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Lipolysis-stimulated lipoprotein receptor (Lipolysis-stimulated receptor) (Liver-specific bHLH-Zip transcription factor) (Liver-specific gene on mouse chromosome 7 protein)

 LSR_MOUSE               Reviewed;         594 AA.
Q99KG5; Q3TJE7; Q3UIQ9; Q61148; Q61149; Q6U816;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 131.
RecName: Full=Lipolysis-stimulated lipoprotein receptor;
AltName: Full=Lipolysis-stimulated receptor;
AltName: Full=Liver-specific bHLH-Zip transcription factor;
AltName: Full=Liver-specific gene on mouse chromosome 7 protein;
Flags: Precursor;
Name=Lsr; Synonyms=Lisch7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 256-594.
STRAIN=C57BL/6 X CBA;
Lin Q., Ooi K.S., Sawadogo M.;
"Lisch7, a liver-specific gene immediately upstream of the USF2 gene
on mouse chromosome 7.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Amnion, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-576, FUNCTION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
STRAIN=129/Ola;
PubMed=15265030; DOI=10.1111/j.1432-1033.2004.04223.x;
Mesli S., Javorschi S., Berard A.M., Landry M., Priddle H.,
Kivlichan D., Smith A.J.H., Yen F.T., Bihain B.E., Darmon M.;
"Distribution of the lipolysis stimulated receptor in adult and
embryonic murine tissues and lethality of LSR-/- embryos at 12.5 to
14.5 days of gestation.";
Eur. J. Biochem. 271:3103-3114(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-588, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND SER-379, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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). {ECO:0000250,
ECO:0000269|PubMed:15265030}.
-!- SUBUNIT: Homotrimer or homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99KG5-1; Sequence=Displayed;
Name=2;
IsoId=Q99KG5-2; Sequence=VSP_019696;
Name=3;
IsoId=Q99KG5-3; Sequence=VSP_019695;
-!- TISSUE SPECIFICITY: Specifically expressed in liver and to a lower
extent in kidney (at protein level). Also detected in brain,
testis, ovaries, adrenal gland, intestine, muscle, and lung.
{ECO:0000269|PubMed:15265030}.
-!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (at protein
level). Detected from E7.5 to E17. {ECO:0000269|PubMed:15265030}.
-!- DISRUPTION PHENOTYPE: Death between E12.5 and E15.5 probably due
to impaired liver and embryonic development.
{ECO:0000269|PubMed:15265030}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA92719.1; Type=Frameshift; Positions=2; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U49507; AAA92719.1; ALT_FRAME; mRNA.
EMBL; U49508; AAA92720.1; -; Genomic_DNA.
EMBL; AK146807; BAE27447.1; -; mRNA.
EMBL; AK167463; BAE39548.1; -; mRNA.
EMBL; BC004672; AAH04672.1; -; mRNA.
EMBL; AY376636; AAQ83379.1; -; Genomic_DNA.
CCDS; CCDS21119.1; -. [Q99KG5-1]
CCDS; CCDS52185.1; -. [Q99KG5-3]
CCDS; CCDS52186.1; -. [Q99KG5-2]
RefSeq; NP_001157656.1; NM_001164184.1. [Q99KG5-2]
RefSeq; NP_001157657.1; NM_001164185.1. [Q99KG5-3]
RefSeq; NP_059101.1; NM_017405.2. [Q99KG5-1]
UniGene; Mm.4067; -.
ProteinModelPortal; Q99KG5; -.
BioGrid; 207572; 1.
IntAct; Q99KG5; 2.
MINT; Q99KG5; -.
iPTMnet; Q99KG5; -.
PhosphoSitePlus; Q99KG5; -.
SwissPalm; Q99KG5; -.
PaxDb; Q99KG5; -.
PeptideAtlas; Q99KG5; -.
PRIDE; Q99KG5; -.
Ensembl; ENSMUST00000001279; ENSMUSP00000001279; ENSMUSG00000001247. [Q99KG5-1]
Ensembl; ENSMUST00000098553; ENSMUSP00000096153; ENSMUSG00000001247. [Q99KG5-3]
Ensembl; ENSMUST00000108116; ENSMUSP00000103751; ENSMUSG00000001247. [Q99KG5-2]
Ensembl; ENSMUST00000205961; ENSMUSP00000146120; ENSMUSG00000001247. [Q99KG5-1]
GeneID; 54135; -.
KEGG; mmu:54135; -.
UCSC; uc009ghj.2; mouse. [Q99KG5-1]
UCSC; uc009ghk.2; mouse. [Q99KG5-2]
UCSC; uc009ghl.2; mouse. [Q99KG5-3]
CTD; 51599; -.
MGI; MGI:1927471; Lsr.
eggNOG; ENOG410IKMJ; Eukaryota.
eggNOG; ENOG411004A; LUCA.
GeneTree; ENSGT00430000030906; -.
HOGENOM; HOG000253962; -.
HOVERGEN; HBG061576; -.
InParanoid; Q99KG5; -.
OMA; DWRSRPS; -.
OrthoDB; EOG091G0875; -.
PhylomeDB; Q99KG5; -.
TreeFam; TF330877; -.
PRO; PR:Q99KG5; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000001247; -.
CleanEx; MM_LSR; -.
ExpressionAtlas; Q99KG5; baseline and differential.
Genevisible; Q99KG5; MM.
GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0061689; C:tricellular tight junction; IDA:UniProtKB.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0030228; F:lipoprotein particle receptor activity; TAS:HGNC.
GO; GO:0030169; F:low-density lipoprotein particle binding; TAS:HGNC.
GO; GO:0060856; P:establishment of blood-brain barrier; IMP:UniProtKB.
GO; GO:0042953; P:lipoprotein transport; TAS:HGNC.
GO; GO:0001889; P:liver development; IMP:HGNC.
GO; GO:0061833; P:protein localization to tricellular tight junction; IDA:MGI.
GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI.
GO; GO:1904274; P:tricellular tight junction assembly; IMP:UniProtKB.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR003599; Ig_sub.
InterPro; IPR008664; LISCH7.
Pfam; PF05624; LSR; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 2.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Chylomicron; Complete proteome;
Disulfide bond; Immunoglobulin domain; LDL; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix; VLDL.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 594 Lipolysis-stimulated lipoprotein
receptor.
/FTId=PRO_0000245309.
TOPO_DOM 36 206 Extracellular. {ECO:0000255}.
TRANSMEM 207 227 Helical. {ECO:0000255}.
TOPO_DOM 228 594 Cytoplasmic. {ECO:0000255}.
DOMAIN 89 181 Ig-like V-type.
COMPBIAS 227 251 Cys-rich.
MOD_RES 283 283 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WU74}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 396 396 Phosphothreonine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 478 478 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000250|UniProtKB:Q86X29}.
DISULFID 113 165 {ECO:0000250}.
VAR_SEQ 187 255 GRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLFFLLLGIC
WCQCCPHTCCCYVRCPCCPDKCCCPEAL -> V (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019695.
VAR_SEQ 187 205 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019696.
CONFLICT 423 423 P -> T (in Ref. 1; AAA92720).
{ECO:0000305}.
CONFLICT 456 456 P -> H (in Ref. 2; BAE39548).
{ECO:0000305}.
CONFLICT 579 579 R -> L (in Ref. 1; AAA92720).
{ECO:0000305}.
SEQUENCE 594 AA; 66108 MW; 2ADE28BB870A001D CRC64;
MAPAASACAG APGSHPATTI FVCLFLIIYC PDRASAIQVT VPDPYHVVIL FQPVTLHCTY
QMSNTLTAPI VIWKYKSFCR DRVADAFSPA SVDNQLNAQL AAGNPGYNPY VECQDSVRTV
RVVATKQGNA VTLGDYYQGR RITITGNADL TFEQTAWGDS GVYYCSVVSA QDLDGNNEAY
AELIVLGRTS EAPELLPGFR AGPLEDWLFV VVVCLASLLF FLLLGICWCQ CCPHTCCCYV
RCPCCPDKCC CPEALYAAGK AATSGVPSIY APSIYTHLSP AKTPPPPPAM IPMRPPYGYP
GDFDRTSSVG GHSSQVPLLR EVDGSVSSEV RSGYRIQANQ QDDSMRVLYY MEKELANFDP
SRPGPPNGRV ERAMSEVTSL HEDDWRSRPS RAPALTPIRD EEWNRHSPRS PRTWEQEPLQ
EQPRGGWGSG RPRARSVDAL DDINRPGSTE SGRSSPPSSG RRGRAYAPPR SRSRDDLYDP
DDPRDLPHSR DPHYYDDLRS RDPRADPRSR QRSHDPRDAG FRSRDPQYDG RLLEEALKKK
GAGERRRVYR EEEEEEEEGH YPPAPPPYSE TDSQASRERR MKKNLALSRE SLVV


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