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Protein

Low-density lipoprotein receptor-related protein

Gene

lrp-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as a receptor for the endocytosis of extracellular ligands such as chylomicron remnants, protease-inhibitor complexes and vitellogenin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4744Critical for endocytosisBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • sterol transporter activity Source: WormBase

GO - Biological processi

  • ecdysis, collagen and cuticulin-based cuticle Source: WormBase
  • endocytosis Source: UniProtKB-KW
  • nematode larval development Source: WormBase
  • positive regulation of locomotion Source: WormBase
  • positive regulation of multicellular organism growth Source: WormBase
  • regulation of cell migration Source: WormBase
  • sterol transport Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-CEL-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-CEL-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein
Short name:
LRP
Gene namesi
Name:lrp-1
ORF Names:F29D11.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF29D11.1; CE05765; WBGene00003071; lrp-1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 4570ExtracellularSequence analysisAdd BLAST4552
Transmembranei4571 – 4596HelicalSequence analysisAdd BLAST26
Topological domaini4597 – 4753CytoplasmicSequence analysisAdd BLAST157

GO - Cellular componenti

  • apical plasma membrane Source: WormBase
  • clathrin-coated pit Source: UniProtKB-SubCell
  • endocytic vesicle Source: WormBase
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001734119 – 4753Low-density lipoprotein receptor-related proteinAdd BLAST4735

