 – 388138EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Repeati3933 – 398048LDL-receptor class B 31Add
    BLAST
    Repeati3981 – 403858LDL-receptor class B 32Add
    BLAST
    Repeati4039 – 408244LDL-receptor class B 33Add
    BLAST
    Repeati4083 – 412745LDL-receptor class B 34Add
    BLAST
    Domaini4171 – 420838EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini4213 – 424937EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini4249 – 428537EGF-like 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini4285 – 432137EGF-like 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini4321 – 435737EGF-like 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini4357 – 439236EGF-like 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini4390 – 442738EGF-like 22PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4492 – 44954Endocytosis signalSequence Analysis
    Motifi4559 – 45624Endocytosis signalSequence Analysis

    Sequence similaritiesi

    Belongs to the LDLR family.Curated
    Contains 22 EGF-like domains.PROSITE-ProRule annotation
    Contains 32 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG235850.
    HOVERGENiHBG006292.
    InParanoidiQ9JI18.

    Family and domain databases

    Gene3Di2.120.10.30. 8 hits.
    4.10.400.10. 31 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    [Graphical view]
    PfamiPF12662. 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]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 16 hits.
    SM00179. EGF_CA. 4 hits.
    SM00192. LDLa. 32 hits.
    SM00135. LY. 36 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 6 hits.
    SSF57424. SSF57424. 32 hits.
    PROSITEiPS00010. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9JI18-1 [UniParc]FASTAAdd to Basket

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    MSQLLLAILT LSGLLPNAEV LIVGANQDQH LCDPGEFLCH DHVTCVSQSW     50
    LCDGDPDCPD QSDESLDTCP EEVEIKCPLN HIACHGSSAC VHLSKLCNGV 100
    VDCPDGFDEG GHCQELLPSC QQLNCQFKCA MVRNATRCYC EDGFEVAEDG 150
    RSCKDQDECS IYGICSQTCK NTYGSYACSC VEGYIMQSDN RSCKVKHEPT 200
    DKAPMLLISS LETIELFYIN GSKMTTLSSA NRNEIHTLDF IYSEEMICWI 250
    ESRESSNQLK CGQITKAGRL TDQRIINSLQ SFQNVEQMAF DWLTRNIYFV 300
    DHVSDRIFVC NFNGSVCVTL IESELHNPKA IAADPIAGKL FFTDYGNVPK 350
    IERCDLDGMN RTRIVYSKAE QPSALALDLV NRLVYWVDLY LDYVGVVDYQ 400
    GKNRHTIVQG RQVKHLYGIT VFEDYLYATS SDNFNIIRIN RFNGTDIHSI 450
    IKMESARGIR TYQKRTQPTV RSHACEVDAY GMPGGCSHIC LLSSSYKTRT 500
    CRCRTGFNMG SDGRSCKRPK NELFLFYGKG RPGIVRGMDL NTKIADECMI 550
    PIENLVNPRA LDFHAEANYI YFADTTSFLI GRQKIDGTER ETILKDDLDN 600
    VEGIAVDWIG NNLYWTNDGH RKTINVARLE KASQSRKTLL EGGMSHPRAI 650
    VVDPVNGWMY WTDWKEDKID DSVGRIEKAW MDGVNRQVFV TSKMLWPNGL 700
    TLDFHTSTLY WCDAYYDHIE KVFLNGTHRK VVYSGKELNH PFGLSHHGNY 750
    VFWTDYMNGS IFQLDLMTNE VTLLRHERAP LFGLQIYDPR KQQGDNMCRI 800
    NNGGCGTLCL AIPAGRVCAC ADNQLLDENG TTCTFNPEEI RFHICKPGEF 850
    RCKNKHCIQA RWKCDGDDDC LDGSDEDSVT CFNHSCPDDQ FKCQNNRCIP 900
    KRWLCDGAND CGSNEDESNQ TCTARTCQAD QFSCGNGRCI PTAWLCDRED 950
    DCGDQTDEVA SCEFPTCEPL TQFICKSGRC ISNKWHCDTD DDCGDRSDEV 1000
    GCVHSCLDDQ FRCSSGRCIP GHWACDGDND CGDFSDETHI NCTKEEARSP 1050
    AGCIGNEFQC RPDGNCIPDL WRCDGEKDCE DGSDEKGCNG TIRLCDHKTK 1100
    FSCRSTGRCI NNAWVCDGDV DCEDQSDEED CDSFLCGPPK YPCANDTSVC 1150
    LQPEKLCNGR KDCPDGSDEG DLCDECSLNN GGCSNHCSVV PGRGIVCSCP 1200
    EGHQLKKDNR TCEIVDYCAS HLRCSQVCEQ QKHMVKCSCY EGWALGTDGE 1250
    SCTSVDSFEA FIIFSIRHEI RRIDLHKGDY SLLVPGLRNT IALDFHFNQS 1300
    LLYWTDVVED RIYRGKLSES GGVSAIEVVV EHGLATPEGL TVDWIAGNIY 1350
    WIDSNLDQIE VSKLDGSLRA TLIAGAMEHP RAIALDPRYG ILFWTDWDAN 1400
    FPRIESASMS GAGRKTIYKD MKTGAWPNGL TVDHFERRIV WTDARSDAIY 1450
    SAFYDGTNMI EIIRGHEYLS HPFAVSLYGS EVYWTDWRTN TLAKANKWTG 1500
    QNVSVIQKTS AQPFDLQIYH PSRQPQAPNP CAANEGRGPC SHLCLINHNR 1550
    SAACACPHLM KLSSDKKTCY EMKKFLLYAR RSEIRGVDID NPYVNFITAF 1600
    TVPDIDDVAV IDFDASEERL YWTDIKTQTI TRAFINGTGL ETVISRDIQS 1650
    IRGLAVDWVS RNLYWISSEF DETQINVARL DGSLKTSIIH GIDKPQCLAA 1700
    HPVRGKLYWT DGNTINMANM DGSNSKILFQ NQKEPVGLSI DYVENKLYWI 1750
    SSGNGTINRC NLDGGNLEVI ESMKEELTKA TALTIMDKKL WWADQNLAQL 1800
    GTCNKRDGRN PSILRNKTSG VVHMKVYDKE AQQGSNSCQV NNGGCSQLCL 1850
    PTSETTRTCM CTVGYYLQKN RMSCQGIESF LMYSVHEGIR GIPLEPRDKV 1900
    DALMPISGAA FAVGIDFHAE NDTIYWTDMG LNKISRAKRD QTWKEDVVTN 1950
    GLGRVEGIAV DWIAGNIYWT DHGFNLIEVA RLNGSFRYVI ISQGLDQPRS 2000
    IAVHPEKGFL FWTEWGQVPC IGKARLDGSE KVMIVSVGIT WPNGISIDYE 2050
    ENKLYWCDAR SDKIERIDLD TGANREVLLS GSNVDLFSVA VFGAYIYWSD 2100
    RAHANGSVRR GHKNDATETV TMRTGLGVNL KEIKIFNRVR EKGTNVCAKE 2150
    NGGCQQLCLY RGNSRRTCAC AHGYLAGDGV TCLRHEGYLL YSGRTILKSI 2200
    HLSDETNLNS PVRPYENPNY FKNIIALAFD YNQRREGTNR IFYSDAHFGN 2250
    IQLIKDNWED RQVIVENVGS VEGLAYHRAW DTLYWTSSST SSITRHTVDQ 2300
    TRPGAIDREA VITMSEDDHP HVLALDECQN LMFWTNWNEQ HPSIMRATLT 2350
    GKNAHVVVST DILTPNGLTI DHRAEKLYFS DGSLGKIERC EYDGSQRHVI 2400
    VKSGPGTFLS LAVYDSYIFW SDWGRRAILR SNKYTGGETK ILRSDIPHQP 2450
    MGIIAVANDT NSCELSPCAL LNGGCHDLCL LTPDGRVNCS CRGDRVLLAN 2500
    NRCVTKNSSC NIYSEFECGN GDCVDYVLTC DGIPHCKDKS DEKLLYCENR 2550
    SCRSGFKPCY NRRCVPHGKL CDGTNDCGDS SDELDCKVST CSTVEFRCAD 2600
    GTCIPRSARC NQNMDCSDAS DEKGCNNTDC THFYKLGVKS TGFIRCNSTS 2650
    LCVLPSWICD GSNDCGDYSD ELKCPVQNKH KCEENYFGCP SGRCILNTWV 2700
    CDGQKDCEDG LDELHCDSSC SWNQFACSVK KCISKHWICD GEDDCGDSLD 2750
    ESDSICGAVT CAADMFSCQG SHACVPQHWL CDGERDCPDG SDELSSAGCA 2800
    PNNTCDENAF MCHNKVCIPK QFVCDHDDDC GDGSDEFLQC GYRQCGPEEF 2850
    RCADGRCLVN TLWQCDGDFD CPDSSDEAPI NPRCRSAEHS CNSSFFMCKN 2900
    GRCIPSDGLC DIRDDCGDGS DETNCHINEC LSKKISGCSQ DCQDLPVSYK 2950
    CKCWPGFQLK DDGKTCVDID ECSSGFPCSQ QCINTYGTYK CHCAEGYETQ 3000
    PDNPNGCRSL SDEEPFLILA DQHEIRKIST DGSNYTLLKQ GLNNVIALDF 3050
    DYREEFIYWI DSSRPNGSRI NRMCLNGSDI KVVHNTAVPN ALAVDWIGKN 3100
    LYWSDTEKRI IEVSKLNGLY PTVLVSKRLK FPRDLSLDPR AGNLYWIDCC 3150
    EYPHIGRVGM DGTNQSVVIE TKISRPMALT IDYVNHRLYW ADENHIEFSN 3200
    MDGSHRHKVP NQDIPGVIAL TLFEDYIYWT DGKTKSLSRV HKTSGADRLS 3250
    LINSWHAITD IQVYHSYRQP DVSKHLCTVN NGGCSHLCLL GPGKTHTCAC 3300
    PTNFYLAADN RTCLSNCTAS QFRCKTDKCI PFWWKCDTVD DCGDGSDEPD 3350
    DCPEFKCQPG RFQCGTGLCA LPAFICDGEN DCGDNSDELN CDTHVCLAGQ 3400
    FKCTKNKKCI PVNLRCNGQD DCGDEEDEKD CPENSCSPDY FQCKTTKHCI 3450
    SKLWVCDEDP DCADASDEAN CDKKTCGPHE FQCKNNNCIP DHWRCDNQND 3500
    CSDNSDEDNC KPQTCTLKDF LCSNGDCVSS RFWCDGEFDC ADGSDEKNCE 3550
    TSCSKDQFQC SNGQCLSAKW KCDGHEDCKY GEDEKNCEPA FPVCSSSEYM 3600
    CASGGCLSAS LKCNGEPDCV DGSDEMDCVI ECKEDQFQCK NKAYCIPIRW 3650
    LCDGIYDCVD GSDEETCGRG GSICRDDEFL CNNSLCKLHF WVCDGEDDCG 3700
    DNSDEAPDMC VKFLCPPTRP YRCRNDRICL QLEKICNGIN DCGDNSDEEH 3750
    CSGKLSLKSK PCKKDEFTCS NRNCIPMELQ CDSLDDCGDG SDEQGCLKTP 3800
    IEHTCENNGN PCGDDAYCNQ IKTSVFCRCK PGFQRNMKGR ECADLNECLL 3850
    FGICSHHCLN TRGSYKCVCD QNFQEKNNSC IAKGSEDQAL YIANDTDILG 3900
    FVYPFNYSGG HQQISHVEHN SRITGMDVHY QRNVIVWSTQ FNPGGIFYKM 3950
    IDAREKRQAN SGLICPEFKR PRDIAVDWVA GNVYWTDHSR MHWFSYYTTH 4000
    WTSLRYSINV GQLNGPNCTR LLTNMAGEPY AIAVNPKRGM MYWTVIGDHS 4050
    HIEEAAMDGT LRRVLVQKNL QRPTGLTVDH FGERIYWADF ELSIIGSVLY 4100
    DGSSPVVSVS SKQGLLHPHR IDVFEDYIYG AGPKNGIFRV QKFGHGSVEV 4150
    LALGVDKTKS ILVSHRYKQL NLPNPCLDLS CDFLCLLNPS GATCICPEGK 4200
    YMMNGTCHDD SLLDDSCKLT CENGGRCILN EKGDLRCHCW PSYSGGRCEV 4250
    NHCSNYCQNG GTCIPSTLGR PTCICALGFT GPNCGKAVCE DSCHNGGSCV 4300
    VTAGNQPYCH CQADYTGDRC QYYVCHHYCV NSESCTIGND GSVECVCPTR 4350
    YEGPKCEIDK CVRCHGGHCI INKDNEDIFC NCTNGKIASS CQLCDGYCYN 4400
    GGTCQLDPET SIPVCVCSTN WSGTQCERPA PKSSKSEHIS TRSIAIIVPL 4450
    VLLVTLVTTL VIGLVVCKRK RRTKTIRRQP IINGGINVEI GNPSYNMYEV 4500
    DHDHSDGGLL EPSFMIDPVK SRYIGGGSSA FKLPHTAPPI YLNSDLKGPL 4550
    TFGPTNYSNP VYAKLYMDGQ NCRNSLASVD ERKELLPKKI EIGIRETVA 4599
    Length:4,599
    Mass (Da):513,634
    Last modified:October 1, 2000 - v1
    Checksum:i11462A3354FFB200
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4521 – 455333Missing in BAC29188. (PubMed:16141072)CuratedAdd
    BLAST
    Sequence conflicti4552 – 45521F → S in BAC28594. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF270884 mRNA. Translation: AAF81758.1.
    AK035795 mRNA. Translation: BAC29188.1.
    AK034122 mRNA. Translation: BAC28594.1.
    UniGeneiMm.441398.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF270884 mRNA. Translation: AAF81758.1 .
    AK035795 mRNA. Translation: BAC29188.1 .
    AK034122 mRNA. Translation: BAC28594.1 .
    UniGenei Mm.441398.

    3D structure databases

    ProteinModelPortali Q9JI18.
    SMRi Q9JI18. Positions 32-111, 129-833, 845-4430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JI18. 7 interactions.
    MINTi MINT-4998267.
    STRINGi 10090.ENSMUSP00000054275.

    PTM databases

    PhosphoSitei Q9JI18.

    Proteomic databases

    PaxDbi Q9JI18.
    PRIDEi Q9JI18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:2151136. Lrp1b.

    Phylogenomic databases

    eggNOGi NOG235850.
    HOVERGENi HBG006292.
    InParanoidi Q9JI18.

    Miscellaneous databases

    ChiTaRSi LRP1B. mouse.
    PROi Q9JI18.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q9JI18.

    Family and domain databases

    Gene3Di 2.120.10.30. 8 hits.
    4.10.400.10. 31 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    [Graphical view ]
    Pfami 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 ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 16 hits.
    SM00179. EGF_CA. 4 hits.
    SM00192. LDLa. 32 hits.
    SM00135. LY. 36 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 6 hits.
    SSF57424. SSF57424. 32 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiLRP1B_MOUSE
    AccessioniPrimary (citable) accession number: Q9JI18
    Secondary accession number(s): Q8BZD3, Q8BZM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3