LSR_RAT
ID LSR_RAT Reviewed; 593 AA.
AC Q9WU74; Q497B9; Q9WU75; Q9WU76;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Lipolysis-stimulated lipoprotein receptor {ECO:0000305};
DE AltName: Full=Lipolysis-stimulated remnant receptor;
DE Flags: Precursor;
GN Name=Lsr {ECO:0000312|RGD:69236}; Synonyms=Lisch7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10224102; DOI=10.1074/jbc.274.19.13390;
RA Yen F.T., Masson M., Clossais-Besnard N., Andre P., Grosset J.-M.,
RA Bougueleret L., Dumas J.-B., Guerassimenko O., Bihain B.E.;
RT "Molecular cloning of a lipolysis-stimulated remnant receptor expressed in
RT the liver.";
RL J. Biol. Chem. 274:13390-13398(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-283; SER-407; SER-436 AND
RP SER-473, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probable role in the clearance of triglyceride-rich
CC lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of
CC free fatty acids and allows their subsequent uptake in the cells
CC (PubMed:10224102). Maintains epithelial barrier function by recruiting
CC MARVELD2/tricellulin to tricellular tight junctions (By similarity).
CC {ECO:0000250|UniProtKB:Q99KG5, ECO:0000269|PubMed:10224102}.
CC -!- SUBUNIT: Homotrimer or homotetramer constituted of isoform 1 and/or
CC isoform 2 and isoform 3 (PubMed:10224102). Assembles into cell-cell
CC contacts. Interacts (via the cytoplasmic domain) with MARVELD2 (via C-
CC terminal cytoplasmic domain); the interaction is required to recruit
CC MARVELD2 to tricellular contacts. Interacts with OCLN (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q99KG5,
CC ECO:0000269|PubMed:10224102}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99KG5};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:Q99KG5}. Note=Located at tricellular
CC contacts. {ECO:0000250|UniProtKB:Q99KG5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=alpha;
CC IsoId=Q9WU74-1; Sequence=Displayed;
CC Name=2; Synonyms=alpha';
CC IsoId=Q9WU74-2; Sequence=VSP_019698;
CC Name=3; Synonyms=beta;
CC IsoId=Q9WU74-3; Sequence=VSP_019697;
CC -!- TISSUE SPECIFICITY: Specifically expressed in liver. Also detected in
CC kidney and lung. {ECO:0000269|PubMed:10224102}.
CC -!- PTM: Phosphorylation at Ser-308 by MAPK8/JNK1 and MAPK9/JNK2 may be
CC required for exclusive localization at tricellular tight junstions.
CC {ECO:0000250|UniProtKB:Q99KG5}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family.
CC {ECO:0000305}.
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DR EMBL; AF119667; AAD30028.1; -; mRNA.
DR EMBL; AF119668; AAD30029.1; -; mRNA.
DR EMBL; AF119669; AAD30030.1; -; mRNA.
DR EMBL; BC100626; AAI00627.1; -; mRNA.
DR RefSeq; NP_116005.1; NM_032616.1. [Q9WU74-1]
DR RefSeq; XP_006228906.1; XM_006228844.3. [Q9WU74-2]
DR RefSeq; XP_006228907.1; XM_006228845.3. [Q9WU74-3]
DR AlphaFoldDB; Q9WU74; -.
DR IntAct; Q9WU74; 1.
DR MINT; Q9WU74; -.
DR STRING; 10116.ENSRNOP00000041379; -.
DR iPTMnet; Q9WU74; -.
DR PhosphoSitePlus; Q9WU74; -.
DR PaxDb; Q9WU74; -.
DR PRIDE; Q9WU74; -.
DR Ensembl; ENSRNOT00000028585; ENSRNOP00000028585; ENSRNOG00000021053. [Q9WU74-2]
DR Ensembl; ENSRNOT00000044678; ENSRNOP00000041379; ENSRNOG00000021053. [Q9WU74-1]
DR Ensembl; ENSRNOT00000116572; ENSRNOP00000097477; ENSRNOG00000021053. [Q9WU74-3]
DR GeneID; 64355; -.
DR KEGG; rno:64355; -.
DR UCSC; RGD:69236; rat. [Q9WU74-1]
DR CTD; 51599; -.
DR RGD; 69236; Lsr.
DR eggNOG; ENOG502QWP5; Eukaryota.
DR GeneTree; ENSGT00950000183058; -.
DR HOGENOM; CLU_028969_2_0_1; -.
DR InParanoid; Q9WU74; -.
DR OMA; GPLMNQP; -.
DR OrthoDB; 457764at2759; -.
DR PhylomeDB; Q9WU74; -.
DR TreeFam; TF330877; -.
DR PRO; PR:Q9WU74; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021053; Expressed in stomach and 19 other tissues.
DR Genevisible; Q9WU74; RN.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005504; F:fatty acid binding; TAS:HGNC-UCL.
DR GO; GO:0017129; F:triglyceride binding; TAS:HGNC-UCL.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0060856; P:establishment of blood-brain barrier; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISS:HGNC.
DR GO; GO:0061833; P:protein localization to tricellular tight junction; ISO:RGD.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IDA:RGD.
DR GO; GO:1904274; P:tricellular tight junction assembly; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR008664; LISCH7.
DR Pfam; PF05624; LSR; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Chylomicron;
KW Disulfide bond; Immunoglobulin domain; LDL; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Tight junction; Transmembrane;
KW Transmembrane helix; VLDL.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..593
FT /note="Lipolysis-stimulated lipoprotein receptor"
FT /id="PRO_0000245310"
FT TOPO_DOM 36..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 89..181
FT /note="Ig-like V-type"
FT REGION 375..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 478
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT DISULFID 113..165
FT /evidence="ECO:0000250"
FT VAR_SEQ 187..255
FT /note="GRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLLFLLLGICWCQCCPHTCCC
FT YVRCPCCPDKCCCPEAL -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10224102"
FT /id="VSP_019697"
FT VAR_SEQ 187..205
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10224102,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019698"
FT CONFLICT 481
FT /note="D -> E (in Ref. 2; AAI00627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 65777 MW; 7C0288823492C87F CRC64;
MAPAAGACAG APDSHPATVV FVCLFLIIFC PDPASAIQVT VSDPYHVVIL FQPVTLPCTY
QMSNTLTVPI VIWKYKSFCR DRIADAFSPA SVDNQLNAQL AAGNPGYNPY VECQDSVRTV
RVVATKQGNA VTLGDYYQGR RITITGNADL TFEQTAWGDS GVYYCSVVSA QDLDGNNEAY
AELIVLGRTS EAPELLPGFR AGPLEDWLFV VVVCLASLLL FLLLGICWCQ CCPHTCCCYV
RCPCCPDKCC CPEALYAAGK AATSGVPSIY APSIYTHLSP AKTPPPPPAM IPMGPPYGYP
GDFDRHSSVG GHSSQVPLLR DVDGSVSSEV RSGYRIQANQ QDDSMRVLYY MEKELANFDP
SRPGPPNGRV ERAMSEVTSL HEDDWRSRPS RAPALTPIRD EEWNRHSPQS PRTWEQEPLQ
EQPRGGWGSG RPRARSVDAL DDINRPGSTE SGRSSPPSSG RRGRAYAPPR SRSRDDLYDP
DDPRDLPHSR DPHYYDDIRS RDPRADPRSR QRSRDPRDAG FRSRDPQYDG RLLEEALKKK
GSGERRRVYR EEEEEEEGQY PPAPPPYSET DSQASRERRL KKNLALSRES LVV
