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Q7Z4F1 (LRP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low-density lipoprotein receptor-related protein 10

Short name=LRP-10
Gene names
Name:LRP10
ORF Names:MSTP087, SP220, UNQ389/PRO724
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Membranecoated pit By similarity.

Tissue specificity

Expressed in blood leukocyte, lung, placenta, small intestine, liver, kidney, spleen, thymus, colon, skeletal muscle and heart. Ref.10

Sequence similarities

Belongs to the LDLR family.

Contains 2 CUB domains.

Contains 4 LDL-receptor class A domains.

Sequence caution

The sequence AAD20037.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG17980.1 differs from that shown. Reason: Frameshift at positions 370 and 700.

The sequence AAQ13610.1 differs from that shown. Reason: Frameshift at positions 312, 337, 496, 502 and 512.

The sequence CAD39174.2 differs from that shown. Reason: Chimera.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCoated pit
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcoated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z4F1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7Z4F1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     557-713: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 713697Low-density lipoprotein receptor-related protein 10
PRO_0000017335

Regions

Topological domain17 – 440424Extracellular Potential
Transmembrane441 – 46121Helical; Potential
Topological domain462 – 713252Cytoplasmic Potential
Domain28 – 136109CUB 1
Domain139 – 17537LDL-receptor class A 1
Domain192 – 305114CUB 2
Domain307 – 35448LDL-receptor class A 2
Domain355 – 39743LDL-receptor class A 3
Domain398 – 43437LDL-receptor class A 4
Compositional bias545 – 57935Arg-rich
Compositional bias614 – 67865Pro-rich

Amino acid modifications

Modified residue5961Phosphothreonine Ref.12
Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 57 By similarity
Disulfide bond80 ↔ 98 By similarity
Disulfide bond140 ↔ 152 By similarity
Disulfide bond147 ↔ 165 By similarity
Disulfide bond159 ↔ 174 By similarity
Disulfide bond192 ↔ 220 By similarity
Disulfide bond308 ↔ 331 By similarity
Disulfide bond315 ↔ 344 By similarity
Disulfide bond338 ↔ 353 By similarity
Disulfide bond356 ↔ 374 By similarity
Disulfide bond363 ↔ 387 By similarity
Disulfide bond381 ↔ 396 By similarity
Disulfide bond399 ↔ 411 By similarity
Disulfide bond406 ↔ 424 By similarity
Disulfide bond418 ↔ 433 By similarity

Natural variations

Alternative sequence557 – 713157Missing in isoform 2.
VSP_009820
Natural variant481R → W.
Corresponds to variant rs2273837 [ dbSNP | Ensembl ].
VAR_018172
Natural variant1391M → V.
Corresponds to variant rs28534929 [ dbSNP | Ensembl ].
VAR_034097

Experimental info

Sequence conflict3651A → T Ref.8
Sequence conflict4341S → C Ref.8
Sequence conflict5581R → H in CAB45753. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: A463FB5584322220

FASTA71376,193
        10         20         30         40         50         60 
MLLATLLLLL LGGALAHPDR IIFPNHACED PPAVLLEVQG TLQRPLVRDS RTSPANCTWL 

        70         80         90        100        110        120 
ILGSKEQTVT IRFQKLHLAC GSERLTLRSP LQPLISLCEA PPSPLQLPGG NVTITYSYAG 

       130        140        150        160        170        180 
ARAPMGQGFL LSYSQDWLMC LQEEFQCLNH RCVSAVQRCD GVDACGDGSD EAGCSSDPFP 

       190        200        210        220        230        240 
GLTPRPVPSL PCNVTLEDFY GVFSSPGYTH LASVSHPQSC HWLLDPHDGR RLAVRFTALD 

       250        260        270        280        290        300 
LGFGDAVHVY DGPGPPESSR LLRSLTHFSN GKAVTVETLS GQAVVSYHTV AWSNGRGFNA 

       310        320        330        340        350        360 
TYHVRGYCLP WDRPCGLGSG LGAGEGLGER CYSEAQRCDG SWDCADGTDE EDCPGCPPGH 

       370        380        390        400        410        420 
FPCGAAGTSG ATACYLPADR CNYQTFCADG ADERRCRHCQ PGNFRCRDEK CVYETWVCDG 

       430        440        450        460        470        480 
QPDCADGSDE WDCSYVLPRK VITAAVIGSL VCGLLLVIAL GCTCKLYAIR TQEYSIFAPL 

       490        500        510        520        530        540 
SRMEAEIVQQ QAPPSYGQLI AQGAIPPVED FPTENPNDNS VLGNLRSLLQ ILRQDMTPGG 

       550        560        570        580        590        600 
GPGARRRQRG RLMRRLVRRL RRWGLLPRTN TPARASEARS QVTPSAAPLE ALDGGTGPAR 

       610        620        630        640        650        660 
EGGAVGGQDG EQAPPLPIKA PLPSASTSPA PTTVPEAPGP LPSLPLEPSL LSGVVQALRG 

       670        680        690        700        710 
RLLPSLGPPG PTRSPPGPHT AVLALEDEDD VLLVPLAEPG VWVAEAEDEP LLT 

« Hide

Isoform 2 [UniParc].

Checksum: 1CCA7CAEA16A0AB1
Show »

FASTA55660,213

References

« Hide 'large scale' references
[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Cervix carcinoma.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-713 (ISOFORM 2).
Tissue: Lung.
[7]Lu H., Liu B.H., Qin B.M., Sheng H., Zhang Q., Liu Y.Q., Zhao B., Liu B., Wang X.Y., Song L., Ji X.J., Xu H.S., Chen J.Z., Zheng W.Y., Teng C.Y., Liu Q., Yu L.T., Lin J. expand/collapse author list , Gong J., Gao R.L., Hui R.T.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-713 (ISOFORM 1).
Tissue: Aorta.
[8]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 329-713 (ISOFORM 1).
[9]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-713 (ISOFORM 1).
Tissue: Brain.
[10]"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: TISSUE SPECIFICITY.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY358399 mRNA. Translation: AAQ88765.1.
BX161500 mRNA. Translation: CAD61944.1.
AK291030 mRNA. Translation: BAF83719.1.
AL080164 mRNA. Translation: CAB45753.1.
AL834518 mRNA. Translation: CAD39174.2. Sequence problems.
CH471078 Genomic DNA. Translation: EAW66232.1.
CH471078 Genomic DNA. Translation: EAW66235.1.
BC064901 mRNA. Translation: AAH64901.1.
BC113714 mRNA. Translation: AAI13715.1.
BC113716 mRNA. Translation: AAI13717.1.
AF172816 mRNA. Translation: AAQ13610.1. Frameshift.
AF177336 mRNA. Translation: AAG17980.1. Frameshift.
AF131760 mRNA. Translation: AAD20037.1. Different initiation.
PIRT12469.
RefSeqNP_054764.2. NM_014045.3.
UniGeneHs.525232.

3D structure databases

ProteinModelPortalQ7Z4F1.
SMRQ7Z4F1. Positions 25-136, 138-176, 199-305, 323-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117491. 1 interaction.
IntActQ7Z4F1. 1 interaction.
STRING9606.ENSP00000352601.

PTM databases

PhosphoSiteQ7Z4F1.

Polymorphism databases

DMDM46396347.

Proteomic databases

PaxDbQ7Z4F1.
PRIDEQ7Z4F1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359591; ENSP00000352601; ENSG00000197324. [Q7Z4F1-1]
ENST00000546834; ENSP00000447559; ENSG00000197324. [Q7Z4F1-2]
GeneID26020.
KEGGhsa:26020.
UCSCuc001whd.3. human. [Q7Z4F1-1]

Organism-specific databases

CTD26020.
GeneCardsGC14P023340.
HGNCHGNC:14553. LRP10.
HPAHPA000932.
MIM609921. gene.
neXtProtNX_Q7Z4F1.
PharmGKBPA38383.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312857.
HOVERGENHBG049162.
InParanoidQ7Z4F1.
OMAEDFYGVF.
OrthoDBEOG7PCJG4.
PhylomeDBQ7Z4F1.
TreeFamTF332149.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ7Z4F1.
BgeeQ7Z4F1.
CleanExHS_LRP10.
GenevestigatorQ7Z4F1.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
4.10.400.10. 4 hits.
InterProIPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF00431. CUB. 1 hit.
PF00057. Ldl_recept_a. 2 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00042. CUB. 2 hits.
SM00192. LDLa. 4 hits.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF57424. SSF57424. 2 hits.
PROSITEPS01180. CUB. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLRP10. human.
GeneWikiLRP10.
GenomeRNAi26020.
NextBio47794.
PROQ7Z4F1.
SOURCESearch...

Entry information

Entry nameLRP10_HUMAN
AccessionPrimary (citable) accession number: Q7Z4F1
Secondary accession number(s): A8K4R5 expand/collapse secondary AC list , D3DS31, O95882, Q14CK7, Q86T02, Q8NCZ4, Q9HC42, Q9UG33
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: March 19, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM