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Protein

Low-density lipoprotein receptor-related protein 10

Gene

Lrp10

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

Functioni

Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver.1 Publication

GO - Molecular functioni

  • low-density lipoprotein receptor activity Source: MGI

GO - Biological processi

  • inner ear development Source: MGI
  • lipid metabolic process Source: MGI
  • lipid transport Source: MGI
  • receptor-mediated endocytosis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 10
Short name:
LRP-10
Gene namesi
Name:Lrp10
Synonyms:Lrp9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1929480. Lrp10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 441424ExtracellularSequence analysisAdd
BLAST
Transmembranei442 – 46221HelicalSequence analysisAdd
BLAST
Topological domaini463 – 713251CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • coated pit Source: UniProtKB-SubCell
  • integral component of membrane Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 713696Low-density lipoprotein receptor-related protein 10PRO_0000017336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 58By similarity
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi81 ↔ 99By similarity
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi141 ↔ 153By similarity
Disulfide bondi148 ↔ 166By similarity
Disulfide bondi160 ↔ 175By similarity
Disulfide bondi193 ↔ 221By similarity
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Disulfide bondi309 ↔ 332By similarity
Disulfide bondi316 ↔ 345By similarity
Disulfide bondi339 ↔ 354By similarity
Disulfide bondi357 ↔ 375By similarity
Disulfide bondi364 ↔ 388By similarity
Disulfide bondi382 ↔ 397By similarity
Disulfide bondi400 ↔ 412By similarity
Disulfide bondi407 ↔ 425By similarity
Disulfide bondi419 ↔ 434By similarity
Modified residuei596 – 5961PhosphothreonineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ7TQH7.
MaxQBiQ7TQH7.
PaxDbiQ7TQH7.
PRIDEiQ7TQH7.

PTM databases

iPTMnetiQ7TQH7.
PhosphoSiteiQ7TQH7.

Expressioni

Tissue specificityi

Highly expressed in heart, lung, liver and liver. Expressed at low level in brain and spleen. Weakly or not expressed in testis and skeletal muscle. In liver, it is expressed in hepatocytes and at higher level in sinusoidal lining. In the kidney, it is expressed in peritubular capillaries. In brain, it is expressed in the epithelium of the choroid plexus ependymal cells of the third ventricle pia matter, and to lesser extent in hippocampal fields CA2 and CA3.1 Publication

Gene expression databases

BgeeiQ7TQH7.
GenevisibleiQ7TQH7. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022782.

Structurei

3D structure databases

ProteinModelPortaliQ7TQH7.
SMRiQ7TQH7. Positions 329-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 137109CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 17637LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 306114CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini308 – 35548LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini356 – 39843LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 43537LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi546 – 58035Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 4 LDL-receptor class A domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPT0. Eukaryota.
ENOG410XV08. LUCA.
GeneTreeiENSGT00810000125405.
HOGENOMiHOG000013017.
HOVERGENiHBG049162.
InParanoidiQ7TQH7.
KOiK20050.
OMAiYQTFCAD.
OrthoDBiEOG7PCJG4.
TreeFamiTF332149.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
4.10.400.10. 4 hits.
InterProiIPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF00431. CUB. 1 hit.
PF00057. Ldl_recept_a. 2 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00042. CUB. 2 hits.
SM00192. LDLa. 4 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF57424. SSF57424. 2 hits.
PROSITEiPS01180. CUB. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7TQH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSALPLLFL LLGGALARPD RITFPRSACE APPAVLSEVQ GTLQRPLGRD
60 70 80 90 100
SRSSPANCTW VILGSKDQTV TVRFQKLHLA CGSEHLILHS PLQPPISLCE
110 120 130 140 150
APSGPLQLPG GNVTITYSYA GARAPMGQGF LLTYSQDWLL CLQEEFQCLN
160 170 180 190 200
HRCIPAAQRC DGIDACGDGS DEAGCSSDPF PNLNPAPAPT LACNLTLEDF
210 220 230 240 250
YGVFSSPGYS HLASVSHPQS CLWLLDPHDG RRLAVRFTAL DLSYGDAVHV
260 270 280 290 300
YDGAGPPETP RLLRSLTHFS NGKAVTVETL SGQAVVSYHT VAWSSGRGFN
310 320 330 340 350
ATYHVRGYCL PWDRPCGLGS GLGASENLGE RCYSEAQRCD GSWDCADGTD
360 370 380 390 400
EEGCPGCPPG HFPCGAAGTP GATACYLPAD RCNYQTFCAD GADERRCRHC
410 420 430 440 450
QPGNFRCRDE KCVYETWVCD GQPDCTDGSD EWDCSYALPR KVITAAVIGS
460 470 480 490 500
LVCGLLLVIA LGCTCKLYAI RTQEYSIFAP LSRMEAEIVQ QQAPPSYGQL
510 520 530 540 550
IAQGAIPPVE DFPTENPNDN SVLGNLRSLL QILRQDMTPG GTSGGRRRQR
560 570 580 590 600
GRSIRRLVRR LRRWGLLPRT NTPARAPETR SQVTPSVPSE ALDDSTGQAC
610 620 630 640 650
EGGAVGGQDG EQAPPLPIKT PIPTPSTLPA LATVSEPPGP LPSVPVESSL
660 670 680 690 700
LSGVVQVLRG RLLPSLWSPG PTWTQTGTHT TVLSPEDEDD VLLLPLAEPE
710
VWVVEAEDEP LLA
Length:713
Mass (Da):76,461
Last modified:July 27, 2011 - v2
Checksum:i27B2B2D44E9AB6E1
GO

Sequence cautioni

The sequence AAH11058.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti554 – 5541I → V in BAB20775 (PubMed:11123907).Curated
Sequence conflicti554 – 5541I → V in AAH54447 (PubMed:15489334).Curated
Sequence conflicti598 – 5981Q → H in BAB20775 (PubMed:11123907).Curated
Sequence conflicti637 – 6371P → T in BAB20775 (PubMed:11123907).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042200 mRNA. Translation: BAB20775.1.
AK144035 mRNA. Translation: BAE25667.1.
BC011058 mRNA. Translation: AAH11058.1. Different initiation.
BC052378 mRNA. Translation: AAH52378.1.
BC054447 mRNA. Translation: AAH54447.1.
CCDSiCCDS27089.1.
RefSeqiNP_075369.2. NM_022993.3.
UniGeneiMm.472719.

Genome annotation databases

EnsembliENSMUST00000022782; ENSMUSP00000022782; ENSMUSG00000022175.
GeneIDi65107.
KEGGimmu:65107.
UCSCiuc007twd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042200 mRNA. Translation: BAB20775.1.
AK144035 mRNA. Translation: BAE25667.1.
BC011058 mRNA. Translation: AAH11058.1. Different initiation.
BC052378 mRNA. Translation: AAH52378.1.
BC054447 mRNA. Translation: AAH54447.1.
CCDSiCCDS27089.1.
RefSeqiNP_075369.2. NM_022993.3.
UniGeneiMm.472719.

3D structure databases

ProteinModelPortaliQ7TQH7.
SMRiQ7TQH7. Positions 329-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022782.

PTM databases

iPTMnetiQ7TQH7.
PhosphoSiteiQ7TQH7.

Proteomic databases

EPDiQ7TQH7.
MaxQBiQ7TQH7.
PaxDbiQ7TQH7.
PRIDEiQ7TQH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022782; ENSMUSP00000022782; ENSMUSG00000022175.
GeneIDi65107.
KEGGimmu:65107.
UCSCiuc007twd.1. mouse.

Organism-specific databases

CTDi26020.
MGIiMGI:1929480. Lrp10.

Phylogenomic databases

eggNOGiENOG410IPT0. Eukaryota.
ENOG410XV08. LUCA.
GeneTreeiENSGT00810000125405.
HOGENOMiHOG000013017.
HOVERGENiHBG049162.
InParanoidiQ7TQH7.
KOiK20050.
OMAiYQTFCAD.
OrthoDBiEOG7PCJG4.
TreeFamiTF332149.

Miscellaneous databases

ChiTaRSiLrp10. mouse.
PROiQ7TQH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TQH7.
GenevisibleiQ7TQH7. MM.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
4.10.400.10. 4 hits.
InterProiIPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF00431. CUB. 1 hit.
PF00057. Ldl_recept_a. 2 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00042. CUB. 2 hits.
SM00192. LDLa. 4 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF57424. SSF57424. 2 hits.
PROSITEiPS01180. CUB. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel low-density lipoprotein receptor-related protein mediating cellular uptake of apolipoprotein E-enriched beta-VLDL in vitro."
    Sugiyama T., Kumagai H., Morikawa Y., Wada Y., Sugiyama A., Yasuda K., Yokoi N., Tamura S., Kojima T., Nosaka T., Senba E., Kimura S., Kadowaki T., Kodama T., Kitamura T.
    Biochemistry 39:15817-15825(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Lymphocyte.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain, Colon and Mammary tumor.

Entry informationi

Entry nameiLRP10_MOUSE
AccessioniPrimary (citable) accession number: Q7TQH7
Secondary accession number(s): Q3UNT0
, Q7TS95, Q921T0, Q9EPE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 116 of the entry and version 2 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.