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Q86X29 (LSR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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:
Lipolysis-stimulated lipoprotein receptor
Gene names
Name:LSR
Synonyms:LISCH
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells By similarity.

Subunit structure

Homotrimer or homotetramer By similarity.

Subcellular location

Cell membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the immunoglobulin superfamily. LISCH7 family.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Caution

In contrast to the rodent orthologous protein, it is longer in N-terminus and no signal sequence is detected by any prediction method.

Sequence caution

The sequence AAB51178.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAB58317.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86X29-1)

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: Q86X29-2)

The sequence of this isoform differs from the canonical sequence as follows:
     52-88: Missing.
     366-386: Missing.
Isoform 3 (identifier: Q86X29-3)

The sequence of this isoform differs from the canonical sequence as follows:
     240-258: Missing.
     386-386: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 649649Lipolysis-stimulated lipoprotein receptor
PRO_0000245308

Regions

Topological domain1 – 259259Extracellular Potential
Transmembrane260 – 28021Helical; Potential
Topological domain281 – 649369Cytoplasmic Potential
Domain86 – 234149Ig-like V-type
Compositional bias280 – 30425Cys-rich

Amino acid modifications

Modified residue1851Phosphothreonine By similarity
Modified residue3091Phosphotyrosine Ref.6
Modified residue3281Phosphotyrosine Ref.6
Modified residue3641Phosphoserine By similarity
Modified residue3721Phosphotyrosine Ref.12
Modified residue4061Phosphotyrosine Ref.6 Ref.12
Modified residue4361Phosphoserine By similarity
Modified residue4931Phosphoserine Ref.9
Modified residue5281Phosphoserine Ref.7
Modified residue5301Phosphoserine Ref.7 Ref.10
Modified residue5351Phosphotyrosine Ref.6
Modified residue5511Phosphotyrosine Ref.6 Ref.8
Modified residue5861Phosphotyrosine Ref.6 Ref.8
Modified residue6151Phosphotyrosine Ref.6
Modified residue6431Phosphoserine Ref.11 Ref.13
Modified residue6461Phosphoserine Ref.5 Ref.11
Disulfide bond111 ↔ 218 By similarity

Natural variations

Alternative sequence52 – 8837Missing in isoform 2.
VSP_019691
Alternative sequence240 – 25819Missing in isoform 3.
VSP_019692
Alternative sequence366 – 38621Missing in isoform 2.
VSP_019693
Alternative sequence3861Missing in isoform 3.
VSP_019694
Natural variant3631S → N. Ref.2
Corresponds to variant rs34259399 [ dbSNP | Ensembl ].
VAR_049902

Experimental info

Sequence conflict2591D → G in AAB51178. Ref.3
Sequence conflict3081L → R in AAB51178. Ref.3
Sequence conflict4301A → G in AAB51178. Ref.3
Sequence conflict5181G → GR in BAC86714. Ref.2
Sequence conflict6391N → D in AAB51178. Ref.3

Sequences

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

Last modified October 17, 2006. Version 4.
Checksum: 01E8F1CE0197CE9B

FASTA64971,439
        10         20         30         40         50         60 
MQQDGLGVGT RNGSGKGRSV HPSWPWCAPR PLRYFGRDAR ARRAQTAAMA LLAGGLSRGL 

        70         80         90        100        110        120 
GSHPAAAGRD AVVFVWLLLS TWCTAPARAI QVTVSNPYHV VILFQPVTLP CTYQMTSTPT 

       130        140        150        160        170        180 
QPIVIWKYKS FCRDRIADAF SPASVDNQLN AQLAAGNPGY NPYVECQDSV RTVRVVATKQ 

       190        200        210        220        230        240 
GNAVTLGDYY QGRRITITGN ADLTFDQTAW GDSGVYYCSV VSAQDLQGNN EAYAELIVLG 

       250        260        270        280        290        300 
RTSGVAELLP GFQAGPIEDW LFVVVVCLAA FLIFLLLGIC WCQCCPHTCC CYVRCPCCPD 

       310        320        330        340        350        360 
KCCCPEALYA AGKAATSGVP SIYAPSTYAH LSPAKTPPPP AMIPMGPAYN GYPGGYPGDV 

       370        380        390        400        410        420 
DRSSSAGGQG SYVPLLRDTD SSVASEVRSG YRIQASQQDD SMRVLYYMEK ELANFDPSRP 

       430        440        450        460        470        480 
GPPSGRVERA MSEVTSLHED DWRSRPSRGP ALTPIRDEEW GGHSPRSPRG WDQEPAREQA 

       490        500        510        520        530        540 
GGGWRARRPR ARSVDALDDL TPPSTAESGS RSPTSNGGRS RAYMPPRSRS RDDLYDQDDS 

       550        560        570        580        590        600 
RDFPRSRDPH YDDFRSRERP PADPRSHHHR TRDPRDNGSR SGDLPYDGRL LEEAVRKKGS 

       610        620        630        640 
EERRRPHKEE EEEAYYPPAP PPYSETDSQA SRERRLKKNL ALSRESLVV

« Hide

Isoform 2 [UniParc].

Checksum: E254FA92B362D418
Show »

FASTA59165,587
Isoform 3 [UniParc].

Checksum: 32D531E33D09464E
Show »

FASTA62969,429

References

« Hide 'large scale' references
[1]"Cloning and functional analysis of LISCH."
Teramoto T., Thorgeirsson S.S.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ASN-363.
Tissue: Amygdala.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[6]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309; TYR-328; TYR-406; TYR-535; TYR-551; TYR-586 AND TYR-615, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[7]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-551 AND TYR-586, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, MASS SPECTROMETRY.
Tissue: Liver.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-646, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-372 AND TYR-406, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF130366 mRNA. Translation: AAD22101.1.
AK126834 mRNA. Translation: BAC86714.1.
AC002128 Genomic DNA. Translation: AAB58317.1. Sequence problems.
AD000684 Genomic DNA. Translation: AAB51178.1. Sequence problems.
BC047376 mRNA. Translation: AAH47376.2.
IPIIPI00328218.
IPI00409640.
IPI00641640.
RefSeqNP_057009.3. NM_015925.5.
NP_991403.1. NM_205834.2.
NP_991404.1. NM_205835.2.
UniGeneHs.466507.

3D structure databases

ProteinModelPortalQ86X29.
SMRQ86X29. Positions 199-240.
ModBaseSearch...

Protein-protein interaction databases

IntActQ86X29. 3 interactions.
MINTMINT-5000691.
STRINGQ86X29.

PTM databases

PhosphoSiteQ86X29.

Polymorphism databases

DMDM116242622.

Proteomic databases

PRIDEQ86X29.

Protocols and materials databases

DNASU51599.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361790; ENSP00000354575; ENSG00000105699.
GeneID51599.
KEGGhsa:51599.
UCSCuc002nyl.3. human.
uc002nyo.3. human.
uc002nyp.3. human.

Organism-specific databases

CTD51599.
GeneCardsGC19P035739.
H-InvDBHIX0015024.
HGNCHGNC:29572. LSR.
HPAHPA007270.
neXtProtNX_Q86X29.
PharmGKBPA142671504.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72582.
GeneTreeENSGT00430000030906.
HOGENOMHOG000253962.
HOVERGENHBG061576.
InParanoidQ86X29.
OMAWRSRPSR.
PhylomeDBQ86X29.

Gene expression databases

ArrayExpressQ86X29.
BgeeQ86X29.
CleanExHS_LSR.
GenevestigatorQ86X29.
GermOnlineENSG00000105699. Homo sapiens.

Family and domain databases

Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR008664. LISCH7.
[Graphical view]
PfamPF05624. LSR. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio55459.

Entry information

Entry nameLSR_HUMAN
AccessionPrimary (citable) accession number: Q86X29
Secondary accession number(s): O00112 expand/collapse secondary AC list , O00426, Q6ZT80, Q9UQL3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 17, 2006
Last modified: May 16, 2012
This is version 95 of the entry and version 4 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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents