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Protein

Low-density lipoprotein receptor-related protein 2

Gene

Lrp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts together with cubilin to mediate HDL endocytosis.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1206Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1209CalciumBy similarity1
Metal bindingi1211Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1213CalciumBy similarity1
Metal bindingi1219CalciumBy similarity1
Metal bindingi1220CalciumBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • receptor activity Source: MGI

GO - Biological processi

  • aorta development Source: MGI
  • cell proliferation Source: MGI
  • coronary vasculature development Source: MGI
  • forebrain development Source: MGI
  • heart development Source: MGI
  • receptor-mediated endocytosis Source: MGI
  • ventricular septum development Source: MGI
  • vitamin metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-196791. Vitamin D (calciferol) metabolism.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-975634. Retinoid metabolism and transport.

Protein family/group databases

TCDBi9.B.87.1.1. the selenoprotein p receptor (selp-receptor) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name:
LRP-2
Alternative name(s):
Glycoprotein 330
Short name:
gp330
Megalin
Gene namesi
Name:Lrp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95794. Lrp2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 4425ExtracellularSequence analysisAdd BLAST4400
Transmembranei4426 – 4446HelicalSequence analysisAdd BLAST21
Topological domaini4447 – 4660CytoplasmicSequence analysisAdd BLAST214

GO - Cellular componenti

  • apical part of cell Source: MGI
  • apical plasma membrane Source: UniProtKB
  • brush border Source: MGI
  • brush border membrane Source: MGI
  • clathrin-coated pit Source: MGI
  • endocytic vesicle Source: MGI
  • endoplasmic reticulum Source: MGI
  • endosome Source: MGI
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: MGI
  • membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000030984526 – 4660Low-density lipoprotein receptor-related protein 2Add BLAST4635

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 40By similarity
Disulfide bondi35 ↔ 53By similarity
Disulfide bondi47 ↔ 62By similarity
Disulfide bondi67 ↔ 80By similarity
Disulfide bondi74 ↔ 93By similarity
Disulfide bondi87 ↔ 103By similarity
Disulfide bondi108 ↔ 120By similarity
Disulfide bondi115 ↔ 133By similarity
Disulfide bondi127 ↔ 142By similarity
Disulfide bondi147 ↔ 157By similarity
Disulfide bondi152 ↔ 170By similarity
Glycosylationi159N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi164 ↔ 179By similarity
Glycosylationi178N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi183 ↔ 195By similarity
Disulfide bondi190 ↔ 208By similarity
Disulfide bondi202 ↔ 217By similarity
Disulfide bondi222 ↔ 234By similarity
Disulfide bondi229 ↔ 247By similarity
Disulfide bondi241 ↔ 256By similarity
Disulfide bondi265 ↔ 278By similarity
Disulfide bondi272 ↔ 291By similarity
Disulfide bondi285 ↔ 306By similarity
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi311 ↔ 320By similarity
Disulfide bondi316 ↔ 329By similarity
Disulfide bondi331 ↔ 345By similarity
Glycosylationi340N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi351 ↔ 361By similarity
Disulfide bondi357 ↔ 370By similarity
Disulfide bondi372 ↔ 384By similarity
Glycosylationi387N-linked (GlcNAc...)1 Publication1
Glycosylationi399N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi462N-linked (GlcNAc...)Sequence analysis1
Glycosylationi657N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi662 ↔ 673By similarity
Disulfide bondi669 ↔ 688By similarity
Disulfide bondi690 ↔ 703By similarity
Glycosylationi865N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi973 ↔ 987By similarity
Disulfide bondi983 ↔ 997By similarity
Disulfide bondi999 ↔ 1012By similarity
Disulfide bondi1025 ↔ 1037By similarity
Disulfide bondi1032 ↔ 1050By similarity
Disulfide bondi1044 ↔ 1059By similarity
Glycosylationi1063N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1066 ↔ 1079By similarity
Disulfide bondi1073 ↔ 1092By similarity
Disulfide bondi1086 ↔ 1101By similarity
Disulfide bondi1110 ↔ 1122By similarity
Disulfide bondi1117 ↔ 1135By similarity
Disulfide bondi1129 ↔ 1144By similarity
Disulfide bondi1150 ↔ 1162By similarity
Disulfide bondi1157 ↔ 1175By similarity
Disulfide bondi1169 ↔ 1184By similarity
Glycosylationi1187N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1188 ↔ 1201By similarity
Disulfide bondi1195 ↔ 1214By similarity
Disulfide bondi1208 ↔ 1223By similarity
Disulfide bondi1231 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1257By similarity
Disulfide bondi1251 ↔ 1267By similarity
Disulfide bondi1272 ↔ 1284By similarity
Disulfide bondi1279 ↔ 1297By similarity
Disulfide bondi1291 ↔ 1306By similarity
Disulfide bondi1313 ↔ 1326By similarity
Disulfide bondi1320 ↔ 1339By similarity
Glycosylationi1328N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1333 ↔ 1349By similarity
Glycosylationi1341N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1354 ↔ 1365By similarity
Disulfide bondi1361 ↔ 1374By similarity
Disulfide bondi1376 ↔ 1389By similarity
Glycosylationi1384N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1395 ↔ 1405By similarity
Disulfide bondi1401 ↔ 1414By similarity
Disulfide bondi1416 ↔ 1429By similarity
Glycosylationi1451N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1497N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1551N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1676N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1705 ↔ 1714By similarity
Disulfide bondi1710 ↔ 1726By similarity
Disulfide bondi1728 ↔ 1741By similarity
Glycosylationi1733N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1811N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2023 ↔ 2034By similarity
Disulfide bondi2030 ↔ 2044By similarity
Disulfide bondi2046 ↔ 2059By similarity
Glycosylationi2131N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2134N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2178N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2225N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2347 ↔ 2358By similarity
Disulfide bondi2354 ↔ 2369By similarity
Disulfide bondi2371 ↔ 2383By similarity
Glycosylationi2396N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2488N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2548N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2656 ↔ 2667By similarity
Disulfide bondi2663 ↔ 2676By similarity
Disulfide bondi2678 ↔ 2693By similarity
Disulfide bondi2701 ↔ 2713By similarity
Disulfide bondi2708 ↔ 2726By similarity
Disulfide bondi2720 ↔ 2737By similarity
Disulfide bondi2742 ↔ 2754By similarity
Disulfide bondi2749 ↔ 2767By similarity
Disulfide bondi2761 ↔ 2776By similarity
Disulfide bondi2781 ↔ 2794By similarity
Glycosylationi2782N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2789 ↔ 2807By similarity
Disulfide bondi2801 ↔ 2818By similarity
Glycosylationi2810N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2823 ↔ 2836By similarity
Disulfide bondi2830 ↔ 2849By similarity
Disulfide bondi2843 ↔ 2860By similarity
Disulfide bondi2865 ↔ 2878By similarity
Disulfide bondi2872 ↔ 2891By similarity
Disulfide bondi2885 ↔ 2901By similarity
Disulfide bondi2908 ↔ 2920By similarity
Disulfide bondi2915 ↔ 2933By similarity
Disulfide bondi2927 ↔ 2945By similarity
Glycosylationi2949N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2950 ↔ 2967By similarity
Disulfide bondi2957 ↔ 2980By similarity
Disulfide bondi2974 ↔ 2990By similarity
Glycosylationi2989N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2995 ↔ 3007By similarity
Disulfide bondi3002 ↔ 3020By similarity
Disulfide bondi3014 ↔ 3029By similarity
Disulfide bondi3034 ↔ 3046By similarity
Disulfide bondi3041 ↔ 3059By similarity
Disulfide bondi3053 ↔ 3070By similarity
Disulfide bondi3077 ↔ 3089By similarity
Disulfide bondi3084 ↔ 3102By similarity
Disulfide bondi3096 ↔ 3111By similarity
Disulfide bondi3116 ↔ 3128By similarity
Disulfide bondi3124 ↔ 3137By similarity
Glycosylationi3127N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3139 ↔ 3152By similarity
Disulfide bondi3158 ↔ 3169By similarity
Disulfide bondi3165 ↔ 3178By similarity
Disulfide bondi3180 ↔ 3193By similarity
Glycosylationi3213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3259N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3317N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3357N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3448N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3471 ↔ 3482By similarity
Disulfide bondi3478 ↔ 3493By similarity
Disulfide bondi3495 ↔ 3510By similarity
Disulfide bondi3514 ↔ 3527By similarity
Disulfide bondi3521 ↔ 3540By similarity
Disulfide bondi3534 ↔ 3550By similarity
Disulfide bondi3555 ↔ 3567By similarity
Disulfide bondi3562 ↔ 3580By similarity
Glycosylationi3566N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3574 ↔ 3591By similarity
Disulfide bondi3596 ↔ 3608By similarity
Disulfide bondi3603 ↔ 3621By similarity
Disulfide bondi3615 ↔ 3632By similarity
Disulfide bondi3637 ↔ 3649By similarity
Disulfide bondi3644 ↔ 3662By similarity
Disulfide bondi3656 ↔ 3673By similarity
Disulfide bondi3680 ↔ 3694By similarity
Glycosylationi3682N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3688 ↔ 3707By similarity
Disulfide bondi3701 ↔ 3716By similarity
Disulfide bondi3721 ↔ 3734By similarity
Disulfide bondi3729 ↔ 3747By similarity
Disulfide bondi3741 ↔ 3756By similarity
Disulfide bondi3761 ↔ 3773By similarity
Disulfide bondi3768 ↔ 3786By similarity
Disulfide bondi3780 ↔ 3795By similarity
Disulfide bondi3800 ↔ 3812By similarity
Disulfide bondi3807 ↔ 3825By similarity
Disulfide bondi3819 ↔ 3834By similarity
Glycosylationi3840N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3844 ↔ 3856By similarity
Disulfide bondi3851 ↔ 3869By similarity
Disulfide bondi3863 ↔ 3880By similarity
Disulfide bondi3885 ↔ 3898By similarity
Disulfide bondi3893 ↔ 3911By similarity
Disulfide bondi3905 ↔ 3922By similarity
Disulfide bondi3930 ↔ 3942By similarity
Disulfide bondi3937 ↔ 3955By similarity
Disulfide bondi3949 ↔ 3964By similarity
Glycosylationi3969N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3972 ↔ 3981By similarity
Disulfide bondi3977 ↔ 3991By similarity
Glycosylationi3980N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3993 ↔ 4007By similarity
Disulfide bondi4013 ↔ 4023By similarity
Disulfide bondi4019 ↔ 4032By similarity
Disulfide bondi4034 ↔ 4049By similarity
Glycosylationi4070N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4329N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4336 ↔ 4344By similarity
Disulfide bondi4340 ↔ 4353By similarity
Disulfide bondi4355 ↔ 4369By similarity
Disulfide bondi4383 ↔ 4391By similarity
Disulfide bondi4385 ↔ 4401By similarity
Disulfide bondi4403 ↔ 4412By similarity
Modified residuei4464PhosphoserineCombined sources1
Modified residuei4467PhosphoserineCombined sources1
Modified residuei4577PhosphoserineCombined sources1
Modified residuei4624PhosphoserineBy similarity1
Modified residuei4637PhosphothreonineCombined sources1
Modified residuei4658PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiA2ARV4.
PaxDbiA2ARV4.
PeptideAtlasiA2ARV4.
PRIDEiA2ARV4.

PTM databases

iPTMnetiA2ARV4.
PhosphoSitePlusiA2ARV4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027070.
ExpressionAtlasiA2ARV4. baseline and differential.
GenevisibleiA2ARV4. MM.

Interactioni

Subunit structurei

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 LRPAP1 (By similarity). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By similarity). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif (PubMed:11247302).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab1P973182EBI-300875,EBI-81680
Dlg4Q621082EBI-300875,EBI-300895
Gipc1Q9Z0G02EBI-300875,EBI-300855
Mapk8ip1Q9WVI92EBI-300875,EBI-74515
Mapk8ip2Q9ERE92EBI-300875,EBI-74576
Synj2bpQ9D6K52EBI-300875,EBI-300910

Protein-protein interaction databases

BioGridi200005. 4 interactors.
IntActiA2ARV4. 11 interactors.
MINTiMINT-4106203.
STRINGi10090.ENSMUSP00000079752.

Structurei

3D structure databases

ProteinModelPortaliA2ARV4.
SMRiA2ARV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 64LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST39
Domaini65 – 105LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini106 – 144LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini145 – 181LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST37
Domaini181 – 219LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST39
Domaini220 – 258LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST39
Domaini263 – 307LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST45
Domaini308 – 346EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini347 – 385EGF-like 2PROSITE-ProRule annotationAdd BLAST39
Repeati435 – 477LDL-receptor class B 1Add BLAST43
Repeati478 – 520LDL-receptor class B 2Add BLAST43
Repeati521 – 567LDL-receptor class B 3Add BLAST47
Repeati568 – 611LDL-receptor class B 4Add BLAST44
Repeati612 – 652LDL-receptor class B 5Add BLAST41
Domaini658 – 704EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Repeati752 – 794LDL-receptor class B 6Add BLAST43
Repeati795 – 836LDL-receptor class B 7Add BLAST42
Repeati837 – 880LDL-receptor class B 8Add BLAST44
Repeati881 – 924LDL-receptor class B 9Add BLAST44
Domaini969 – 1013EGF-like 4PROSITE-ProRule annotationAdd BLAST45
Domaini1023 – 1061LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST39
Domaini1064 – 1103LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST40
Domaini1108 – 1146LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST39
Domaini1148 – 1186LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST39
Domaini1186 – 1225LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST40
Domaini1229 – 1269LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST41
Domaini1270 – 1308LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST39
Domaini1311 – 1351LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST41
Domaini1350 – 1390EGF-like 5PROSITE-ProRule annotationAdd BLAST41
Domaini1391 – 1430EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati1479 – 1521LDL-receptor class B 10Add BLAST43
Repeati1522 – 1564LDL-receptor class B 11Add BLAST43
Repeati1567 – 1610LDL-receptor class B 12Add BLAST44
Repeati1611 – 1654LDL-receptor class B 13Add BLAST44
Repeati1655 – 1696LDL-receptor class B 14Add BLAST42
Domaini1701 – 1742EGF-like 7PROSITE-ProRule annotationAdd BLAST42
Repeati1791 – 1833LDL-receptor class B 15Add BLAST43
Repeati1834 – 1883LDL-receptor class B 16Add BLAST50
Repeati1884 – 1931LDL-receptor class B 17Add BLAST48
Repeati1932 – 1972LDL-receptor class B 18Add BLAST41
Repeati1973 – 2014LDL-receptor class B 19Add BLAST42
Domaini2019 – 2060EGF-like 8PROSITE-ProRule annotationAdd BLAST42
Repeati2108 – 2157LDL-receptor class B 20Add BLAST50
Repeati2158 – 2202LDL-receptor class B 21Add BLAST45
Repeati2203 – 2246LDL-receptor class B 22Add BLAST44
Repeati2247 – 2290LDL-receptor class B 23Add BLAST44
Repeati2291 – 2332LDL-receptor class B 24Add BLAST42
Domaini2343 – 2384EGF-like 9PROSITE-ProRule annotationAdd BLAST42
Repeati2433 – 2478LDL-receptor class B 25Add BLAST46
Repeati2479 – 2519LDL-receptor class B 26Add BLAST41
Repeati2520 – 2563LDL-receptor class B 27Add BLAST44
Repeati2564 – 2604LDL-receptor class B 28Add BLAST41
Repeati2605 – 2647LDL-receptor class B 29Add BLAST43
Domaini2652 – 2694EGF-like 10PROSITE-ProRule annotationAdd BLAST43
Domaini2699 – 2739LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST41
Domaini2740 – 2778LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST39
Domaini2779 – 2820LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST42
Domaini2821 – 2862LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST42
Domaini2863 – 2903LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST41
Domaini2906 – 2947LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST42
Domaini2948 – 2992LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST45
Domaini2993 – 3031LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST39
Domaini3032 – 3072LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST41
Domaini3075 – 3112LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST38
Domaini3113 – 3153EGF-like 11PROSITE-ProRule annotationAdd BLAST41
Domaini3154 – 3194EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3241 – 3283LDL-receptor class B 30Add BLAST43
Repeati3284 – 3326LDL-receptor class B 31Add BLAST43
Repeati3335 – 3378LDL-receptor class B 32Add BLAST44
Repeati3379 – 3420LDL-receptor class B 33Add BLAST42
Repeati3421 – 3462LDL-receptor class B 34Add BLAST42
Domaini3467 – 3511EGF-like 13PROSITE-ProRule annotationAdd BLAST45
Domaini3512 – 3552LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST41
Domaini3553 – 3593LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST41
Domaini3594 – 3634LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST41
Domaini3635 – 3675LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST41
Domaini3678 – 3718LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST41
Domaini3719 – 3758LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST40
Domaini3759 – 3797LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST39
Domaini3798 – 3836LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST39
Domaini3842 – 3882LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST41
Domaini3883 – 3924LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST42
Domaini3928 – 3966LDL-receptor class A 36PROSITE-ProRule annotationAdd BLAST39
Domaini3968 – 4008EGF-like 14PROSITE-ProRule annotationAdd BLAST41
Domaini4009 – 4050EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Repeati4156 – 4198LDL-receptor class B 35Add BLAST43
Repeati4199 – 4242LDL-receptor class B 36Add BLAST44
Repeati4244 – 4285LDL-receptor class B 37Add BLAST42
Domaini4332 – 4370EGF-like 16PROSITE-ProRule annotationAdd BLAST39
Domaini4379 – 4413EGF-like 17PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4597 – 4610Interaction with DAB2By similarityAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1743 – 1745Cell attachment siteSequence analysis3
Motifi4454 – 4463SH3-bindingSequence analysis10
Motifi4457 – 4462PxLPxI/L motif 1; mediates interaction with ANKRA2By similarity6
Motifi4460 – 4465PxLPxI/L motif 2; mediates interaction with ANKRA2By similarity6
Motifi4522 – 4527Endocytosis signalSequence analysis6
Motifi4601 – 4606NPXY motif6
Motifi4606 – 4609SH2-bindingSequence analysis4
Motifi4619 – 4630SH3-bindingSequence analysisAdd BLAST12

Domaini

Two overlapping PxLPxI/L motifs mediate interaction with ankyrin repeats of ANKRA2.By similarity

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 17 EGF-like domains.PROSITE-ProRule annotation
Contains 36 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 37 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG097941.
InParanoidiA2ARV4.
KOiK06233.
OMAiTRPPGMC.
OrthoDBiEOG091G000N.
PhylomeDBiA2ARV4.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
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]
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 17 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 25 hits.
SM00179. EGF_CA. 9 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 37 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 35 hits.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

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

A2ARV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGAAAAAW MLLLAIAACL APVSGQECGS GNFRCDNGYC IPASWRCDGT
60 70 80 90 100
RDCLDDTDEI GCPPRSCGSG FFLCPAEGTC IPSSWVCDQD KDCSDGADEQ
110 120 130 140 150
QNCPGTTCSS QQLTCSNGQC VPIEYRCDHV SDCPDGSDER NCYYPTCDQL
160 170 180 190 200
TCANGACYNT SQKCDHKVDC RDSSDEANCT TLCSQKEFQC GSGECILRAY
210 220 230 240 250
VCDHDNDCED NSDEHNCNYD TCGGHQFTCS NGQCINQNWV CDGDDDCQDS
260 270 280 290 300
GDEDGCESNQ RHHTCYPREW ACPGSGRCIS MDKVCDGVPD CPEGEDENNA
310 320 330 340 350
TSGRYCGTGL CSILNCEYQC HQTPYGGECF CPPGHIINSN DSRTCIDFDD
360 370 380 390 400
CQIWGICDQK CESRQGRHQC LCEEGYILER GQHCKSNDSF SAASIIFSNG
410 420 430 440 450
RDLLVGDLHG RNFRILAESK NRGIVMGVDF HYQKHRVFWT DPMQAKVFST
460 470 480 490 500
DINGLNTQEI LNVSIDAPEN LAVDWINNKL YLVETRVNRI DVVNLEGNQR
510 520 530 540 550
VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA FMDGSNRKDL
560 570 580 590 600
VTTKLGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
610 620 630 640 650
PHPFGISLFE EHVFFTDWTK MAVMKANKFT DTNPQVYHQS SLTPFGVTVY
660 670 680 690 700
HALRQPNATN PCGNNNGGCA QICVLSHRTD NGGLGYRCKC EFGFELDADE
710 720 730 740 750
HHCVAVKNFL LFSSQTAVRG IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ
760 770 780 790 800
HSTIFYSDLS KNIIYQQKID GTGKEVITAN RLQNVECLSF DWISRNLYWT
810 820 830 840 850
DGGSKSVTVM KLADKSRRQI ISNLNNPRSI VVHPAAGYMF LSDWFRPAKI
860 870 880 890 900
MRAWSDGSHL MPIVNTSLGW PNGLAIDWST SRLYWVDAFF DKIEHSNLDG
910 920 930 940 950
LDRKRLGHVD QMTHPFGLTV FKDNVFLTDW RLGAIIRVRK SDGGDMTVVR
960 970 980 990 1000
RGISSIMHVK AYDADLQTGT NYCSQTTHPN GDCSHFCFPV PNFQRVCGCP
1010 1020 1030 1040 1050
YGMKLQRDQM TCEGDPAREP PTQQCGSSSF PCNNGKCVPS IFRCDGVDDC
1060 1070 1080 1090 1100
HDNSDEHQCG ALNNTCSSSA FTCVHGGQCI PGQWRCDKQN DCLDGSDEQN
1110 1120 1130 1140 1150
CPTRSPSSTC PPTSFTCDNH MCIPKEWVCD TDNDCSDGSD EKNCQASGTC
1160 1170 1180 1190 1200
HPTQFRCPDH RCISPLYVCD GDKDCVDGSD EAGCVLNCTS SQFKCADGSS
1210 1220 1230 1240 1250
CINSRYRCDG VYDCKDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE
1260 1270 1280 1290 1300
CDGHPDCIQG SDEHNGCVPK TCSPSHFLCD NGNCIYNSWV CDGDNDCRDM
1310 1320 1330 1340 1350
SDEKDCPTQP FHCPSSQWQC PGYSICVNLS ALCDGVFDCP NGTDESPLCN
1360 1370 1380 1390 1400
QDSCLHFNGG CTHRCIQGPF GATCVCPIGY QLANDTKTCE DVNECDIPGF
1410 1420 1430 1440 1450
CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTASENLLLV VASRDKIIMD
1460 1470 1480 1490 1500
NITAHTHNIY SLVQDVSFVV ALDFDSVTGR VFWSDLLEGK TWSAFQNGTD
1510 1520 1530 1540 1550
KRVVHDSGLS LTEMIAVDWI GRNIYWTDYT LETIEVSKID GSHRTVLISK
1560 1570 1580 1590 1600
NVTKPRGLAL DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW
1610 1620 1630 1640 1650
PCGLSIDYPN RLIYFMDAYL DYIEFCDYDG QNRRQVIASD LVLHHPHALT
1660 1670 1680 1690 1700
LFEDSVFWTD RGTHQVMQAN KWHGRNQSVV MYSVPQPLGI IAIHPSRQPS
1710 1720 1730 1740 1750
SPNPCASATC SHLCLLSAQE PRHYSCACPS GWNLSDDSVN CVRGDQPFLI
1760 1770 1780 1790 1800
SVRENVIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
1810 1820 1830 1840 1850
EIHRVKTDGS NRTAFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT
1860 1870 1880 1890 1900
LRGDTRYGKT LITNDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK
1910 1920 1930 1940 1950
IASANMDGTS LKILFTGNME HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD
1960 1970 1980 1990 2000
GTERMILVHH LAHPWGLVVH GSFLYYSDEQ YEVIERVDKS SGSNKVVFRD
2010 2020 2030 2040 2050
NIPYLRGLRV YHHRNAADSS NGCSNNPNAC QQICLPVPGG MFSCACASGF
2060 2070 2080 2090 2100
KLSPDGRSCS PYNSFIVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
2110 2120 2130 2140 2150
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP NGSNFTNIVT YGIGANGIRG
2160 2170 2180 2190 2200
VAVDWVAGNL YFTNAFVYET LIEVIRINTT YRRVLLKVSV DMPRHIVVDP
2210 2220 2230 2240 2250
KHRYLFWADY GQKPKIERSF LDCTNRTVLV SEGIVTPRGL AVDHDTGYIY
2260 2270 2280 2290 2300
WVDDSLDIIA RIHRDGGESQ VVRYGSRYPT PYGITVFGES IIWVDRNLRK
2310 2320 2330 2340 2350
VFQASKQPGN TDPPTVIRDS INLLRDVTIF DEHVQPLSPA ELNNNPCLQS
2360 2370 2380 2390 2400
NGGCSHFCFA LPELPTPKCG CAFGTLEDDG KNCATSREDF LIYSLNNSLR
2410 2420 2430 2440 2450
SLHFDPQDHN LPFQAISVEG MAIALDYDRR NNRIFFTQKL NPIRGQISYV
2460 2470 2480 2490 2500
NLYSGASSPT ILLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN
2510 2520 2530 2540 2550
RAVIARVSKP RAIVLDPCRG YMYWTDWGTN AKIERATLGG NFRVPIVNTS
2560 2570 2580 2590 2600
LVWPNGLTLD LETDLLYWAD ASLQKIERST LTGSNREVVI STAFHSFGLT
2610 2620 2630 2640 2650
VYGQYIYWTD FYTKKIYRAN KYDGSDLIAM TTRLPTQPSG ISTVVKTQQQ
2660 2670 2680 2690 2700
QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGSWYLANDN KYCVVDTGAR
2710 2720 2730 2740 2750
CNQFQFTCLN GRCISQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCA
2760 2770 2780 2790 2800
NGRCVPYHYR CDFYNDCGDN SDEAGCLFRS CNSTTEFTCS NGRCIPLSYV
2810 2820 2830 2840 2850
CNGINNCHDN DTSDEKNCPP ITCQPDFAKC QTTNICVPRA FLCDGDNDCG
2860 2870 2880 2890 2900
DGSDENPIYC ASHTCRSNEF QCVSPHRCIP SYWFCDGEAD CVDSSDEPDT
2910 2920 2930 2940 2950
CGHSLNSCSA NQFHCDNGRC ISSSWVCDGD NDCGDMSDED QRHHCELQNC
2960 2970 2980 2990 3000
SSTEFTCINS RPPNRRCIPQ HWVCDGDADC ADALDELQNC TMRACSTGEF
3010 3020 3030 3040 3050
SCANGRCIRQ SFRCDRRNDC GDYSDERGCS YPPCRDDQFT CQNGQCITKL
3060 3070 3080 3090 3100
YVCDEDNDCG DGSDEQEHLC HTPEPTCPPH QFRCDNGHCI EMGTVCNHVD
3110 3120 3130 3140 3150
DCSDNSDEKG CGINECQDSS ISHCDHNCTD TITSFYCSCL PGYKLMSDKR
3160 3170 3180 3190 3200
TCVDIDECKE TPQLCSQKCE NVIGSYICKC APGYIREPDG KSCRQNSNIE
3210 3220 3230 3240 3250
PYLVFSNRYY IRNLTIDGTS YSLILQGLGN VVALDFDRVE ERLYWIDAEK
3260 3270 3280 3290 3300
QIIERMFLNK TNQETIISHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
3310 3320 3330 3340 3350
LEGRQRKMLA QHCVDANNTF CFENPRGIVL HPQRGYVYWA DWGDHAYIAR
3360 3370 3380 3390 3400
IGMDGTNKTV IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH
3410 3420 3430 3440 3450
RHTVYDGTLP HPFALTIFED TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT
3460 3470 3480 3490 3500
HKPFDIHVLH PYRQPIMSNP CATNNGGCSH LCLIKAGGRG FTCECPDDFQ
3510 3520 3530 3540 3550
TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC SDGSDESDLC
3560 3570 3580 3590 3600
PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCEANE
3610 3620 3630 3640 3650
WQCANKRCIP EYWQCDSVDD CLDNSDEDPS HCASRTCRPG QFKCNNGRCI
3660 3670 3680 3690 3700
PQSWKCDVDN DCGDYSDEPI HECMTAAYNC DNHTEFSCKT NYRCIPQWAV
3710 3720 3730 3740 3750
CNGFDDCRDN SDEQGCESVP CHPSGDFRCG NHHCIPLRWK CDGIDDCGDN
3760 3770 3780 3790 3800
SDEESCVPRE CTESEFRCAD QQCIPSRWVC DQENDCGDNS DERDCEMKTC
3810 3820 3830 3840 3850
HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN GTYCPAAMFE
3860 3870 3880 3890 3900
CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNVPCESPQR FRCDNSRCIY
3910 3920 3930 3940 3950
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCVSQHYVCD
3960 3970 3980 3990 4000
NVDDCGDLSD ETGCNLGENR TCAEKICEQN CTQLSNGGFI CSCRPGFKPS
4010 4020 4030 4040 4050
TLDKNSCQDI NECEEFGICP QSCRNSKGSY ECFCVDGFKS MSTHYGERCA
4060 4070 4080 4090 4100
ADGSPPLLLL PENVRIRKYN ISSEKFSEYL EEEEHIQAID YDWDPEGIGL
4110 4120 4130 4140 4150
SVVYYTVLSQ GSQFGAIKRA YLPDFESGSN NPVREVDLGL KYLMQPDGLA
4160 4170 4180 4190 4200
VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
4210 4220 4230 4240 4250
MFWTDQGKQP KIESAWMNGE HRSVLASANL GWPNGLSIDY LNGDRIYWSD
4260 4270 4280 4290 4300
SKEDVIESIK YDGTDRRLII NDAMKPFSLD IFEDQLYWVA KEKGEVWRQN
4310 4320 4330 4340 4350
KFGKGNKEKL LVVNPWLTQV RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG
4360 4370 4380 4390 4400
YSCACPQGSD FVTGSTVECD AASELPITMP SPCRCMHGGS CYFDENDLPK
4410 4420 4430 4440 4450
CKCSSGYSGE YCEIGLSRGI PPGTTMALLL TFAMVIIVGA LVLVGFFHYR
4460 4470 4480 4490 4500
KTGSLLPSLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
4510 4520 4530 4540 4550
IDRSMAMNEQ FVMEVGKQPV IFENPMYAAK DSTSKVGLAV QGPSVSSQVT
4560 4570 4580 4590 4600
VPENVENQNY GRSIDPSEIV PEPKPASPGA DETQGTKWNI FKRKPKQTTN
4610 4620 4630 4640 4650
FENPIYAEMD TEQKEAVAVA PPPSPSLPAK ASKRSSTPGY TATEDTFKDT
4660
ANLVKEDSDV
Length:4,660
Mass (Da):519,208
Last modified:February 20, 2007 - v1
Checksum:i4CF399C24DF2FAA4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4198L → F in CAA69877 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL845489 Genomic DNA. Translation: CAM20178.1.
AK166702 mRNA. Translation: BAE38957.1.
Y08566 mRNA. Translation: CAA69877.1.
AF197160 mRNA. Translation: AAF61488.1.
CCDSiCCDS38135.1.
RefSeqiNP_001074557.1. NM_001081088.1.
UniGeneiMm.23847.

Genome annotation databases

EnsembliENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070.
GeneIDi14725.
KEGGimmu:14725.
UCSCiuc008jyc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL845489 Genomic DNA. Translation: CAM20178.1.
AK166702 mRNA. Translation: BAE38957.1.
Y08566 mRNA. Translation: CAA69877.1.
AF197160 mRNA. Translation: AAF61488.1.
CCDSiCCDS38135.1.
RefSeqiNP_001074557.1. NM_001081088.1.
UniGeneiMm.23847.

3D structure databases

ProteinModelPortaliA2ARV4.
SMRiA2ARV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200005. 4 interactors.
IntActiA2ARV4. 11 interactors.
MINTiMINT-4106203.
STRINGi10090.ENSMUSP00000079752.

Protein family/group databases

TCDBi9.B.87.1.1. the selenoprotein p receptor (selp-receptor) family.

PTM databases

iPTMnetiA2ARV4.
PhosphoSitePlusiA2ARV4.

Proteomic databases

MaxQBiA2ARV4.
PaxDbiA2ARV4.
PeptideAtlasiA2ARV4.
PRIDEiA2ARV4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080953; ENSMUSP00000079752; ENSMUSG00000027070.
GeneIDi14725.
KEGGimmu:14725.
UCSCiuc008jyc.1. mouse.

Organism-specific databases

CTDi4036.
MGIiMGI:95794. Lrp2.

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
HOVERGENiHBG097941.
InParanoidiA2ARV4.
KOiK06233.
OMAiTRPPGMC.
OrthoDBiEOG091G000N.
PhylomeDBiA2ARV4.
TreeFamiTF315253.

Enzyme and pathway databases

ReactomeiR-MMU-196791. Vitamin D (calciferol) metabolism.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-975634. Retinoid metabolism and transport.

Miscellaneous databases

PROiA2ARV4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027070.
ExpressionAtlasiA2ARV4. baseline and differential.
GenevisibleiA2ARV4. MM.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
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]
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 17 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 25 hits.
SM00179. EGF_CA. 9 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 37 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 35 hits.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiLRP2_MOUSE
AccessioniPrimary (citable) accession number: A2ARV4
Secondary accession number(s): P70215, Q3TL35, Q9JLB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 20, 2007
Last modified: November 30, 2016
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.