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Leptin receptor (LEP-R) (B219) (OB receptor) (OB-R) (CD antigen CD295)

 LEPR_MOUSE              Reviewed;        1162 AA.
P48356; O35686; O54986; Q61215; Q64309; Q9QWG3; Q9QWV5;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
30-AUG-2017, entry version 175.
RecName: Full=Leptin receptor;
Short=LEP-R;
AltName: Full=B219;
AltName: Full=OB receptor;
Short=OB-R;
AltName: CD_antigen=CD295;
Flags: Precursor;
Name=Lepr; Synonyms=Db, Obr;
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 A).
TISSUE=Choroid plexus;
PubMed=8548812; DOI=10.1016/0092-8674(95)90151-5;
Tartaglia L.A., Dembski M., Weng X., Deng N., Culpepper J., Devos R.,
Richards G.J., Campfield L.A., Clark F.T., Deeds J., Muir C.,
Sanker S., Moriarty A., Moore K.J., Smutko J.S., Mays G.G.,
Woolf E.A., Monroe C.A., Tepper R.I.;
"Identification and expression cloning of a leptin receptor, OB-R.";
Cell 83:1263-1271(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
STRAIN=C57BLKS/J; TISSUE=Hypothalamus;
PubMed=8608603; DOI=10.1016/S0092-8674(00)81294-5;
Chen H., Charlat O., Tartaglia L.A., Woolf E.A., Weng X., Ellis S.J.,
Lakey N.D., Culpepper J., Moore K.J., Breitbart R.E., Duyk G.M.,
Tepper R.I., Morgenstern J.P.;
"Evidence that the diabetes gene encodes the leptin receptor:
identification of a mutation in the leptin receptor gene in db/db
mice.";
Cell 84:491-495(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).
STRAIN=C57BLKS/J; TISSUE=Hypothalamus;
PubMed=8628397; DOI=10.1038/379632a0;
Lee G.-H., Proenca R., Montez J.M., Carroll K.M., Darvishzadeh J.G.,
Lee J.I., Friedman J.M.;
"Abnormal splicing of the leptin receptor in diabetic mice.";
Nature 379:632-635(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8616721; DOI=10.1038/nm0596-585;
Cioffi J.A., Shafer A.W., Zupancic T.J., Smith-Gbur J., Mikhail A.,
Platika D., Snodgrass H.R.;
"Novel B219/OB receptor isoforms: possible role of leptin in
hematopoiesis and reproduction.";
Nat. Med. 2:585-589(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
STRAIN=FVB/N; TISSUE=Spleen;
PubMed=8692797; DOI=10.1073/pnas.93.13.6231;
Ghilardi N., Ziegler S., Wiestner A., Stoffel R., Heim M.H.,
Skoda R.C.;
"Defective STAT signaling by the leptin receptor in diabetic mice.";
Proc. Natl. Acad. Sci. U.S.A. 93:6231-6235(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
STRAIN=NZO; TISSUE=Hypothalamus;
PubMed=9322935; DOI=10.1210/endo.138.10.5428;
Igel M., Becker W., Herberg L., Joost H.G.;
"Hyperleptinemia, leptin resistance, and polymorphic leptin receptor
in the New Zealand obese mouse.";
Endocrinology 138:4234-4239(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; B; C AND E).
STRAIN=129/J;
PubMed=9344648; DOI=10.1006/geno.1997.4962;
Chua S.C., Koutras I.K., Han L., Liu S.M., Kay J., Young S.J.,
Chung W.K., Leibel R.L.;
"Fine structure of the murine leptin receptor gene: splice site
suppression is required to form two alternatively spliced
transcripts.";
Genomics 45:264-270(1997).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT ASN-600.
STRAIN=KK Obese; TISSUE=Hypothalamus;
PubMed=9845674; DOI=10.1677/jme.0.0210337;
Igel M., Taylor B.A., Phillips S.J., Becker W., Herberg L.,
Joost H.G.;
"Hyperleptinemia and leptin receptor variant Asp600Asn in the obese,
hyperinsulinemic KK mouse strain.";
J. Endocrinol. 21:337-345(1998).
[9]
NUCLEOTIDE SEQUENCE OF 890-1162 (ISOFORM B).
STRAIN=129;
Banks A.S., Myers M.G. Jr.;
"Murine leptin receptor genomic exon 18b and surrounding sequence.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=9732873; DOI=10.1038/29795;
Lord G.M., Matarese G., Howard J.K., Baker R.J., Bloom S.R.,
Lechler R.I.;
"Leptin modulates the T-cell immune response and reverses starvation-
induced immunosuppression.";
Nature 394:897-901(1998).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10660043; DOI=10.1016/S0092-8674(00)81558-5;
Ducy P., Amling M., Takeda S., Priemel M., Schilling A.F., Beil F.T.,
Shen J., Vinson C., Rueger J.M., Karsenty G.;
"Leptin inhibits bone formation through a hypothalamic relay: a
central control of bone mass.";
Cell 100:197-207(2000).
[12]
PHOSPHORYLATION AT TYR-985 AND TYR-1077.
PubMed=11108838; DOI=10.1016/S0014-5793(00)02205-5;
Eyckerman S., Broekaert D., Verhee A., Vandekerckhove J.,
Tavernier J.;
"Identification of the Y985 and Y1077 motifs as SOCS3 recruitment
sites in the murine leptin receptor.";
FEBS Lett. 486:33-37(2000).
[13]
PHOSPHORYLATION AT TYR-985 AND TYR-1138, STAT3 ACTIVATION, ERK/FOS
ACTIVATION, AND MUTAGENESIS OF TYR-985; TYR-1077 AND TYR-1138.
PubMed=10799542; DOI=10.1074/jbc.275.19.14563;
Banks A.S., Davis S.M., Bates S.H., Myers M.G. Jr.;
"Activation of downstream signals by the long form of the leptin
receptor.";
J. Biol. Chem. 275:14563-14572(2000).
[14]
INTERACTION WITH SOCS3, AND MUTAGENESIS OF TYR-985 AND TYR-1138.
PubMed=11018044; DOI=10.1074/jbc.M007577200;
Bjorbaek C., Lavery H.J., Bates S.H., Olson R.K., Davis S.M.,
Flier J.S., Myers M.G. Jr.;
"SOCS3 mediates feedback inhibition of the leptin receptor via
Tyr985.";
J. Biol. Chem. 275:40649-40657(2000).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11861497; DOI=10.1210/endo.143.3.8669;
Hileman S.M., Pierroz D.D., Masuzaki H., Bjoerbaek C., El-Haschimi K.,
Banks W.A., Flier J.S.;
"Characterizaton of short isoforms of the leptin receptor in rat
cerebral microvessels and of brain uptake of leptin in mouse models of
obesity.";
Endocrinology 143:775-783(2002).
[16]
DOMAIN JAK2 ACTIVATION.
PubMed=12196522; DOI=10.1074/jbc.M205148200;
Kloek C., Haq A.K., Dunn S.L., Lavery H.J., Banks A.S.,
Myers M.G. Jr.;
"Regulation of Jak kinases by intracellular leptin receptor
sequences.";
J. Biol. Chem. 277:41547-41555(2002).
[17]
FUNCTION (ISOFORM A AND ISOFORM B), INTERACTION WITH JAK2, AND
MUTAGENESIS OF GLU-891; GLU-894; 896-LEU-PHE-897; 899-LYS-HIS-900;
GLU-902 AND PRO-908.
PubMed=11923481; DOI=10.1210/mend.16.4.0800;
Bahrenberg G., Behrmann I., Barthel A., Hekerman P., Heinrich P.C.,
Joost H.G., Becker W.;
"Identification of the critical sequence elements in the cytoplasmic
domain of leptin receptor isoforms required for Janus kinase/signal
transducer and activator of transcription activation by receptor
heterodimers.";
Mol. Endocrinol. 16:859-872(2002).
[18]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-1138.
PubMed=12594516; DOI=10.1038/nature01388;
Bates S.H., Stearns W.H., Dundon T.A., Schubert M., Tso A.W., Wang Y.,
Banks A.S., Lavery H.J., Haq A.K., Maratos-Flier E., Neel B.G.,
Schwartz M.W., Myers M.G. Jr.;
"STAT3 signalling is required for leptin regulation of energy balance
but not reproduction.";
Nature 421:856-859(2003).
[19]
FUNCTION (ISOFORM A AND ISOFORM E), TISSUE SPECIFICITY (ISOFORM E),
AND SUBCELLULAR LOCATION (ISOFORM E).
PubMed=17620316; DOI=10.1002/jcp.21195;
Tu H., Kastin A.J., Hsuchou H., Pan W.;
"Soluble receptor inhibits leptin transport.";
J. Cell. Physiol. 214:301-305(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
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).
[21]
FUNCTION (ISOFORM A).
PubMed=20223942; DOI=10.1096/fj.09-143487;
Tu H., Hsuchou H., Kastin A.J., Wu X., Pan W.;
"Unique leptin trafficking by a tailless receptor.";
FASEB J. 24:2281-2291(2010).
[22]
REVIEW ON FUNCTION, AND SUBUNIT.
PubMed=25232147; DOI=10.1530/JOE-14-0404;
Allison M.B., Myers M.G. Jr.;
"20 years of leptin: connecting leptin signaling to biological
function.";
J. Endocrinol. 223:T25-T35(2014).
[23]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=25383904; DOI=10.1038/nn.3861;
Flak J.N., Patterson C.M., Garfield A.S., D'Agostino G., Goforth P.B.,
Sutton A.K., Malec P.A., Wong J.M., Germani M., Jones J.C., Rajala M.,
Satin L., Rhodes C.J., Olson D.P., Kennedy R.T., Heisler L.K.,
Myers M.G. Jr.;
"Leptin-inhibited PBN neurons enhance responses to hypoglycemia in
negative energy balance.";
Nat. Neurosci. 17:1744-1750(2014).
-!- FUNCTION: Receptor for hormone LEP/leptin (Probable)
(PubMed:11861497). On ligand binding, mediates LEP central and
peripheral effects through the activation of different signaling
pathways such as JAK2/STAT3 and MAPK cascade/FOS (PubMed:10799542,
PubMed:25383904, PubMed:11923481, PubMed:11861497). In the
hypothalamus, LEP acts as an appetite-regulating factor that
induces a decrease in food intake and an increase in energy
consumption by inducing anorexinogenic factors and suppressing
orexigenic neuropeptides, also regulates bone mass and secretion
of hypothalamo-pituitary-adrenal hormones (PubMed:10660043,
PubMed:12594516). In the periphery, increases basal metabolism,
influences reproductive function, regulates pancreatic beta-cell
function and insulin secretion, is pro-angiogenic and affects
innate and adaptive immunity (PubMed:25383904, PubMed:11923481).
Control of energy homeostasis and melanocortin production
(stimulation of POMC and full repression of AgRP transcription) is
mediated by STAT3 signaling, whereas distinct signals regulate NPY
and the control of fertility, growth and glucose homeostasis
(PubMed:12594516). Involved in the regulation of counter-
regulatory response to hypoglycemia by inhibiting neurons of the
parabrachial nucleus (PubMed:25383904). Has a specific effect on T
lymphocyte responses, differentially regulating the proliferation
of naive and memory T-cells. Leptin increases Th1 and suppresses
Th2 cytokine production (PubMed:9732873).
{ECO:0000269|PubMed:10660043, ECO:0000269|PubMed:10799542,
ECO:0000269|PubMed:11861497, ECO:0000269|PubMed:11923481,
ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:25383904,
ECO:0000269|PubMed:9732873, ECO:0000305|PubMed:25232147}.
-!- FUNCTION: Isoform A: May transport LEP across the blood-brain
barrier. Binds LEP and mediates LEP endocytosis (PubMed:17620316,
PubMed:20223942). Does not induce phosphorylation of and activate
STAT3 (PubMed:11923481, PubMed:20223942).
{ECO:0000269|PubMed:11923481, ECO:0000269|PubMed:17620316,
ECO:0000269|PubMed:20223942}.
-!- FUNCTION: Isoform E: Antagonizes Isoform A and isoform B-mediated
LEP binding and endocytosis. {ECO:0000269|PubMed:17620316}.
-!- SUBUNIT: Present as a mixture of monomers and dimers (Probable).
The phosphorylated receptor binds a number of SH2 domain-
containing proteins such as JAK2, STAT3, PTPN11, and SOCS3 (By
similarity) (PubMed:11018044, PubMed:11923481). Interaction with
SOCS3 inhibits JAK/STAT signaling and MAPK cascade
(PubMed:11018044). {ECO:0000250|UniProtKB:P48357,
ECO:0000269|PubMed:11018044, ECO:0000269|PubMed:11923481,
ECO:0000305|PubMed:25232147}.
-!- INTERACTION:
Q8NFJ9:BBS1 (xeno); NbExp=3; IntAct=EBI-6143588, EBI-1805484;
Q62077:Plcg1; NbExp=2; IntAct=EBI-2257257, EBI-300133;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P48357}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P48357}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P48357}.
-!- SUBCELLULAR LOCATION: Isoform E: Secreted
{ECO:0000305|PubMed:17620316}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=B;
IsoId=P48356-1; Sequence=Displayed;
Name=A;
IsoId=P48356-2; Sequence=VSP_001697, VSP_001698;
Name=C;
IsoId=P48356-3; Sequence=VSP_001699, VSP_001700;
Name=D;
IsoId=P48356-4; Sequence=VSP_001701, VSP_001702;
Name=E;
IsoId=P48356-5; Sequence=VSP_001703, VSP_001704;
-!- TISSUE SPECIFICITY: Isoform A: highest level of expression in lung
and kidney, also present in heart, brain, spleen, liver, muscle,
choroid plexus and hypothalamus. Isoform B: highest levels of
expression in hypothalamus and lower levels in brain, testes and
adipose tissue. Expressed by neurons of the parabrachial nucleus
(PubMed:25383904). Expressed by peripheral blood mononuclear cells
and CD4(+) T-cells (PubMed:9732873). Isoform E: expressed in
adipose tissue, liver, hypothalamus, cerebral microvessels, heart,
and testes (PubMed:17620316). {ECO:0000269|PubMed:17620316,
ECO:0000269|PubMed:25383904, ECO:0000269|PubMed:9732873}.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding. {ECO:0000269|PubMed:12196522}.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation. {ECO:0000269|PubMed:12196522}.
-!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
tyrosine residues (isoform B only) by JAK2. Tyr-985 is required
for complete binding and activation of PTPN11, ERK/FOS
activation,for interaction with SOCS3 and SOCS3 mediated
inhibition of leptin signaling. Phosphorylation on Tyr-1138 is
required for STAT3 binding/activation. Phosphorylation of Tyr-1077
has a more accessory role. {ECO:0000269|PubMed:10799542,
ECO:0000269|PubMed:11108838}.
-!- DISRUPTION PHENOTYPE: Mutants are hyperphagic, obese, infertile,
diabetic and have impaired growth (PubMed:12594516). Have wet
brain weight significantly lower than controls. Brain uptake of
leptin is also reduced (PubMed:11861497). Animals have an
increased bone formation leading to high bone mass
(PubMed:10660043). Have impaired T-cell immunity, Th2 responses
are favoured in mutants (PubMed:9732873). Conditional knockout in
parabrachial nucleus CCK-expressing neurons, treated with 2-
deoxyglucose, have increased levels of glucagon, corticosterone
and epinephrin concentrations compared to wild-types
(PubMed:25383904). {ECO:0000269|PubMed:10660043,
ECO:0000269|PubMed:11861497, ECO:0000269|PubMed:12594516,
ECO:0000269|PubMed:25383904, ECO:0000269|PubMed:9732873}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
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EMBL; U42467; AAA93014.1; -; mRNA.
EMBL; U46135; AAC52408.1; -; mRNA.
EMBL; U49106; AAC52420.1; -; mRNA.
EMBL; U49107; AAC52421.1; -; mRNA.
EMBL; U49108; AAC52422.1; -; mRNA.
EMBL; U49109; AAC52423.1; -; mRNA.
EMBL; U49110; AAC52424.1; -; mRNA.
EMBL; U52915; AAC52599.1; -; mRNA.
EMBL; U58861; AAC52705.1; -; mRNA.
EMBL; U58862; AAC52706.1; -; mRNA.
EMBL; U58863; AAC52707.1; -; mRNA.
EMBL; Y10298; CAA71343.1; -; mRNA.
EMBL; AF039456; AAB95334.1; -; Genomic_DNA.
EMBL; AF039443; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039444; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039445; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039446; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039447; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039448; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039449; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039450; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039451; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039452; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039453; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039454; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039455; AAB95334.1; JOINED; Genomic_DNA.
EMBL; AF039461; AAB95333.1; ALT_TERM; Genomic_DNA.
EMBL; AF039443; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039444; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039445; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039446; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039447; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039448; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039449; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039450; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039451; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039452; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039453; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039454; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039455; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039456; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039457; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039458; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039459; AAB95333.1; JOINED; Genomic_DNA.
EMBL; AF039459; AAB95335.1; -; Genomic_DNA.
EMBL; AF039443; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039444; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039445; AAB95335.1; JOINED; Genomic_DNA.
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EMBL; AF039447; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039448; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039449; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039450; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039451; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039452; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039453; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039454; AAB95335.1; JOINED; Genomic_DNA.
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EMBL; AF039458; AAB95335.1; JOINED; Genomic_DNA.
EMBL; AF039460; AAB95332.1; -; Genomic_DNA.
EMBL; AF039443; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039444; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039445; AAB95332.1; JOINED; Genomic_DNA.
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EMBL; AF039447; AAB95332.1; JOINED; Genomic_DNA.
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EMBL; AF039450; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039451; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039452; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039453; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039454; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039455; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039456; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039457; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039458; AAB95332.1; JOINED; Genomic_DNA.
EMBL; AF039459; AAB95332.1; JOINED; Genomic_DNA.
EMBL; Y10296; CAA71342.1; -; mRNA.
EMBL; AF098792; AAD13218.1; -; Genomic_DNA.
CCDS; CCDS18397.1; -. [P48356-3]
CCDS; CCDS51239.1; -. [P48356-2]
CCDS; CCDS51240.1; -. [P48356-1]
PIR; S68437; S68437.
PIR; S68438; S68438.
PIR; S68439; S68439.
PIR; S68440; S68440.
PIR; S68441; S68441.
RefSeq; NP_001116371.1; NM_001122899.1. [P48356-2]
RefSeq; NP_034834.1; NM_010704.2. [P48356-3]
RefSeq; NP_666258.2; NM_146146.2. [P48356-1]
UniGene; Mm.259282; -.
ProteinModelPortal; P48356; -.
BioGrid; 201139; 3.
DIP; DIP-42763N; -.
ELM; P48356; -.
IntAct; P48356; 10.
MINT; MINT-2569396; -.
STRING; 10090.ENSMUSP00000037385; -.
GuidetoPHARMACOLOGY; 1712; -.
iPTMnet; P48356; -.
PhosphoSitePlus; P48356; -.
MaxQB; P48356; -.
PaxDb; P48356; -.
PeptideAtlas; P48356; -.
PRIDE; P48356; -.
Ensembl; ENSMUST00000037552; ENSMUSP00000037385; ENSMUSG00000057722. [P48356-1]
Ensembl; ENSMUST00000102777; ENSMUSP00000099838; ENSMUSG00000057722. [P48356-3]
Ensembl; ENSMUST00000106921; ENSMUSP00000102534; ENSMUSG00000057722. [P48356-2]
GeneID; 16847; -.
KEGG; mmu:16847; -.
UCSC; uc008tvx.2; mouse. [P48356-1]
UCSC; uc008twa.1; mouse. [P48356-5]
CTD; 3953; -.
MGI; MGI:104993; Lepr.
eggNOG; ENOG410IKH4; Eukaryota.
eggNOG; ENOG4110JZP; LUCA.
GeneTree; ENSGT00730000111209; -.
HOVERGEN; HBG000140; -.
InParanoid; P48356; -.
KO; K05062; -.
OMA; KPETFEH; -.
OrthoDB; EOG091G00QX; -.
PhylomeDB; P48356; -.
TreeFam; TF106501; -.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-2586552; Signaling by Leptin.
PRO; PR:P48356; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000057722; -.
CleanEx; MM_LEPR; -.
ExpressionAtlas; P48356; baseline and differential.
Genevisible; P48356; MM.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0038021; F:leptin receptor activity; IMP:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:MGI.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0098868; P:bone growth; IMP:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IGI:MGI.
GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:MGI.
GO; GO:0051346; P:negative regulation of hydrolase activity; IGI:MGI.
GO; GO:0006909; P:phagocytosis; IMP:UniProtKB.
GO; GO:0046850; P:regulation of bone remodeling; IMP:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; IMP:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; IMP:UniProtKB.
GO; GO:0019222; P:regulation of metabolic process; TAS:MGI.
GO; GO:0044321; P:response to leptin; IMP:UniProtKB.
GO; GO:0019953; P:sexual reproduction; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003961; FN3_dom.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
InterPro; IPR015752; Lep_receptor.
PANTHER; PTHR23036:SF142; PTHR23036:SF142; 1.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 3.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Obesity; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1162 Leptin receptor.
/FTId=PRO_0000010906.
TOPO_DOM 22 839 Extracellular. {ECO:0000255}.
TRANSMEM 840 860 Helical. {ECO:0000255}.
TOPO_DOM 861 1162 Cytoplasmic. {ECO:0000255}.
DOMAIN 238 331 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 329 427 Ig-like.
DOMAIN 537 632 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 637 729 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 738 832 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 465 482 Leptin-binding.
{ECO:0000250|UniProtKB:P48357}.
REGION 891 896 Required for JAK2 activation.
{ECO:0000269|PubMed:12196522}.
REGION 896 904 Required for STAT3 phosphorylation.
{ECO:0000269|PubMed:11923481}.
MOTIF 620 624 WSXWS motif.
MOTIF 869 877 Box 1 motif.
MOD_RES 880 880 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 985 985 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:10799542,
ECO:0000269|PubMed:11108838}.
MOD_RES 1077 1077 Phosphotyrosine.
{ECO:0000269|PubMed:11108838}.
MOD_RES 1138 1138 Phosphotyrosine; by JAK2.
{ECO:0000305|PubMed:10799542}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 698 698 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 726 726 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 90 {ECO:0000250|UniProtKB:P48357}.
DISULFID 89 99 {ECO:0000250|UniProtKB:P48357}.
DISULFID 131 142 {ECO:0000250|UniProtKB:P48357}.
DISULFID 186 195 {ECO:0000250|UniProtKB:P48357}.
DISULFID 188 193 {ECO:0000250|UniProtKB:P48357}.
DISULFID 350 410 {ECO:0000250|UniProtKB:P48357}.
DISULFID 411 416 {ECO:0000250|UniProtKB:P48357}.
DISULFID 434 445 {ECO:0000250|UniProtKB:P48357}.
DISULFID 471 526 {ECO:0000250|UniProtKB:P48357}.
DISULFID 486 496 {ECO:0000250|UniProtKB:P48357}.
VAR_SEQ 797 805 DNFIPIEKY -> GMCTVLFMD (in isoform E).
{ECO:0000303|PubMed:8628397}.
/FTId=VSP_001703.
VAR_SEQ 806 1162 Missing (in isoform E).
{ECO:0000303|PubMed:8628397}.
/FTId=VSP_001704.
VAR_SEQ 890 900 PETFEHLFTKH -> DISFHEVFIFR (in isoform
D). {ECO:0000303|PubMed:8628397}.
/FTId=VSP_001701.
VAR_SEQ 890 894 PETFE -> RTDTL (in isoform A).
{ECO:0000303|PubMed:8548812,
ECO:0000303|PubMed:8628397,
ECO:0000303|PubMed:8692797}.
/FTId=VSP_001697.
VAR_SEQ 890 892 PET -> VTV (in isoform C).
{ECO:0000303|PubMed:8616721,
ECO:0000303|PubMed:8628397}.
/FTId=VSP_001699.
VAR_SEQ 893 1162 Missing (in isoform C).
{ECO:0000303|PubMed:8616721,
ECO:0000303|PubMed:8628397}.
/FTId=VSP_001700.
VAR_SEQ 895 1162 Missing (in isoform A).
{ECO:0000303|PubMed:8548812,
ECO:0000303|PubMed:8628397,
ECO:0000303|PubMed:8692797}.
/FTId=VSP_001698.
VAR_SEQ 901 1162 Missing (in isoform D).
{ECO:0000303|PubMed:8628397}.
/FTId=VSP_001702.
VARIANT 541 541 V -> I (in strain: NZO).
VARIANT 600 600 D -> N (in strain: KK Obese).
{ECO:0000269|PubMed:9845674}.
VARIANT 651 651 V -> I (in strain: NZO).
VARIANT 1044 1044 T -> I (in strain: NZO).
MUTAGEN 891 891 E->A: No effect on STAT3 phosphorylation.
{ECO:0000269|PubMed:11923481}.
MUTAGEN 894 894 E->A: No effect on STAT3 phosphorylation.
{ECO:0000269|PubMed:11923481}.
MUTAGEN 896 897 LF->AA: Abrogates STAT3 phosphorylation.
{ECO:0000269|PubMed:11923481}.
MUTAGEN 899 900 KH->AA: No effect on STAT3
phosphorylation.
{ECO:0000269|PubMed:11923481}.
MUTAGEN 902 902 E->A: No effect on STAT3 phosphorylation.
{ECO:0000269|PubMed:11923481}.
MUTAGEN 908 908 P->A: No effect on STAT3 phosphorylation.
{ECO:0000269|PubMed:11923481}.
MUTAGEN 985 985 Y->L: No change in EPO-induced JAK2
activation and EPO-induced tyrosine
phosphorylation. No phosphorylation; when
associated with S-1138. No
phosphorylation; when associated with
both S-1138 and F-1077. No change in
STAT3 activation. No PTPN11 binding. No
SOCS3 binding nor inhibition of
signaling. Greatly reduced ERK/FOS
activation. Mutants are hyperphagic,
obese and hyperglycaemic, females show a
defect in lactation.
{ECO:0000269|PubMed:10799542,
ECO:0000269|PubMed:11018044,
ECO:0000269|PubMed:12594516}.
MUTAGEN 1077 1077 Y->F: No effect on EPO-induced tyrosine
phosphorylation.
{ECO:0000269|PubMed:10799542}.
MUTAGEN 1138 1138 Y->S: No change in EPO-induced JAK2
activation and EPO-induced tyrosine
phosphorylation. No phosphorylation; when
associated with L-985. No
phosphorylation; when associated with L-
985 and F-1077. No STAT3 activation. No
change in SOCS3 binding nor signaling
inhibition. No effect on ERK/FOS
activation. {ECO:0000269|PubMed:10799542,
ECO:0000269|PubMed:11018044}.
CONFLICT 140 140 F -> I (in Ref. 5; AAC52705/AAC52706/
AAC52707). {ECO:0000305}.
CONFLICT 720 720 A -> T (in Ref. 6; CAA71343).
{ECO:0000305}.
SEQUENCE 1162 AA; 130789 MW; 0E1E75B076BA60A2 CRC64;
MMCQKFYVVL LHWEFLYVIA ALNLAYPISP WKFKLFCGPP NTTDDSFLSP AGAPNNASAL
KGASEAIVEA KFNSSGIYVP ELSKTVFHCC FGNEQGQNCS ALTDNTEGKT LASVVKASVF
RQLGVNWDIE CWMKGDLTLF ICHMEPLPKN PFKNYDSKVH LLYDLPEVID DSPLPPLKDS
FQTVQCNCSL RGCECHVPVP RAKLNYALLM YLEITSAGVS FQSPLMSLQP MLVVKPDPPL
GLHMEVTDDG NLKISWDSQT MAPFPLQYQV KYLENSTIVR EAAEIVSATS LLVDSVLPGS
SYEVQVRSKR LDGSGVWSDW SSPQVFTTQD VVYFPPKILT SVGSNASFHC IYKNENQIIS
SKQIVWWRNL AEKIPEIQYS IVSDRVSKVT FSNLKATRPR GKFTYDAVYC CNEQACHHRY
AELYVIDVNI NISCETDGYL TKMTCRWSPS TIQSLVGSTV QLRYHRRSLY CPDSPSIHPT
SEPKNCVLQR DGFYECVFQP IFLLSGYTMW IRINHSLGSL DSPPTCVLPD SVVKPLPPSN
VKAEITVNTG LLKVSWEKPV FPENNLQFQI RYGLSGKEIQ WKTHEVFDAK SKSASLLVSD
LCAVYVVQVR CRRLDGLGYW SNWSSPAYTL VMDVKVPMRG PEFWRKMDGD VTKKERNVTL
LWKPLTKNDS LCSVRRYVVK HRTAHNGTWS EDVGNRTNLT FLWTEPAHTV TVLAVNSLGA
SLVNFNLTFS WPMSKVSAVE SLSAYPLSSS CVILSWTLSP DDYSLLYLVI EWKILNEDDG
MKWLRIPSNV KKFYIHDNFI PIEKYQFSLY PVFMEGVGKP KIINGFTKDA IDKQQNDAGL
YVIVPIIISS CVLLLGTLLI SHQRMKKLFW DDVPNPKNCS WAQGLNFQKP ETFEHLFTKH
AESVIFGPLL LEPEPISEEI SVDTAWKNKD EMVPAAMVSL LLTTPDPESS SICISDQCNS
ANFSGSQSTQ VTCEDECQRQ PSVKYATLVS NDKLVETDEE QGFIHSPVSN CISSNHSPLR
QSFSSSSWET EAQTFFLLSD QQPTMISPQL SFSGLDELLE LEGSFPEENH REKSVCYLGV
TSVNRRESGV LLTGEAGILC TFPAQCLFSD IRILQERCSH FVENNLSLGT SGENFVPYMP
QFQTCSTHSH KIMENKMCDL TV


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