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi17N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi53 ↔ 65By similarity
Disulfide bondi60 ↔ 78By similarity
Disulfide bondi72 ↔ 87By similarity
Disulfide bondi92 ↔ 109By similarity
Disulfide bondi99 ↔ 122By similarity
Disulfide bondi116 ↔ 131By similarity
Glycosylationi118N-linked (GlcNAc...)2 Publications1
Disulfide bondi138 ↔ 152By similarity
Disulfide bondi146 ↔ 165By similarity
Disulfide bondi159 ↔ 175By similarity
Glycosylationi178N-linked (GlcNAc...)1 Publication1
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 208By similarity
Disulfide bondi202 ↔ 218By similarity
Disulfide bondi223 ↔ 235By similarity
Disulfide bondi230 ↔ 248By similarity
Disulfide bondi242 ↔ 257By similarity
Disulfide bondi262 ↔ 275By similarity
Disulfide bondi269 ↔ 288By similarity
Disulfide bondi282 ↔ 297By similarity
Disulfide bondi302 ↔ 311By similarity
Disulfide bondi307 ↔ 320By similarity
Disulfide bondi322 ↔ 336By similarity
Disulfide bondi342 ↔ 352By similarity
Disulfide bondi348 ↔ 361By similarity
Disulfide bondi363 ↔ 367By similarity
Glycosylationi380N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi673 ↔ 682By similarity
Disulfide bondi678 ↔ 697By similarity
Disulfide bondi699 ↔ 711By similarity
Glycosylationi887N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1001 ↔ 1010By similarity
Disulfide bondi1006 ↔ 1026By similarity
Disulfide bondi1028 ↔ 1042By similarity
Glycosylationi1039N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1054 ↔ 1068By similarity
Glycosylationi1057N-linked (GlcNAc...)1 Publication1
Disulfide bondi1063 ↔ 1081By similarity
Disulfide bondi1075 ↔ 1095By similarity
Disulfide bondi1101 ↔ 1114By similarity
Disulfide bondi1108 ↔ 1127By similarity
Disulfide bondi1121 ↔ 1138By similarity
Disulfide bondi1146 ↔ 1158By similarity
Disulfide bondi1153 ↔ 1171By similarity
Disulfide bondi1165 ↔ 1182By similarity
Glycosylationi1184N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1187 ↔ 1199By similarity
Disulfide bondi1194 ↔ 1212By similarity
Disulfide bondi1206 ↔ 1223By similarity
Disulfide bondi1228 ↔ 1241By similarity
Disulfide bondi1235 ↔ 1254By similarity
Disulfide bondi1248 ↔ 1263By similarity
Disulfide bondi1270 ↔ 1283By similarity
Disulfide bondi1277 ↔ 1296By similarity
Disulfide bondi1290 ↔ 1307By similarity
Disulfide bondi1313 ↔ 1325By similarity
Disulfide bondi1320 ↔ 1338By similarity
Disulfide bondi1332 ↔ 1350By similarity
Disulfide bondi1359 ↔ 1373By similarity
Disulfide bondi1366 ↔ 1386By similarity
Disulfide bondi1380 ↔ 1396By similarity
Disulfide bondi1401 ↔ 1412By similarity
Disulfide bondi1408 ↔ 1421By similarity
Disulfide bondi1423 ↔ 1435By similarity
Glycosylationi1431N-linked (GlcNAc...)1 Publication1
Disulfide bondi1441 ↔ 1451By similarity
Disulfide bondi1447 ↔ 1460By similarity
Disulfide bondi1462 ↔ 1475By similarity
Glycosylationi1542N-linked (GlcNAc...)1 Publication1
Glycosylationi1545N-linked (GlcNAc...)1 Publication1
Glycosylationi1597N-linked (GlcNAc...)2 Publications1
Glycosylationi1718N-linked (GlcNAc...)2 Publications1
Disulfide bondi1751 ↔ 1760By similarity
Disulfide bondi1756 ↔ 1770By similarity
Disulfide bondi1772 ↔ 1785By similarity
Glycosylationi1871N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2084 ↔ 2095By similarity
Disulfide bondi2091 ↔ 2105By similarity
Disulfide bondi2107 ↔ 2119By similarity
Glycosylationi2364N-linked (GlcNAc...)1 Publication1
Disulfide bondi2400 ↔ 2415By similarity
Disulfide bondi2411 ↔ 2426By similarity
Disulfide bondi2428 ↔ 2438By similarity
Glycosylationi2501N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2732 ↔ 2743By similarity
Disulfide bondi2739 ↔ 2759By similarity
Disulfide bondi2761 ↔ 2779By similarity
Glycosylationi2762N-linked (GlcNAc...)1 Publication1
Disulfide bondi2792 ↔ 2805By similarity
Disulfide bondi2800 ↔ 2818By similarity
Disulfide bondi2812 ↔ 2829By similarity
Disulfide bondi2834 ↔ 2846By similarity
Disulfide bondi2841 ↔ 2859By similarity
Disulfide bondi2853 ↔ 2868By similarity
Disulfide bondi2874 ↔ 2886By similarity
Disulfide bondi2881 ↔ 2899By similarity
Glycosylationi2888N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2893 ↔ 2912By similarity
Disulfide bondi2919 ↔ 2932By similarity
Disulfide bondi2926 ↔ 2945By similarity
Disulfide bondi2939 ↔ 2956By similarity
Disulfide bondi2961 ↔ 2973By similarity
Disulfide bondi2968 ↔ 2986By similarity
Disulfide bondi2980 ↔ 2997By similarity
Glycosylationi2996N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3006 ↔ 3019By similarity
Disulfide bondi3014 ↔ 3032By similarity
Disulfide bondi3026 ↔ 3044By similarity
Glycosylationi3046N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3049 ↔ 3069By similarity
Disulfide bondi3056 ↔ 3082By similarity
Disulfide bondi3076 ↔ 3093By similarity
Disulfide bondi3100 ↔ 3112By similarity
Disulfide bondi3107 ↔ 3125By similarity
Disulfide bondi3119 ↔ 3135By similarity
Glycosylationi3134N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3140 ↔ 3152By similarity
Disulfide bondi3147 ↔ 3165By similarity
Disulfide bondi3159 ↔ 3174By similarity
Disulfide bondi3187 ↔ 3199By similarity
Disulfide bondi3194 ↔ 3212By similarity
Disulfide bondi3206 ↔ 3222By similarity
Disulfide bondi3227 ↔ 3239By similarity
Disulfide bondi3235 ↔ 3248By similarity
Disulfide bondi3250 ↔ 3264By similarity
Disulfide bondi3270 ↔ 3281By similarity
Disulfide bondi3277 ↔ 3290By similarity
Disulfide bondi3292 ↔ 3305By similarity
Glycosylationi3557N-linked (GlcNAc...)1 Publication1
Disulfide bondi3586 ↔ 3597By similarity
Disulfide bondi3593 ↔ 3608By similarity
Disulfide bondi3610 ↔ 3623By similarity
Glycosylationi3626N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3627 ↔ 3641By similarity
Disulfide bondi3634 ↔ 3654By similarity
Disulfide bondi3648 ↔ 3666By similarity
Disulfide bondi3671 ↔ 3683By similarity
Disulfide bondi3678 ↔ 3696By similarity
Glycosylationi3682N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3690 ↔ 3705By similarity
Disulfide bondi3709 ↔ 3722By similarity
Disulfide bondi3716 ↔ 3735By similarity
Disulfide bondi3729 ↔ 3746By similarity
Glycosylationi3752N-linked (GlcNAc...)1 Publication1
Disulfide bondi3753 ↔ 3765By similarity
Disulfide bondi3760 ↔ 3778By similarity
Disulfide bondi3772 ↔ 3788By similarity
Disulfide bondi3793 ↔ 3806By similarity
Disulfide bondi3800 ↔ 3819By similarity
Disulfide bondi3813 ↔ 3830By similarity
Disulfide bondi3833 ↔ 3847By similarity
Disulfide bondi3841 ↔ 3860By similarity
Disulfide bondi3854 ↔ 3871By similarity
Disulfide bondi3878 ↔ 3890By similarity
Disulfide bondi3885 ↔ 3903By similarity
Disulfide bondi3897 ↔ 3912By similarity
Disulfide bondi3917 ↔ 3929By similarity
Disulfide bondi3924 ↔ 3942By similarity
Disulfide bondi3936 ↔ 3951By similarity
Disulfide bondi3959 ↔ 3971By similarity
Disulfide bondi3966 ↔ 3984By similarity
Disulfide bondi3978 ↔ 3995By similarity
Disulfide bondi4000 ↔ 4014By similarity
Disulfide bondi4008 ↔ 4027By similarity
Disulfide bondi4021 ↔ 4040By similarity
Disulfide bondi4049 ↔ 4061By similarity
Disulfide bondi4056 ↔ 4074By similarity
Glycosylationi4063N-linked (GlcNAc...)1 Publication1
Disulfide bondi4068 ↔ 4083By similarity
Disulfide bondi4092 ↔ 4105By similarity
Disulfide bondi4101 ↔ 4114By similarity
Disulfide bondi4116 ↔ 4130By similarity
Disulfide bondi4136 ↔ 4146By similarity
Glycosylationi4139N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4142 ↔ 4155By similarity
Disulfide bondi4157 ↔ 4175By similarity
Glycosylationi4248N-linked (GlcNAc...)1 Publication1
Disulfide bondi4481 ↔ 4490By similarity
Disulfide bondi4486 ↔ 4500By similarity
Disulfide bondi4502 ↔ 4514By similarity
Disulfide bondi4528 ↔ 4536By similarity
Disulfide bondi4530 ↔ 4542By similarity
Disulfide bondi4544 ↔ 4553By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ04833.
PaxDbiQ04833.
PeptideAtlasiQ04833.
PRIDEiQ04833.

