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Reviewed, UniProtKB/Swiss-Prot P98158 (LRP2_RAT)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Low-density lipoprotein receptor-related protein 2
Alternative name(s):
    Megalin
    Glycoprotein 330
      Short name=gp330
Gene names
Name: Lrp2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length4660 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts together with cubilin to mediate HDL endocytosis By similarity. Receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B.

Subunit structure

Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex together with a receptor-associated protein (RAP). Binds to ankyrin-repeat family A protein 2 (ANKRA2). Interacts with LRP2BP By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Membrane › clathrin-coated pit. Cytoplasm. Note: Expressed in clathrin-coated pits, a soluble form is possibly derived by cleavage at the cell surface.

Tissue specificity

Epithelial cells of kidney glomerulus and proximal tubule, lung, epididymis, yolk sac, among others. Ref.3

Sequence similarities

Belongs to the LDLR family.

Contains 17 EGF-like domains.

Contains 36 LDL-receptor class A domains.

Contains 37 LDL-receptor class B repeats.

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Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Coated pit
Cytoplasm
Membrane
   DomainEGF-like domain
Repeat
SH3-binding
Signal
Transmembrane
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processaging

Inferred from expression pattern. Source: RGD

endosome transport

Inferred from mutant phenotype. Source: RGD

hormone secretion

Inferred from mutant phenotype. Source: RGD

lipoprotein transport

Inferred from mutant phenotype. Source: RGD

organ regeneration

Inferred from expression pattern. Source: RGD

receptor-mediated endocytosis

Inferred from direct assay. Source: RGD

response to X-ray

Inferred from direct assay. Source: RGD

response to drug

Inferred from expression pattern. Source: RGD

response to retinoic acid

Inferred from expression pattern. Source: RGD

response to vitamin D

Inferred from expression pattern. Source: RGD

transcytosis

Inferred from mutant phenotype. Source: RGD

vitamin metabolic process

Traceable author statement. Source: RGD

   Cellular componentapical plasma membrane

Inferred from direct assay. Source: RGD

brush border membrane

Inferred from direct assay. Source: RGD

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay. Source: RGD

extracellular space

Inferred from direct assay. Source: RGD

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane fraction

Inferred from direct assay. Source: RGD

   Molecular functionSH3 domain binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: InterPro

receptor activity

Inferred from mutant phenotype. Source: RGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 46604635Low-density lipoprotein receptor-related protein 2
PRO_0000017322