PTM databases

iPTMnetiQ04833.

Expressioni

Gene expression databases

BgeeiWBGene00003071.

Interactioni

Protein-protein interaction databases

BioGridi37962. 7 interactors.
STRINGi6239.F29D11.1.

Structurei

3D structure databases

ProteinModelPortaliQ04833.
SMRiQ04833.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 89LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST39
Domaini90 – 133LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST44
Domaini136 – 177LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST42
Domaini180 – 220LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST41
Domaini221 – 259LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST39
Domaini260 – 298LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST39
Domaini299 – 337EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini338 – 368EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST31
Repeati436 – 482LDL-receptor class B 1Add BLAST47
Repeati483 – 525LDL-receptor class B 2Add BLAST43
Repeati526 – 566LDL-receptor class B 3Add BLAST41
Repeati567 – 609LDL-receptor class B 4Add BLAST43
Repeati610 – 654LDL-receptor class B 5Add BLAST45
Domaini669 – 712EGF-like 3PROSITE-ProRule annotationAdd BLAST44
Repeati766 – 808LDL-receptor class B 6Add BLAST43
Repeati809 – 858LDL-receptor class B 7Add BLAST50
Repeati859 – 902LDL-receptor class B 8Add BLAST44
Repeati903 – 944LDL-receptor class B 9Add BLAST42
Domaini997 – 1043EGF-like 4PROSITE-ProRule annotationAdd BLAST47
Domaini1052 – 1097LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST46
Domaini1099 – 1140LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST42
Domaini1144 – 1184LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST41
Domaini1185 – 1225LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST41
Domaini1226 – 1265LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST40
Domaini1268 – 1309LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST42
Domaini1311 – 1352LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST42
Domaini1357 – 1397LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST41
Domaini1398 – 1436EGF-like 5PROSITE-ProRule annotationAdd BLAST39
Domaini1437 – 1476EGF-like 6PROSITE-ProRule annotationAdd BLAST40
Repeati1524 – 1566LDL-receptor class B 10Add BLAST43
Repeati1567 – 1610LDL-receptor class B 11Add BLAST44
Repeati1611 – 1654LDL-receptor class B 12Add BLAST44
Repeati1655 – 1699LDL-receptor class B 13Add BLAST45
Domaini1747 – 1786EGF-like 7PROSITE-ProRule annotationAdd BLAST40
Repeati1894 – 1942LDL-receptor class B 14Add BLAST49
Repeati1943 – 1989LDL-receptor class B 15Add BLAST47
Repeati1990 – 2032LDL-receptor class B 16Add BLAST43
Domaini2080 – 2120EGF-like 8PROSITE-ProRule annotationAdd BLAST41
Repeati2215 – 2259LDL-receptor class B 17Add BLAST45
Repeati2260 – 2303LDL-receptor class B 18Add BLAST44
Repeati2304 – 2345LDL-receptor class B 19Add BLAST42
Domaini2396 – 2439EGF-like 9PROSITE-ProRule annotationAdd BLAST44
Repeati2582 – 2632LDL-receptor class B 20Add BLAST51
Repeati2633 – 2675LDL-receptor class B 21Add BLAST43
Domaini2728 – 2780EGF-like 10PROSITE-ProRule annotationAdd BLAST53
Domaini2790 – 2831LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST42
Domaini2832 – 2870LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST39
Domaini2872 – 2914LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST43
Domaini2917 – 2958LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST42
Domaini2959 – 2999LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST41
Domaini3004 – 3046LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST43
Domaini3047 – 3095LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST49
Domaini3098 – 3137LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST40
Domaini3138 – 3176LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST39
Domaini3185 – 3223LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST39
Domaini3224 – 3265EGF-like 11PROSITE-ProRule annotationAdd BLAST42
Domaini3266 – 3306EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3354 – 3401LDL-receptor class B 22Add BLAST48
Repeati3402 – 3444LDL-receptor class B 23Add BLAST43
Repeati3445 – 3493LDL-receptor class B 24Add BLAST49
Repeati3494 – 3536LDL-receptor class B 25Add BLAST43
Repeati3537 – 3577LDL-receptor class B 26Add BLAST41
Domaini3582 – 3624EGF-like 13PROSITE-ProRule annotationAdd BLAST43
Domaini3625 – 3668LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST44
Domaini3669 – 3707LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST39
Domaini3707 – 3748LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST42
Domaini3751 – 3790LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST40
Domaini3791 – 3832LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST42
Domaini3831 – 3873LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST43
Domaini3876 – 3914LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST39
Domaini3915 – 3953LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST39
Domaini3957 – 3997LDL-receptor class A 33PROSITE-ProRule annotationAdd BLAST41
Domaini3998 – 4042LDL-receptor class A 34PROSITE-ProRule annotationAdd BLAST45
Domaini4047 – 4085LDL-receptor class A 35PROSITE-ProRule annotationAdd BLAST39
Domaini4088 – 4131EGF-like 14PROSITE-ProRule annotationAdd BLAST44
Domaini4132 – 4176EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Repeati4227 – 4276LDL-receptor class B 27Add BLAST50
Repeati4343 – 4386LDL-receptor class B 28Add BLAST44
Repeati4388 – 4429LDL-receptor class B 29Add BLAST42
Repeati4430 – 4470LDL-receptor class B 30Add BLAST41
Domaini4477 – 4515EGF-like 16PROSITE-ProRule annotationAdd BLAST39
Domaini4526 – 4554EGF-like 17PROSITE-ProRule annotationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4653 – 4658Endocytosis signalSequence analysis6

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 17 EGF-like domains.PROSITE-ProRule annotation
Contains 35 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 30 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
InParanoidiQ04833.
KOiK06233.
OMAiTRPPGMC.
OrthoDBiEOG091G000N.
PhylomeDBiQ04833.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 29 hits.
PF00058. Ldl_recept_b. 8 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 21 hits.
SM00179. EGF_CA. 8 hits.
SM00192. LDLa. 35 hits.
SM00135. LY. 32 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 6 hits.
SSF57424. SSF57424. 33 hits.
PROSITEiPS00010. ASX_HYDROXYL. 6 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 28 hits.
PS50068. LDLRA_2. 34 hits.
PS51120. LDLRB. 30 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q04833-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILRLLIFTA LAVTTANSST RQQSTFHSIQ VDSPPSVRSR IISASVNTAS
60 70 80 90 100
SVCNENDFRC NDGKCIRTEW KCDGSGDCSD GEDEKDCPHP GCKSDQWQCD
110 120 130 140 150
TYTWHSVSCI AEYQRCDNIT DCADGSDEKD CPASTVDCSS QNVFMCADGR
160 170 180 190 200
QCFDVSKKCD GKYDCRDLSD EKDSCSRNHT ACFQYQFRCA DKTQCIQKSW
210 220 230 240 250
VCDGSKDCAD GSDEPDTCEF KKCTANEFQC KNKRCQPRKF RCDYYDDCGD
260 270 280 290 300
NSDEDECGEY RCPPGKWNCP GTGHCIDQLK LCDGSKDCAD GADEQQCSQN
310 320 330 340 350
LCPSLGCQAG CHPSPHGGEC TCPSGYKLDD RFHRTCSDIN ECAEFGYCDQ
360 370 380 390 400
LCANHRPGFT CSCLGDCFTL QMEHGPGKDN LTMRGYCVSN NADKMKLFVA
410 420 430 440 450
RREGLYRLNP KNPDEEVKKL ASGEFIYGID FDYGDRKIFW TDRLAHSAFS
460 470 480 490 500
ADVDDEGEIS QIKKLSLKSL VYPRCLAVDW ITNTLYIIES GSRRIDVSSY
510 520 530 540 550
DGERRTVLLA DGLTLPLDIA LDPLRGEMFF TNQLKLEAAA MDGTNRRTLV
560 570 580 590 600
NTHTHQVSGI VVDITAKRVY WVDPKVDRLE SIDYQGNDRR IVAQGMNVVP
610 620 630 640 650
HPFGLALFDQ YLYWTDWTRL GVIQVEKFGS DTKLLWSNTE NNVFPMGISA
660 670 680 690 700
YHPMAQPGPG QSECLAMKIE NPCTNADCEG MCILSKDNGG FGVGYKCACP
710 720 730 740 750
IGQKLVNGKR CIDSIDYLLF SSNKIVRGIF PEINEKALAE AVLPISPISQ
760 770 780 790 800
RRIGMYFEVE CDVHGNSFFY ADIMDNTIYR IRPDGEGAAP VLVTHNDGLF
810 820 830 840 850
SMSFDWISKQ LYYVDNIRNS LEVVKIGETG LVHPDELVRR QLITELRDPV
860 870 880 890 900
SVVVHPWKGL LFYAEAMRPA AIYRCHIDGQ NCQVIRNTTL GRPSEMAIDF
910 920 930 940 950
AENRLCWGDT LLKTISCMDF DGKNVVKLDI DNPIPVAITI MNEYIYYVHQ
960 970 980 990 1000
RPYSIRRVHK KNGGGSKIVR EFGADERSIF SLKACSHQNQ PIPDDSREHP
1010 1020 1030 1040 1050
CRASQCTQLC FATPSESHPN ELEAKCACRQ GFMINKENNH SCQKDPAEKI
1060 1070 1080 1090 1100
EQLCSSNSTQ FQCKNGRCIP KEWKCDGEND CLDESDEIDE KGDKCFHETE
1110 1120 1130 1140 1150
CAENTIKCRN TKKCIPAQYG CDGDNDCGDY SDEDVKYCKD GQKPVCAAKK
1160 1170 1180 1190 1200
FQCDNHRCIP EQWKCDSDND CGDGSDEKLE MCGNATCAAN QFSCANGRCI
1210 1220 1230 1240 1250
PIYWLCDGDN DCYDGTDEDK ERCPPVQCSA LQFRCANGRQ CVPLRNHCDG
1260 1270 1280 1290 1300
QSDCEDGSDE DSCAVTAESC TPDQFKCVSS GLCIPASWKC DGQQDCDDGS
1310 1320 1330 1340 1350
DEPKFGCTSG RQCSSDQFKC GNGRCILNNW LCDGENDCGD GSDESSERGC
1360 1370 1380 1390 1400
KTSMNARKCP FEHVACENDQ ETCIPLHQLC DGKTHCPGGT DEGGRCARDL
1410 1420 1430 1440 1450
CSADRAGCSF KCHNSPNGPI CSCPFGEQLV NKTKCEPENE CLDSSSCSQR
1460 1470 1480 1490 1500
CKDEKHGFTC SCDEGYELDV DKRTCKVADN VKDTRIYVSN RNRIYYSDHK
1510 1520 1530 1540 1550
LDNWHTFGAI VENAIALAWD SLTDRIYWSD IREKKILSAN RNGTNATVFI
1560 1570 1580 1590 1600
ADGLDITEGI ALDWVGRNLY WVDSSLNTIE VANLEDPKQR TLLVHQNVSQ
1610 1620 1630 1640 1650
PRGIAVDPRK GVMFWTDWGQ NPCIERASMD GTDRQIIVKT KIYWPNTIAL
1660 1670 1680 1690 1700
DYTTDRVYFA DSKLDFIDFV NYDGSGRTQV LASSKFVQHP HALAIFEDMM
1710 1720 1730 1740 1750
YYSDRRLQKL QVYPKYPNGT TSEYPSHTFS KALGVVAVHP VLQPVIKNNP
1760 1770 1780 1790 1800
CSTNPCSHLC LLNNKNTFTC KCPMGEKLDA SGKKCIDDAK PFLVIIQKTN
1810 1820 1830 1840 1850
VFGIEMNSAS EKETPVLAGM VPLSGLGNAF DAAYDALSEE MFILEHTNHA
1860 1870 1880 1890 1900
KTLAQITTDS AIYRSTVNGG NKTKMFSSAV PDDAYCLGFD WNGRNLVVGN
1910 1920 1930 1940 1950
KITQTIEIIR TQGKQYRSVI LSNDQSPTAV VTPVAIAVDA DKGYVFWLDR
1960 1970 1980 1990 2000
GGGAADAKVA RAGLDGSNPL VIASNDLAEL DHIAIDTTNT RVYFSEAKAG
2010 2020 2030 2040 2050
RISSVTYDGQ DRHYVLSDGG RQPNGLAFYG DRLFYADSAF DSIEVATING
2060 2070 2080 2090 2100
DSQPPQWTHF KKDVENLANI KALQPRASSS GHPCHINNGN CDHICIPLMF
2110 2120 2130 2140 2150
AQRTCTCANG YVKDGQTSCK LFDESFVIVA TKTKVIGYPI DETQSKGVAM
2160 2170 2180 2190 2200
EPIGGLSITG VDYDYESKTI YVAEASGINK GITAYTIGES SPRAVIRDSI
2210 2220 2230 2240 2250
GSLTIKSLAI DWINYNMYFI NHDAERTNIE VSKLDGTYRK ILLTTKTETP
2260 2270 2280 2290 2300
SSIAVDPVSR YLYWADQGQK PTIQRSFLDG SRREVIVSSG IAEPTDLVVD
2310 2320 2330 2340 2350
VASKMIYWSD AKMDGIYRVR STGGTPELVR SDIASAAGVA LHGQNMYWTD
2360 2370 2380 2390 2400
NRLEKLFRAT SKPNQTSLLL SPTTVAASLK DIGDVAVFSS NNQPRASSPC
2410 2420 2430 2440 2450
QITDNLRKSP CTQLCFATPG TQTPTCSCAR GVLKGRTCEE PDTYIMFSDG
2460 2470 2480 2490 2500
DKIIDVAIEP DVKASRPLKD PFPEISNLQT FDVDVNLRRV YFVVESPVGV
2510 2520 2530 2540 2550
NISWFSMNNA ENPRLVFGAS KQPHAKEIRH ISDMKLDWLT QKIYFTTGRG
2560 2570 2580 2590 2600
GKVMAIDTAG EHLSTIASGD WTYALAIDPC SGLLFWSDSG YKTSGGLYEP
2610 2620 2630 2640 2650
RIERSNLAGG SRKVIVSESI SLPAAIAVDF RNQKIYWADV NRLNIEVADY
2660 2670 2680 2690 2700
DGQNRKVIAS GYRAKSLDIW DRWLYMSDPL SNGVFRIDKE SGSGLENVVS
2710 2720 2730 2740 2750
DRRIPGALRV FASESDVRTR NQVCNALTSQ LCKTDNGGCD QLCTVVADDI
2760 2770 2780 2790 2800
GLAASKVQCS CNDTYELVQE PGKDYPTQCV LRGSNSEPAK ECLPPYNFQC
2810 2820 2830 2840 2850
GDGSCILLGA TCDSKPDCAD ASDENPNYCN TRSCPEDYNL CTNRRCIDSA
2860 2870 2880 2890 2900
KKCNHIDDCG DGSDELDCPS AVACAEGTFP CSNGHCINQT KVCDGHNDCH
2910 2920 2930 2940 2950
DEQVSDESLA TCPGLPIDCR GVKVRCPNTN ICIQPADLCD GYDDCGDKAD
2960 2970 2980 2990 3000
ENQLFCMNQQ CAQHYVRCPS GRCIPETWQC DGDNDCSDGW DETHTNCTDT
3010 3020 3030 3040 3050
AGKKICVGDY LFQCDNLKCI SRAFICDGED DCGDGSDEHS RHGCGNRTCT
3060 3070 3080 3090 3100
DQEFHCTSNA KLAQPKYECI PRAWLCDGDV TCAGGEDEST ELCKTEKKEC
3110 3120 3130 3140 3150
NKGEFRCSNQ HCIHSTWECD GDNDCLDGSD EHANCTYSSC QPDFFQCANH
3160 3170 3180 3190 3200
KCVPNSWKCD GNDDCEDGSD EKDCPKNSAS AQKASKCSNG QFQCTSGECI
3210 3220 3230 3240 3250
DDAKVCDRNF DCTDRSDESS LCFIDECSLA EKPLCEQKCM DMKIGYKCDC
3260 3270 3280 3290 3300
FEGFAIDISD QKSCHNVNEC YEGISGCSQK CDDKIGSYKC GCVDGYQLSS
3310 3320 3330 3340 3350
DDHSCKRTEM EPEPFFLLAN KHYIRKISID GNKYELAAQG FDNVVSLDID
3360 3370 3380 3390 3400
LTEKKAYLID QGKLRLLRVD LDEMDSPLSS YETVLRHNVY GTEGIAVDWV
3410 3420 3430 3440 3450
GRKLYMLNRQ ERSIRVCELD GRFCKTLIRD RIQQPKAIVV HPGKGYLFFT
3460 3470 3480 3490 3500
EWSLQPYIGR IALDGSPELQ DPIFKLAEHD LGWPNAIAID YFSDRLFWGD
3510 3520 3530 3540 3550
AHLNEIGFMD FDGNGRRHIP AQRTSHVSSM VVFDDYLYWA DWNLREVLRC
3560 3570 3580 3590 3600
DKWTGKNETI LKKTVQLPND LRIVHPMRQP AYPNPCGDNN GGCSHLCLIG
3610 3620 3630 3640 3650
AGGNGYTCSC PDQFVLLSDQ KTCEPNCTER QFACGGDDAK CIPKLWYCDG
3660 3670 3680 3690 3700
EPDCRDGSDE PGESICGQRI CPVGEFQCTN HNCTRPFQIC DGNDDCGDSS
3710 3720 3730 3740 3750
DEQNCDKACD PWMFKCAATG RCIPRRFTCD GDDDCGDRSD EADTLCMSAE
3760 3770 3780 3790 3800
RNCTAEEFRC NNNKCIAKAW RCDNDDDCGD GSDETPECAQ IECKKGWTRC
3810 3820 3830 3840 3850
SSSYRCIPNW AFCNGQDDCR DNSDEDKQRC PTCDDVGEFR CATSGKCIPR
3860 3870 3880 3890 3900
RWMCDTENDC GDNSDELDAS CGGTTRPCSE SEFRCNDGKC IPGSKVCDGT
3910 3920 3930 3940 3950
IQCSDGLDES QCTLRRCLPG HRQCDDGTCI AEHKWCDRKK DCPNAADELH
3960 3970 3980 3990 4000
CEDVSRRTCS PFEFECANSV CIPRKFMCDG DNDCGDNSDE TSSECRSAQC
4010 4020 4030 4040 4050
DPPLRFRCAH SRLCLNILQL CNGFNDCGPN DFSDEHLSMC SSFSEYGDCS
4060 4070 4080 4090 4100
SDQFKCANGK CVNGTVACDR KDDCGDASDE IGCSKHGGKT SCEAFGNNGG
4110 4120 4130 4140 4150
CKHICTDVRD GFYCHCRDGF RPDPQSPKEC IDIDECAGNN TCTQLCLNTK
4160 4170 4180 4190 4200
GSYLCRCHED YENNVVVGSM TGKDCRAKGD AANVMIGADD SLVQLSLHGS
4210 4220 4230 4240 4250
GTNRHAAAKA NDDDNDIIGI AFDPRKELMY WIDGSERTIY RSAIANGNQS
4260 4270 4280 4290 4300
HEGQKLDVDF AAMGVVPTAI AVDYTTGNLF IAAVSENIEN GLVTARKKRM
4310 4320 4330 4340 4350
SEPIDNQNTG FIFVCLPDGR YLKKIVAGHL QQPTALITAP SAGRICYSDA
4360 4370 4380 4390 4400
GLHAKIECAD MDGTHRQIIV KDLVFSPTSM AIDEGKGNRI YWVDPKYRRV
4410 4420 4430 4440 4450
DAVNIDGSER TTVVHDRHIP YAVDVFENHI YWLSRESKTL YVQDKFGRGR
4460 4470 4480 4490 4500
VSVLASDLED GHTVRVSQKY AKDTQRTVSG CERAQCSHLC VSLPSTGFAC
4510 4520 4530 4540 4550
LCPDGIVPQL DGSCATQHVE ALTMPKQCKC TNGGKCRLDG SCECTSDFEG
4560 4570 4580 4590 4600
DQCEKESSVS RKIIGTLSEN FITVLLYILA FLFAFGLIGF CALNLYKRRQ
4610 4620 4630 4640 4650
LLFKKNEAAD GSVSFHGNVI SFSNPVLENK QDAPGSEFNM QQMTSMHDDS
4660 4670 4680 4690 4700
TTFTNPVYEL EDVDMSSPPP SNDQPSTSAS AMSPNRPSTS AASSFVPPTF
4710 4720 4730 4740 4750
DQDEIELKTA DEIIVPKAEI SKPPIPARPK KEKADPLRVD NPLYDPDSEV

SDV
Length:4,753
Mass (Da):526,425
Last modified:October 1, 1996 - v1
Checksum:iCCFC40E397B8D4FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96150 Genomic DNA. Translation: AAA28105.1.
Z73907 Genomic DNA. Translation: CAA98124.1.
PIRiA47437.
RefSeqiNP_492127.1. NM_059726.5.
UniGeneiCel.18450.

Genome annotation databases

EnsemblMetazoaiF29D11.1; F29D11.1; WBGene00003071.
GeneIDi172520.
KEGGicel:CELE_F29D11.1.
UCSCiF29D11.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96150 Genomic DNA. Translation: AAA28105.1.
Z73907 Genomic DNA. Translation: CAA98124.1.
PIRiA47437.
RefSeqiNP_492127.1. NM_059726.5.
UniGeneiCel.18450.

3D structure databases

ProteinModelPortaliQ04833.
SMRiQ04833.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi37962. 7 interactors.
STRINGi6239.F29D11.1.

PTM databases

iPTMnetiQ04833.

Proteomic databases

EPDiQ04833.
PaxDbiQ04833.
PeptideAtlasiQ04833.
PRIDEiQ04833.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF29D11.1; F29D11.1; WBGene00003071.
GeneIDi172520.
KEGGicel:CELE_F29D11.1.
UCSCiF29D11.1. c. elegans.

Organism-specific databases

CTDi172520.
WormBaseiF29D11.1; CE05765; WBGene00003071; lrp-1.

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
ENOG410XP34. LUCA.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000230574.
InParanoidiQ04833.
KOiK06233.
OMAiTRPPGMC.
OrthoDBiEOG091G000N.
PhylomeDBiQ04833.

Enzyme and pathway databases

ReactomeiR-CEL-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-CEL-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

PROiQ04833.

Gene expression databases

BgeeiWBGene00003071.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 29 hits.
PF00058. Ldl_recept_b. 8 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 21 hits.
SM00179. EGF_CA. 8 hits.
SM00192. LDLa. 35 hits.
SM00135. LY. 32 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 6 hits.
SSF57424. SSF57424. 33 hits.
PROSITEiPS00010. ASX_HYDROXYL. 6 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 28 hits.
PS50068. LDLRA_2. 34 hits.
PS51120. LDLRB. 30 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLRP_CAEEL
AccessioniPrimary (citable) accession number: Q04833
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.