Regions

Topological domain26 – 44254400Extracellular Potential
Transmembrane4426 – 444621 Potential
Topological domain4447 – 4660214Cytoplasmic Potential
Domain26 – 6439LDL-receptor class A 1
Domain65 – 10541LDL-receptor class A 2
Domain106 – 14439LDL-receptor class A 3
Domain145 – 18137LDL-receptor class A 4
Domain181 – 21939LDL-receptor class A 5
Domain220 – 25839LDL-receptor class A 6
Domain263 – 30745LDL-receptor class A 7
Domain308 – 34639EGF-like 1
Domain347 – 38539EGF-like 2
Repeat435 – 47743LDL-receptor class B 1
Repeat478 – 52043LDL-receptor class B 2
Repeat521 – 56747LDL-receptor class B 3
Repeat568 – 61144LDL-receptor class B 4
Repeat612 – 65241LDL-receptor class B 5
Domain658 – 70447EGF-like 3
Repeat752 – 79443LDL-receptor class B 6
Repeat795 – 83642LDL-receptor class B 7
Repeat837 – 88044LDL-receptor class B 8
Repeat881 – 92444LDL-receptor class B 9
Domain969 – 101345EGF-like 4
Domain1023 – 106139LDL-receptor class A 8
Domain1064 – 110340LDL-receptor class A 9
Domain1108 – 114639LDL-receptor class A 10
Domain1148 – 118639LDL-receptor class A 11
Domain1186 – 122540LDL-receptor class A 12
Domain1229 – 126941LDL-receptor class A 13
Domain1270 – 130839LDL-receptor class A 14
Domain1311 – 135141LDL-receptor class A 15
Domain1350 – 139041EGF-like 5
Domain1391 – 143040EGF-like 6; calcium-binding Potential
Repeat1479 – 152143LDL-receptor class B 10
Repeat1522 – 156443LDL-receptor class B 11
Repeat1567 – 161044LDL-receptor class B 12
Repeat1611 – 165444LDL-receptor class B 13
Repeat1655 – 169642LDL-receptor class B 14
Domain1701 – 174242EGF-like 7
Repeat1791 – 183343LDL-receptor class B 15
Repeat1834 – 188350LDL-receptor class B 16
Repeat1884 – 193148LDL-receptor class B 17
Repeat1932 – 197241LDL-receptor class B 18
Repeat1973 – 201442LDL-receptor class B 19
Domain2019 – 206042EGF-like 8
Repeat2108 – 215750LDL-receptor class B 20
Repeat2158 – 220245LDL-receptor class B 21
Repeat2203 – 224644LDL-receptor class B 22
Repeat2247 – 229044LDL-receptor class B 23
Repeat2291 – 233242LDL-receptor class B 24
Domain2343 – 238442EGF-like 9
Repeat2433 – 247846LDL-receptor class B 25
Repeat2479 – 251941LDL-receptor class B 26
Repeat2520 – 256344LDL-receptor class B 27
Repeat2564 – 260441LDL-receptor class B 28
Repeat2605 – 264743LDL-receptor class B 29
Domain2652 – 269443EGF-like 10
Domain2699 – 273941LDL-receptor class A 16
Domain2740 – 277839LDL-receptor class A 17
Domain2779 – 282042LDL-receptor class A 18
Domain2821 – 286242LDL-receptor class A 19
Domain2863 – 290341LDL-receptor class A 20
Domain2906 – 294742LDL-receptor class A 21
Domain2948 – 299245LDL-receptor class A 22
Domain2993 – 303139LDL-receptor class A 23
Domain3032 – 307241LDL-receptor class A 24
Domain3075 – 311238LDL-receptor class A 25
Domain3113 – 315341EGF-like 11
Domain3154 – 319441EGF-like 12; calcium-binding Potential
Repeat3241 – 328343LDL-receptor class B 30
Repeat3284 – 332643LDL-receptor class B 31
Repeat3335 – 337844LDL-receptor class B 32
Repeat3379 – 342042LDL-receptor class B 33
Repeat3421 – 346242LDL-receptor class B 34
Domain3467 – 351145EGF-like 13
Domain3512 – 355241LDL-receptor class A 26
Domain3553 – 359341LDL-receptor class A 27
Domain3594 – 363441LDL-receptor class A 28
Domain3635 – 367541LDL-receptor class A 29
Domain3678 – 371841LDL-receptor class A 30
Domain3719 – 375840LDL-receptor class A 31
Domain3759 – 379739LDL-receptor class A 32
Domain3798 – 383639LDL-receptor class A 33
Domain3842 – 388241LDL-receptor class A 34
Domain3883 – 392442LDL-receptor class A 35
Domain3928 – 396639LDL-receptor class A 36
Domain3968 – 400841EGF-like 14
Domain4009 – 405042EGF-like 15; calcium-binding Potential
Repeat4156 – 419843LDL-receptor class B 35
Repeat4199 – 424244LDL-receptor class B 36
Repeat4244 – 428542LDL-receptor class B 37
Domain4332 – 437039EGF-like 16
Domain4379 – 441335EGF-like 17
Motif1743 – 17453Cell attachment site Potential
Motif4454 – 44607SH3-binding Potential
Motif4457 – 44637SH3-binding Potential
Motif4522 – 45276Endocytosis signal Potential
Motif4601 – 46066Endocytosis signal Potential
Motif4606 – 46094SH2-binding Potential
Motif4619 – 46257SH3-binding Potential
Motif4624 – 46307SH3-binding Potential

Amino acid modifications

Modified residue44641Phosphoserine By similarity
Modified residue44721Phosphoserine By similarity
Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Potential
Glycosylation8651N-linked (GlcNAc...) Potential
Glycosylation10631N-linked (GlcNAc...) Potential
Glycosylation11871N-linked (GlcNAc...) Potential
Glycosylation13281N-linked (GlcNAc...) Potential
Glycosylation13411N-linked (GlcNAc...) Potential
Glycosylation13841N-linked (GlcNAc...) Potential
Glycosylation14511N-linked (GlcNAc...) Potential
Glycosylation14971N-linked (GlcNAc...) Potential
Glycosylation15511N-linked (GlcNAc...) Potential
Glycosylation16761N-linked (GlcNAc...) Potential
Glycosylation17331N-linked (GlcNAc...) Potential
Glycosylation18111N-linked (GlcNAc...) Potential
Glycosylation21341N-linked (GlcNAc...) Potential
Glycosylation21781N-linked (GlcNAc...) Potential
Glycosylation22251N-linked (GlcNAc...) Potential
Glycosylation23961N-linked (GlcNAc...) Potential
Glycosylation24881N-linked (GlcNAc...) Potential
Glycosylation25481N-linked (GlcNAc...) Potential
Glycosylation27821N-linked (GlcNAc...) Potential
Glycosylation28101N-linked (GlcNAc...) Potential
Glycosylation29491N-linked (GlcNAc...) Potential
Glycosylation29891N-linked (GlcNAc...) Potential
Glycosylation31271N-linked (GlcNAc...) Potential
Glycosylation32131N-linked (GlcNAc...) Potential
Glycosylation32591N-linked (GlcNAc...) Potential
Glycosylation33171N-linked (GlcNAc...) Potential
Glycosylation33571N-linked (GlcNAc...) Potential
Glycosylation34481N-linked (GlcNAc...) Potential
Glycosylation35661N-linked (GlcNAc...) Potential
Glycosylation36821N-linked (GlcNAc...) Potential
Glycosylation38401N-linked (GlcNAc...) Potential
Glycosylation39691N-linked (GlcNAc...) Potential
Glycosylation39801N-linked (GlcNAc...) Potential
Glycosylation40701N-linked (GlcNAc...) Potential
Glycosylation43291N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 40 By similarity
Disulfide bond35 ↔ 53 By similarity
Disulfide bond47 ↔ 62 By similarity
Disulfide bond67 ↔ 80 By similarity
Disulfide bond74 ↔ 93 By similarity
Disulfide bond87 ↔ 103 By similarity
Disulfide bond108 ↔ 120 By similarity
Disulfide bond115 ↔ 133 By similarity
Disulfide bond127 ↔ 142 By similarity
Disulfide bond147 ↔ 157 By similarity
Disulfide bond152 ↔ 170 By similarity
Disulfide bond164 ↔ 179 By similarity
Disulfide bond183 ↔ 195 By similarity
Disulfide bond190 ↔ 208 By similarity
Disulfide bond202 ↔ 217 By similarity
Disulfide bond222 ↔ 234 By similarity
Disulfide bond229 ↔ 247 By similarity
Disulfide bond241 ↔ 256 By similarity
Disulfide bond265 ↔ 278 By similarity
Disulfide bond272 ↔ 291 By similarity
Disulfide bond285 ↔ 306 By similarity
Disulfide bond311 ↔ 320 By similarity
Disulfide bond316 ↔ 329 By similarity
Disulfide bond331 ↔ 345 By similarity
Disulfide bond351 ↔ 361 By similarity
Disulfide bond357 ↔ 370 By similarity
Disulfide bond372 ↔ 384 By similarity
Disulfide bond662 ↔ 673 By similarity
Disulfide bond669 ↔ 688 By similarity
Disulfide bond690 ↔ 703 By similarity
Disulfide bond973 ↔ 987 By similarity
Disulfide bond983 ↔ 997 By similarity
Disulfide bond999 ↔ 1012 By similarity
Disulfide bond1025 ↔ 1037 By similarity
Disulfide bond1032 ↔ 1050 By similarity
Disulfide bond1044 ↔ 1059 By similarity
Disulfide bond1066 ↔ 1079 By similarity
Disulfide bond1073 ↔ 1092 By similarity
Disulfide bond1086 ↔ 1101 By similarity
Disulfide bond1110 ↔ 1122 By similarity
Disulfide bond1117 ↔ 1135 By similarity
Disulfide bond1129 ↔ 1144 By similarity
Disulfide bond1150 ↔ 1162 By similarity
Disulfide bond1157 ↔ 1175 By similarity
Disulfide bond1169 ↔ 1184 By similarity
Disulfide bond1188 ↔ 1201 By similarity
Disulfide bond1195 ↔ 1214 By similarity
Disulfide bond1208 ↔ 1223 By similarity
Disulfide bond1231 ↔ 1244 By similarity
Disulfide bond1238 ↔ 1257 By similarity
Disulfide bond1251 ↔ 1267 By similarity
Disulfide bond1272 ↔ 1284 By similarity
Disulfide bond1279 ↔ 1297 By similarity
Disulfide bond1291 ↔ 1306 By similarity
Disulfide bond1313 ↔ 1326 By similarity
Disulfide bond1320 ↔ 1339 By similarity
Disulfide bond1333 ↔ 1349 By similarity
Disulfide bond1354 ↔ 1365 By similarity
Disulfide bond1361 ↔ 1374 By similarity
Disulfide bond1376 ↔ 1389 By similarity
Disulfide bond1395 ↔ 1405 By similarity
Disulfide bond1401 ↔ 1414 By similarity
Disulfide bond1416 ↔ 1429 By similarity
Disulfide bond1705 ↔ 1714 By similarity
Disulfide bond1710 ↔ 1726 By similarity
Disulfide bond1728 ↔ 1741 By similarity
Disulfide bond2023 ↔ 2034 By similarity
Disulfide bond2030 ↔ 2044 By similarity
Disulfide bond2046 ↔ 2059 By similarity
Disulfide bond2347 ↔ 2358 By similarity
Disulfide bond2354 ↔ 2369 By similarity
Disulfide bond2371 ↔ 2383 By similarity
Disulfide bond2656 ↔ 2667 By similarity
Disulfide bond2663 ↔ 2676 By similarity
Disulfide bond2678 ↔ 2693 By similarity
Disulfide bond2701 ↔ 2713 By similarity
Disulfide bond2708 ↔ 2726 By similarity
Disulfide bond2720 ↔ 2737 By similarity
Disulfide bond2742 ↔ 2754 By similarity
Disulfide bond2749 ↔ 2767 By similarity
Disulfide bond2761 ↔ 2776 By similarity
Disulfide bond2781 ↔ 2794 By similarity
Disulfide bond2789 ↔ 2807 By similarity
Disulfide bond2801 ↔ 2818 By similarity
Disulfide bond2823 ↔ 2836 By similarity
Disulfide bond2830 ↔ 2849 By similarity
Disulfide bond2843 ↔ 2860 By similarity
Disulfide bond2865 ↔ 2878 By similarity
Disulfide bond2872 ↔ 2891 By similarity
Disulfide bond2885 ↔ 2901 By similarity
Disulfide bond2908 ↔ 2920 By similarity
Disulfide bond2915 ↔ 2933 By similarity
Disulfide bond2927 ↔ 2945 By similarity
Disulfide bond2950 ↔ 2967 By similarity
Disulfide bond2957 ↔ 2980 By similarity
Disulfide bond2974 ↔ 2990 By similarity
Disulfide bond2995 ↔ 3007 By similarity
Disulfide bond3002 ↔ 3020 By similarity
Disulfide bond3014 ↔ 3029 By similarity
Disulfide bond3034 ↔ 3046 By similarity
Disulfide bond3041 ↔ 3059 By similarity
Disulfide bond3053 ↔ 3070 By similarity
Disulfide bond3077 ↔ 3089 By similarity
Disulfide bond3084 ↔ 3102 By similarity
Disulfide bond3096 ↔ 3111 By similarity
Disulfide bond3116 ↔ 3128 By similarity
Disulfide bond3124 ↔ 3137 By similarity
Disulfide bond3139 ↔ 3152 By similarity
Disulfide bond3158 ↔ 3169 By similarity
Disulfide bond3165 ↔ 3178 By similarity
Disulfide bond3180 ↔ 3193 By similarity
Disulfide bond3471 ↔ 3482 By similarity
Disulfide bond3478 ↔ 3493 By similarity
Disulfide bond3495 ↔ 3510 By similarity
Disulfide bond3514 ↔ 3527 By similarity
Disulfide bond3521 ↔ 3540 By similarity
Disulfide bond3534 ↔ 3550 By similarity
Disulfide bond3555 ↔ 3567 By similarity
Disulfide bond3562 ↔ 3580 By similarity
Disulfide bond3574 ↔ 3591 By similarity
Disulfide bond3596 ↔ 3608 By similarity
Disulfide bond3603 ↔ 3621 By similarity
Disulfide bond3615 ↔ 3632 By similarity
Disulfide bond3637 ↔ 3649 By similarity
Disulfide bond3644 ↔ 3662 By similarity
Disulfide bond3656 ↔ 3673 By similarity
Disulfide bond3680 ↔ 3694 By similarity
Disulfide bond3688 ↔ 3707 By similarity
Disulfide bond3701 ↔ 3716 By similarity
Disulfide bond3721 ↔ 3734 By similarity
Disulfide bond3729 ↔ 3747 By similarity
Disulfide bond3741 ↔ 3756 By similarity
Disulfide bond3761 ↔ 3773 By similarity
Disulfide bond3768 ↔ 3786 By similarity
Disulfide bond3780 ↔ 3795 By similarity
Disulfide bond3800 ↔ 3812 By similarity
Disulfide bond3807 ↔ 3825 By similarity
Disulfide bond3819 ↔ 3834 By similarity
Disulfide bond3844 ↔ 3856 By similarity
Disulfide bond3851 ↔ 3869 By similarity
Disulfide bond3863 ↔ 3880 By similarity
Disulfide bond3885 ↔ 3898 By similarity
Disulfide bond3893 ↔ 3911 By similarity
Disulfide bond3905 ↔ 3922 By similarity
Disulfide bond3930 ↔ 3942 By similarity
Disulfide bond3937 ↔ 3955 By similarity
Disulfide bond3949 ↔ 3964 By similarity
Disulfide bond3972 ↔ 3981 By similarity
Disulfide bond3977 ↔ 3991 By similarity
Disulfide bond3993 ↔ 4007 By similarity
Disulfide bond4013 ↔ 4023 By similarity
Disulfide bond4019 ↔ 4032 By similarity
Disulfide bond4034 ↔ 4049 By similarity
Disulfide bond4336 ↔ 4344 By similarity
Disulfide bond4340 ↔ 4353 By similarity
Disulfide bond4355 ↔ 4369 By similarity
Disulfide bond4383 ↔ 4391 By similarity
Disulfide bond4385 ↔ 4401 By similarity
Disulfide bond4403 ↔ 4412 By similarity

Secondary structure

1 ........... 4660
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P98158-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E2A0CFD23D0923C3

FASTA4,660519,276
        10         20         30         40         50         60 
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI 

        70         80         90        100        110        120 
GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ QNCAGTTCSA QQMTCSNGQC 

       130        140        150        160        170        180 
IPSEYRCDHV SDCPDGSDER NCHYPTCDQL TCANGACYNT SQRCDQKVDC RDSSDEANCT 

       190        200        210        220        230        240 
TLCSQKEFEC GSGECILRAY VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV 

       250        260        270        280        290        300 
CDGDDDCQDS GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV 

       310        320        330        340        350        360 
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK 

       370        380        390        400        410        420 
CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG RDLLVGDLHG RNFRILAESK 

       430        440        450        460        470        480 
NRGMVMGVDF HYQKHRVFWT DPMQEKVFST DINGLNTQEI LNVSVDTPEN LAVDWINNKL 

       490        500        510        520        530        540 
YLVETKVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA 

       550        560        570        580        590        600 
FMDGSNRKDL VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV 

       610        620        630        640        650        660 
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY HALRQPNATN 

       670        680        690        700        710        720 
PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE HRCVAVKNFL LFSSKTAVRG 

       730        740        750        760        770        780 
IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTVFYSDLS KDIIYKQKID GTGKEVITAN 

       790        800        810        820        830        840 
RLESVECLTF DWISRNLYWT DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF 

       850        860        870        880        890        900 
LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG 

       910        920        930        940        950        960 
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR RGISSVMHVK 

       970        980        990       1000       1010       1020 
AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP 

      1030       1040       1050       1060       1070       1080 
PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC HDNSDEHQCG VFNNTCSPSA FACVRGGQCI 

      1090       1100       1110       1120       1130       1140 
PGQWHCDRQN DCLDGSDEQN CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD 

      1150       1160       1170       1180       1190       1200 
EKNCQASGTC QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS 

      1210       1220       1230       1240       1250       1260 
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIHG 

      1270       1280       1290       1300       1310       1320 
SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM SDEKDCPTQP FHCPSTQWQC 

      1330       1340       1350       1360       1370       1380 
PGYSTCINLS ALCDGVFDCP NGTDESPLCN QDSCSHFNGG CTHQCMQGPF GATCLCPLGY 

      1390       1400       1410       1420       1430       1440 
QLANDTKTCE DINECDIPGF CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV 

      1450       1460       1470       1480       1490       1500 
VASRDKIIVD NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD 

      1510       1520       1530       1540       1550       1560 
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK NVTKPRGLAL 

      1570       1580       1590       1600       1610       1620 
DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW PCGLSIDYPN RLIYFMDAYL 

      1630       1640       1650       1660       1670       1680 
DYIEFCDYDG HNRRQVIASD LVLHHPHALT LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV 

      1690       1700       1710       1720       1730       1740 
MYSVHQPLGI TAIHPSRQPP SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN 

      1750       1760       1770       1780       1790       1800 
CVRGDQPFLM SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG 

      1810       1820       1830       1840       1850       1860 
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT LKGDTRYGKT 

      1870       1880       1890       1900       1910       1920 
LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK IASANMDGTS LKILFTGNLQ 

      1930       1940       1950       1960       1970       1980 
HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD GTERMILVHH LAHPWGLVVY GSFLYYSDEQ 

      1990       2000       2010       2020       2030       2040 
YEVIERVDKS SGNNKVVLRD NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG 

      2050       2060       2070       2080       2090       2100 
MFSCACASGF KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH 

      2110       2120       2130       2140       2150       2160 
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG VALDWAAGNL 

      2170       2180       2190       2200       2210       2220 
YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP KHRYLFWADY GQKPKIERSF 

      2230       2240       2250       2260       2270       2280 
LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT 

      2290       2300       2310       2320       2330       2340 
PYGITVFGES IIWVDRNLKK VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA 

      2350       2360       2370       2380       2390       2400 
ELNNNPCLQS NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR 

      2410       2420       2430       2440       2450       2460 
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV SLYSGSSSPT 

      2470       2480       2490       2500       2510       2520 
VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN RAVIARVSKP RAIVLDPCRG 

      2530       2540       2550       2560       2570       2580 
YMYWTDWGTN AKIERATLGG NFRVPIVNTS LVWPNGLALD LETDLLYWAD ASLQKIERST 

      2590       2600       2610       2620       2630       2640 
LTGTNREVVV STAFHSFGLT VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG 

      2650       2660       2670       2680       2690       2700 
ISTVVKTQRQ QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR 

      2710       2720       2730       2740       2750       2760 
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG NGRCVPYHYR 

      2770       2780       2790       2800       2810       2820 
CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV CNGINNCHDN DTSDEKNCPP 

      2830       2840       2850       2860       2870       2880 
HTCPPDFTKC QTTNICVPRA FLCDGDNDCG DGSDENPIYC ASHTCRSNEF QCLSPQRCIP 

      2890       2900       2910       2920       2930       2940 
SYWFCDGEAD CADGSDEPDT CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED 

      2950       2960       2970       2980       2990       3000 
QRHHCELQNC SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF 

      3010       3020       3030       3040       3050       3060 
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF FVCDEDNDCG 

      3070       3080       3090       3100       3110       3120 
DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD DCSDNSDEKG CGINECLDSS 

      3130       3140       3150       3160       3170       3180 
ISRCDHNCTD TITSFYCSCL PGYKLMSDKR SCVDIDECKE SPQLCSQKCE NVVGSYICKC 

      3190       3200       3210       3220       3230       3240 
APGYIREPDG KSCRQNSNIE PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE 

      3250       3260       3270       3280       3290       3300 
KRLYWIDAEK QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD 

      3310       3320       3330       3340       3350       3360 
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR IGMDGTNKSV 

      3370       3380       3390       3400       3410       3420 
IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH RHTVYDGSLP HPFALTIFED 

      3430       3440       3450       3460       3470       3480 
TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH 

      3490       3500       3510       3520       3530       3540 
LCLIKAGGRG FTCACPDDFQ TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC 

      3550       3560       3570       3580       3590       3600 
SDGSDEPDLC PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE 

      3610       3620       3630       3640       3650       3660 
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI PQSWKCDVDN 

      3670       3680       3690       3700       3710       3720 
DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV CNGFDDCRDN SDEQGCESVP 

      3730       3740       3750       3760       3770       3780 
CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN SDEENCVPRE CSESEFRCAD QQCIPSRWVC 

      3790       3800       3810       3820       3830       3840 
DQENDCGDNS DERDCEMKTC HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN 

      3850       3860       3870       3880       3890       3900 
GTYCPAAMFE CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY 

      3910       3920       3930       3940       3950       3960 
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD NVNDCGDLSD 

      3970       3980       3990       4000       4010       4020 
ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS TSDKNSCQDI NECEEFGICP 

      4030       4040       4050       4060       4070       4080 
QSCRNSKGSY ECFCVDGFKS MSTHYGERCA ADGSPPLLLL PENVRIRKYN TSSEKFSEYL 

      4090       4100       4110       4120       4130       4140 
EEEEHIQTID YDWDPEHIGL SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL 

      4150       4160       4170       4180       4190       4200 
KYLMQPDGLA VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL 

      4210       4220       4230       4240       4250       4260 
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD SKEDVIEAIK 

      4270       4280       4290       4300       4310       4320 
YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN KFGKENKEKV LVVNPWLTQV 

      4330       4340       4350       4360       4370       4380 
RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG YSCACPQGSD FVTGSTVQCD AASELPVTMP 

      4390       4400       4410       4420       4430       4440 
PPCRCMHGGN CYFDENELPK CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA 

      4450       4460       4470       4480       4490       4500 
LVLVGLFHYR KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI 

      4510       4520       4530       4540       4550       4560 
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT VPENVENQNY 

      4570       4580       4590       4600       4610       4620 
GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN FENPIYAEMD SEVKDAVAVA 

      4630       4640       4650       4660 
PPPSPSLPAK ASKRNLTPGY TATEDTFKDT ANLVKEDSDV

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References

[1]"Complete cloning and sequencing of rat gp330/'megalin,' a distinctive member of the low density lipoprotein receptor gene family."
Saito A., Pietromonaco S., Loo A.K.C., Farquhar M.G.
Proc. Natl. Acad. Sci. U.S.A. 91:9725-9729(1994) [PubMed: 7937880] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Kidney.
[2]"Evidence that epithelial glycoprotein 330/megalin mediates uptake of polybasic drugs."
Moestrup S.K., Cui S., Vorum H., Bregengaard C., Bjorn S.E., Norris K., Gliemann J., Christensen E.I.
J. Clin. Invest. 96:1404-1413(1995) [PubMed: 7544804] [Abstract]
Cited for: FUNCTION IN UPTAKE OF POLYBASIC DRUGS.
[3]"Organ distribution in rats of two members of the low-density lipoprotein receptor gene family, gp330 and LRP/alpa 2MR, and the receptor-associated protein (RAP)."
Zheng G., Bachinsky D.R., Stamenkovic I., Strickland D.K., Brown D., Andres G., McCluskey R.T.
J. Histochem. Cytochem. 42:531-542(1994) [PubMed: 7510321] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L34049 mRNA. Translation: AAA51369.1.
IPIIPI00205325.
PIRT42737.
RefSeqNP_110454.1.
UniGeneRn.26430

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2I1PNMR-A1185-1229[»]
ModBaseSearch...

PTM databases

GlycoSuiteDBP98158.

Proteomic databases

PRIDEP98158.

Genome annotation databases

EnsemblENSRNOG00000030487. Rattus norvegicus. [Contig view]
GeneID29216.
KEGGrno:29216.

Organism-specific databases

RGD68407. Lrp2.

Phylogenomic databases

HOVERGENP98158.

Gene expression databases

ArrayExpressP98158.
GermOnlineENSRNOG00000030487. Rattus norvegicus.

Family and domain databases

InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR002172. LDL_rcpt_classA_cys-rich.
IPR000033. LDLR.
[Graphical view]
Gene3DG3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 8 hits.
G3DSA:4.10.400.10. LDL_rcpt_classA_cys-rich. 31 hits.
PfamPF00008. EGF. 2 hits.
PF07645. EGF_CA. 3 hits.
PF00057. Ldl_recept_a. 36 hits.
PF00058. Ldl_recept_b. 33 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 14 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 36 hits.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 8 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio608401.

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Entry information

Entry nameLRP2_RAT
AccessionPrimary (citable) accession number: P98158
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents