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Leptin receptor (LEP-R) (HuB219) (OB receptor) (OB-R) (CD antigen CD295)

 LEPR_HUMAN              Reviewed;        1165 AA.
P48357; Q13592; Q13593; Q13594; Q92919; Q92920; Q92921;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
27-SEP-2017, entry version 193.
RecName: Full=Leptin receptor;
Short=LEP-R;
AltName: Full=HuB219;
AltName: Full=OB receptor;
Short=OB-R;
AltName: CD_antigen=CD295;
Flags: Precursor;
Name=LEPR; Synonyms=DB, OBR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND E).
TISSUE=Brain;
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] (ISOFORMS A; B AND C), AND FUNCTION.
TISSUE=Fetal liver;
PubMed=8805376; DOI=10.1016/S0960-9822(02)70684-2;
Bennett B.D., Solar G.P., Yuan J.Q., Mathias J., Thomas G.R.,
Matthews W.;
"A role for leptin and its cognate receptor in hematopoiesis.";
Curr. Biol. 6:1170-1180(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D), AND VARIANTS ARG-109
AND ARG-223.
TISSUE=Fetal 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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), AND VARIANTS ARG-109
AND ARG-223.
PubMed=9158141; DOI=10.1093/hmg/6.5.675;
Thompson D.B., Ravussin E., Bennett P.H., Bogardus C.;
"Structure and sequence variation at the human leptin receptor gene in
lean and obese Pima Indians.";
Hum. Mol. Genet. 6:675-679(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=9061609; DOI=10.1677/jme.0.0180077;
Luoh S.-M., Di Marco F., Levin N., Armanini M., Xie M.H., Nelson C.,
Bennett G.L., Williams M., Spencer S.A., Gurney A., de Sauvage F.J.;
"Cloning and characterization of a human leptin receptor using a
biologically active leptin immunoadhesin.";
J. Mol. Endocrinol. 18:77-85(1997).
[6]
INVOLVEMENT IN LEPRD, AND FUNCTION.
PubMed=9537324; DOI=10.1038/32911;
Clement K., Vaisse C., Lahlou N., Cabrol S., Pelloux V., Cassuto D.,
Gourmelen M., Dina C., Chambaz J., Lacorte J.M., Basdevant A.,
Bougneres P., Lebouc Y., Froguel P., Guy-Grand B.;
"A mutation in the human leptin receptor gene causes obesity and
pituitary dysfunction.";
Nature 392:398-401(1998).
[7]
ALTERNATIVE SPLICING DUE TO AN ENDOGENOUS RETROVIRUS.
PubMed=9929394; DOI=10.1007/PL00013153;
Kapitonov V.V., Jurka J.;
"The long terminal repeat of an endogenous retrovirus induces
alternative splicing and encodes an additional carboxy-terminal
sequence in the human leptin receptor.";
J. Mol. Evol. 48:248-251(1999).
[8]
INTERACTION WITH PTPN11, AND MUTAGENESIS OF TYR-986; 1078-TYR-TYR-1079
AND TYR-1141.
PubMed=9600917; DOI=10.1073/pnas.95.11.6061;
Carpenter L.R., Farruggella T.J., Symes A., Karow M.L.,
Yancopoulos G.D., Stahl N.;
"Enhancing leptin response by preventing SH2-containing phosphatase 2
interaction with Ob receptor.";
Proc. Natl. Acad. Sci. U.S.A. 95:6061-6066(1998).
[9]
GLYCOSYLATION AT ASN-23; ASN-41; ASN-56; ASN-73; ASN-81; ASN-98;
ASN-187; ASN-206; ASN-276; ASN-347; ASN-397; ASN-516; ASN-624;
ASN-659; ASN-688; ASN-697; ASN-728 AND ASN-750, DISULFIDE BONDS, AND
PARTIAL PROTEIN SEQUENCE.
PubMed=9786864; DOI=10.1074/jbc.273.44.28691;
Haniu M., Arakawa T., Bures E.J., Young Y., Hui J.O., Rohde M.F.,
Welcher A.A., Horan T.;
"Human leptin receptor. Determination of disulfide structure and N-
glycosylation sites of the extracellular domain.";
J. Biol. Chem. 273:28691-28699(1998).
[10]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=10896907; DOI=10.1136/gut.47.2.178;
Sobhani I., Bado A., Vissuzaine C., Buyse M., Kermorgant S.,
Laigneau J.P., Attoub S., Lehy T., Henin D., Mignon M., Lewin M.J.;
"Leptin secretion and leptin receptor in the human stomach.";
Gut 47:178-183(2000).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12504075; DOI=10.1016/S0006-291X(02)02838-3;
Zhao Y., Sun R., You L., Gao C., Tian Z.;
"Expression of leptin receptors and response to leptin stimulation of
human natural killer cell lines.";
Biochem. Biophys. Res. Commun. 300:247-252(2003).
[12]
TISSUE SPECIFICITY.
PubMed=16052473; DOI=10.1002/jcb.20521;
Solberg R., Aas V., Thoresen G.H., Kase E.T., Drevon C.A.,
Rustan A.C., Reseland J.E.;
"Leptin expression in human primary skeletal muscle cells is reduced
during differentiation.";
J. Cell. Biochem. 96:89-96(2005).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276 AND ASN-516.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276 AND ASN-397.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION.
PubMed=25060689; DOI=10.1016/j.metabol.2014.06.010;
Cassano S., Pucino V., La Rocca C., Procaccini C., De Rosa V.,
Marone G., Matarese G.;
"Leptin modulates autophagy in human CD4+CD25- conventional T cells.";
Metabolism 63:1272-1279(2014).
[18]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 428-633 IN COMPLEX WITH
ANTIBODY, LEPTIN-BINDING REGION, DISULFIDE BONDS, AND FUNCTION.
PubMed=22405007; DOI=10.1016/j.str.2012.01.019;
Carpenter B., Hemsworth G.R., Wu Z., Maamra M., Strasburger C.J.,
Ross R.J., Artymiuk P.J.;
"Structure of the human obesity receptor leptin-binding domain reveals
the mechanism of leptin antagonism by a monoclonal antibody.";
Structure 20:487-497(2012).
[19]
VARIANT ARG-223.
PubMed=8666155; DOI=10.2337/diab.45.7.992;
Considine R.V., Considine E.L., Williams C.J., Hyde T.M., Caro J.F.;
"The hypothalamic leptin receptor in humans: identification of
incidental sequence polymorphisms and absence of the db/db mouse and
fa/fa rat mutations.";
Diabetes 45:992-994(1996).
[20]
VARIANTS ARG-109; ARG-204; ARG-223 AND ASN-656.
PubMed=9144432; DOI=10.1006/bbrc.1997.6430;
Echwald S.M., Soerensen T.D., Soerensen T.I., Tybjaerg-Hansen A.,
Andersen T., Chung W.K., Leibel R.L., Pedersen O.;
"Amino acid variants in the human leptin receptor: lack of association
to juvenile onset obesity.";
Biochem. Biophys. Res. Commun. 233:248-252(1997).
[21]
VARIANTS ARG-109; ARG-223 AND ASN-656.
PubMed=9287054; DOI=10.2337/diab.46.9.1509;
Chung W.K., Power-Kehoe L., Chua M., Chu F., Aronne L., Huma Z.,
Sothern M., Udall J.N., Kahle B., Leibel R.L.;
"Exonic and intronic sequence variation in the human leptin receptor
gene (LEPR).";
Diabetes 46:1509-1511(1997).
[22]
VARIANTS ARG-109; ARG-223 AND ASN-656.
PubMed=9175732; DOI=10.1093/hmg/6.6.869;
Gotoda T., Manning B.S., Goldstone A.P., Imrie H., Evans A.L.,
Strosberg A.D., McKeigue P.M., Scott J., Aitman T.J.;
"Leptin receptor gene variation and obesity: lack of association in a
white British male population.";
Hum. Mol. Genet. 6:869-876(1997).
[23]
VARIANTS ARG-109; ARG-223; ASN-656 AND THR-675.
PubMed=9860295; DOI=10.1007/s004390050867;
Roth H., Korn T., Rosenkranz K., Hinney A., Ziegler A., Kunz J.,
Siegfried W., Mayer H., Hebebrand J., Grzeschik K.-H.;
"Transmission disequilibrium and sequence variants at the leptin
receptor gene in extremely obese German children and adolescents.";
Hum. Genet. 103:540-546(1998).
[24]
VARIANTS [LARGE SCALE ANALYSIS] ARG-109 AND ARG-223.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[25]
VARIANTS LEPRD HIS-422; GLY-604 AND PRO-786.
PubMed=25751111; DOI=10.1210/jc.2015-1036;
Huvenne H., Le Beyec J., Pepin D., Alili R., Kherchiche P.P.,
Jeannic E., Frelut M.L., Lacorte J.M., Nicolino M., Viard A.,
Laville M., Ledoux S., Tounian P., Poitou C., Dubern B., Clement K.;
"Seven novel deleterious LEPR mutations found in early-onset obesity:
a DeltaExon6-8 shared by subjects from Reunion Island, France,
suggests a founder effect.";
J. Clin. Endocrinol. Metab. 100:E757-E766(2015).
-!- FUNCTION: Receptor for hormone LEP/leptin (Probable)
(PubMed:22405007). On ligand binding, mediates LEP central and
peripheral effects through the activation of different signaling
pathways such as JAK2/STAT3 and MAPK cascade/FOS. 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 (By similarity)
(PubMed:9537324). 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:25060689, PubMed:12504075,
PubMed:8805376). 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. Involved in the regulation of counter-
regulatory response to hypoglycemia by inhibiting neurons of the
parabrachial nucleus. Has a specific effect on T lymphocyte
responses, differentially regulating the proliferation of naive
and memory T -ells. Leptin increases Th1 and suppresses Th2
cytokine production (By similarity).
{ECO:0000250|UniProtKB:P48356, ECO:0000269|PubMed:12504075,
ECO:0000269|PubMed:22405007, ECO:0000269|PubMed:25060689,
ECO:0000269|PubMed:8805376, ECO:0000269|PubMed:9537324,
ECO:0000305|PubMed:25232147}.
-!- FUNCTION: Isoform A: May transport LEP across the blood-brain
barrier. Binds LEP and mediates LEP endocytosis. Does not induce
phosphorylation of and activate STAT3.
{ECO:0000250|UniProtKB:P48356}.
-!- FUNCTION: Isoform E: Antagonizes Isoform A and isoform B-mediated
LEP binding and endocytosis. {ECO:0000250|UniProtKB:P48356}.
-!- 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:9600917). Interaction with SOCS3 inhibits
JAK/STAT signaling and MAPK cascade (By similarity).
{ECO:0000250|UniProtKB:P48356, ECO:0000269|PubMed:9600917,
ECO:0000305|PubMed:25232147}.
-!- INTERACTION:
P62993:GRB2; NbExp=3; IntAct=EBI-518596, EBI-401755;
P0CG48:UBC; NbExp=2; IntAct=EBI-7886448, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19159218};
Single-pass type I membrane protein {ECO:0000305}. Basolateral
cell membrane {ECO:0000269|PubMed:19159218}.
-!- SUBCELLULAR LOCATION: Isoform E: Secreted
{ECO:0000250|UniProtKB:P48356}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=B; Synonyms=13.2, OBRb;
IsoId=P48357-1; Sequence=Displayed;
Name=A; Synonyms=6.4, HuB219.3;
IsoId=P48357-2; Sequence=VSP_001689, VSP_001690;
Name=C; Synonyms=12.1, OBRa;
IsoId=P48357-3; Sequence=VSP_001691, VSP_001692;
Name=D; Synonyms=HuB219.2;
IsoId=P48357-4; Sequence=VSP_001693, VSP_001694;
Name=E;
IsoId=P48357-5; Sequence=VSP_001688;
-!- TISSUE SPECIFICITY: Isoform A is expressed in fetal liver and in
hematopoietic tissues and choroid plexus. In adults highest
expression in heart, liver, small intestine, prostate and ovary.
Low level in lung and kidney. Isoform B is highly expressed in
hypothalamus, but also in skeletal muscle. Detected in fundic and
antral epithelial cells of the gastric mucosa (PubMed:19159218).
Isoform B and isoform A are expressed by NK cells (at protein
level) (PubMed:12504075). {ECO:0000269|PubMed:12504075,
ECO:0000269|PubMed:16052473, ECO:0000269|PubMed:19159218}.
-!- DOMAIN: The cytoplasmic domain may be essential for intracellular
signal transduction by activation of JAK tyrosine kinase and
STATs.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
tyrosine residues (isoform B only) by JAK2. Tyr-986 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-1141 is
required for STAT3 binding/activation. Phosphorylation of Tyr-1079
has a more accessory role. {ECO:0000250|UniProtKB:P48356}.
-!- DISEASE: Leptin receptor deficiency (LEPRD) [MIM:614963]: A rare
disease characterized by normal levels of serum leptin,
hyperphagia and severe obesity from an early age. Additional
features include alterations in immune function, and delayed
puberty due to hypogonadotropic hypogonadism.
{ECO:0000269|PubMed:25751111, ECO:0000269|PubMed:9537324}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
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EMBL; U43168; AAA93015.1; -; mRNA.
EMBL; U66495; AAB07495.1; -; mRNA.
EMBL; U66496; AAB07496.1; -; mRNA.
EMBL; U66497; AAB07497.1; -; mRNA.
EMBL; U52912; AAC50509.1; -; mRNA.
EMBL; U52913; AAC50510.1; -; mRNA.
EMBL; U52914; AAC50511.1; -; mRNA.
EMBL; U59263; AAB09673.1; -; Genomic_DNA.
EMBL; U59248; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59249; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59250; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59252; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59253; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59254; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59255; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59256; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59257; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59258; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59259; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59260; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59261; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U59262; AAB09673.1; JOINED; Genomic_DNA.
EMBL; U50748; AAC23650.1; -; mRNA.
CCDS; CCDS30740.1; -. [P48357-2]
CCDS; CCDS30741.1; -. [P48357-3]
CCDS; CCDS55604.1; -. [P48357-4]
CCDS; CCDS631.1; -. [P48357-1]
RefSeq; NP_001003679.1; NM_001003679.3. [P48357-2]
RefSeq; NP_001003680.1; NM_001003680.3. [P48357-3]
RefSeq; NP_001185616.1; NM_001198687.1. [P48357-3]
RefSeq; NP_001185617.1; NM_001198688.1. [P48357-4]
RefSeq; NP_001185618.1; NM_001198689.1. [P48357-2]
RefSeq; NP_002294.2; NM_002303.5. [P48357-1]
UniGene; Hs.23581; -.
UniGene; Hs.723178; -.
PDB; 3V6O; X-ray; 1.95 A; A/B=428-633.
PDBsum; 3V6O; -.
ProteinModelPortal; P48357; -.
SMR; P48357; -.
BioGrid; 110144; 19.
CORUM; P48357; -.
DIP; DIP-6117N; -.
IntAct; P48357; 9.
MINT; MINT-1387953; -.
STRING; 9606.ENSP00000330393; -.
ChEMBL; CHEMBL5913; -.
DrugBank; DB05098; Leptin.
DrugBank; DB09046; Metreleptin.
iPTMnet; P48357; -.
PhosphoSitePlus; P48357; -.
BioMuta; LEPR; -.
DMDM; 116242617; -.
MaxQB; P48357; -.
PaxDb; P48357; -.
PeptideAtlas; P48357; -.
PRIDE; P48357; -.
DNASU; 3953; -.
Ensembl; ENST00000344610; ENSP00000340884; ENSG00000116678. [P48357-4]
Ensembl; ENST00000349533; ENSP00000330393; ENSG00000116678. [P48357-1]
Ensembl; ENST00000371058; ENSP00000360097; ENSG00000116678. [P48357-4]
Ensembl; ENST00000371059; ENSP00000360098; ENSG00000116678. [P48357-3]
Ensembl; ENST00000371060; ENSP00000360099; ENSG00000116678. [P48357-2]
Ensembl; ENST00000616738; ENSP00000483390; ENSG00000116678. [P48357-2]
GeneID; 3953; -.
KEGG; hsa:3953; -.
UCSC; uc001dcg.4; human. [P48357-1]
CTD; 3953; -.
DisGeNET; 3953; -.
EuPathDB; HostDB:ENSG00000116678.18; -.
GeneCards; LEPR; -.
HGNC; HGNC:6554; LEPR.
HPA; HPA030899; -.
MalaCards; LEPR; -.
MIM; 601007; gene.
MIM; 614963; phenotype.
neXtProt; NX_P48357; -.
OpenTargets; ENSG00000116678; -.
Orphanet; 179494; Obesity due to leptin receptor gene deficiency.
PharmGKB; PA229; -.
eggNOG; ENOG410IKH4; Eukaryota.
eggNOG; ENOG4110JZP; LUCA.
GeneTree; ENSGT00730000111209; -.
HOVERGEN; HBG000140; -.
InParanoid; P48357; -.
KO; K05062; -.
OMA; KPETFEH; -.
OrthoDB; EOG091G00QX; -.
PhylomeDB; P48357; -.
TreeFam; TF106501; -.
Reactome; R-HSA-2586552; Signaling by Leptin.
SignaLink; P48357; -.
SIGNOR; P48357; -.
GeneWiki; Leptin_receptor; -.
GenomeRNAi; 3953; -.
PRO; PR:P48357; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116678; -.
CleanEx; HS_LEPR; -.
Genevisible; P48357; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0038021; F:leptin receptor activity; ISS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
GO; GO:0098868; P:bone growth; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; TAS:ProtInc.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
GO; GO:0044321; P:response to leptin; ISS:UniProtKB.
GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS: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;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Obesity; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 21
CHAIN 22 1165 Leptin receptor.
/FTId=PRO_0000010904.
TOPO_DOM 22 839 Extracellular. {ECO:0000255}.
TRANSMEM 840 862 Helical. {ECO:0000255}.
TOPO_DOM 863 1165 Cytoplasmic. {ECO:0000255}.
DOMAIN 239 333 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 331 429 Ig-like.
DOMAIN 539 634 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 639 732 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 740 833 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 467 484 Leptin-binding.
{ECO:0000305|PubMed:22405007}.
REGION 893 898 Required for JAK2 activation.
{ECO:0000250|UniProtKB:P48356}.
REGION 898 906 Required for STAT3 phosphorylation.
{ECO:0000250|UniProtKB:P48356}.
MOTIF 622 626 WSXWS motif.
MOTIF 871 879 Box 1 motif.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 986 986 Phosphotyrosine; by JAK2.
{ECO:0000250|UniProtKB:P48356}.
MOD_RES 1079 1079 Phosphotyrosine.
{ECO:0000250|UniProtKB:P48356}.
MOD_RES 1141 1141 Phosphotyrosine; by JAK2.
{ECO:0000250|UniProtKB:P48356}.
CARBOHYD 23 23 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9786864}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9786864}.
CARBOHYD 516 516 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:9786864}.
CARBOHYD 624 624 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 659 659 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 688 688 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 697 697 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 728 728 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
CARBOHYD 750 750 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9786864}.
DISULFID 37 90 {ECO:0000269|PubMed:22405007}.
DISULFID 89 99 {ECO:0000269|PubMed:22405007}.
DISULFID 131 142 {ECO:0000269|PubMed:22405007}.
DISULFID 186 196 {ECO:0000269|PubMed:22405007}.
DISULFID 188 193 {ECO:0000269|PubMed:22405007}.
DISULFID 352 412 {ECO:0000269|PubMed:22405007}.
DISULFID 413 418 {ECO:0000269|PubMed:22405007}.
DISULFID 436 447 {ECO:0000269|PubMed:22405007}.
DISULFID 473 528 {ECO:0000269|PubMed:22405007}.
DISULFID 488 498 {ECO:0000269|PubMed:22405007}.
VAR_SEQ 840 1165 Missing (in isoform E).
{ECO:0000303|PubMed:8548812}.
/FTId=VSP_001688.
VAR_SEQ 892 958 PETFEHLFIKHTASVTCGPLLLEPETISEDISVDTSWKNKD
EMMPTTVVSLLSTTDLEKGSVCISDQ -> MLEGSMFVKSH
HHSLISSTQGHKHCGRPQGPLHRKTRDLCSLVYLLTLPPLL
SYDPAKSPSVRNTQE (in isoform C).
{ECO:0000303|PubMed:8616721,
ECO:0000303|PubMed:8805376}.
/FTId=VSP_001691.
VAR_SEQ 892 906 PETFEHLFIKHTASV -> KMPGTKELLGGGWLT (in
isoform D). {ECO:0000303|PubMed:8616721}.
/FTId=VSP_001693.
VAR_SEQ 892 896 PETFE -> RTDIL (in isoform A).
{ECO:0000303|PubMed:8616721,
ECO:0000303|PubMed:8805376,
ECO:0000303|PubMed:9061609}.
/FTId=VSP_001689.
VAR_SEQ 897 1165 Missing (in isoform A).
{ECO:0000303|PubMed:8616721,
ECO:0000303|PubMed:8805376,
ECO:0000303|PubMed:9061609}.
/FTId=VSP_001690.
VAR_SEQ 907 1165 Missing (in isoform D).
{ECO:0000303|PubMed:8616721}.
/FTId=VSP_001694.
VAR_SEQ 959 1165 Missing (in isoform C).
{ECO:0000303|PubMed:8616721,
ECO:0000303|PubMed:8805376}.
/FTId=VSP_001692.
VARIANT 109 109 K -> R (in dbSNP:rs1137100).
{ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:8616721,
ECO:0000269|PubMed:9144432,
ECO:0000269|PubMed:9158141,
ECO:0000269|PubMed:9175732,
ECO:0000269|PubMed:9287054,
ECO:0000269|PubMed:9860295}.
/FTId=VAR_002703.
VARIANT 124 124 D -> G (in dbSNP:rs35573508).
/FTId=VAR_049167.
VARIANT 204 204 K -> R (in dbSNP:rs146442768).
{ECO:0000269|PubMed:9144432}.
/FTId=VAR_002704.
VARIANT 223 223 Q -> R (in dbSNP:rs1137101).
{ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:8616721,
ECO:0000269|PubMed:8666155,
ECO:0000269|PubMed:9144432,
ECO:0000269|PubMed:9158141,
ECO:0000269|PubMed:9175732,
ECO:0000269|PubMed:9287054,
ECO:0000269|PubMed:9860295}.
/FTId=VAR_002705.
VARIANT 422 422 Y -> H (in LEPRD; unknown pathological
significance).
{ECO:0000269|PubMed:25751111}.
/FTId=VAR_075723.
VARIANT 503 503 I -> V (in dbSNP:rs13306526).
/FTId=VAR_028201.
VARIANT 604 604 C -> G (in LEPRD; unknown pathological
significance).
{ECO:0000269|PubMed:25751111}.
/FTId=VAR_075724.
VARIANT 656 656 K -> N (in dbSNP:rs8179183).
{ECO:0000269|PubMed:9144432,
ECO:0000269|PubMed:9175732,
ECO:0000269|PubMed:9287054,
ECO:0000269|PubMed:9860295}.
/FTId=VAR_002706.
VARIANT 675 675 S -> T (in dbSNP:rs373154589).
{ECO:0000269|PubMed:9860295}.
/FTId=VAR_002707.
VARIANT 699 699 T -> M (in dbSNP:rs34499590).
/FTId=VAR_049168.
VARIANT 786 786 L -> P (in LEPRD; unknown pathological
significance).
{ECO:0000269|PubMed:25751111}.
/FTId=VAR_075725.
MUTAGEN 986 986 Y->F: Greatly reduced PTPN11 binding; no
PTPN11 phosphorylation; no effect on
STAT3 phosphorylation.
{ECO:0000269|PubMed:9600917}.
MUTAGEN 1078 1079 YY->FF: No effect on PTPN11 nor STAT3
phosphorylation.
{ECO:0000269|PubMed:9600917}.
MUTAGEN 1141 1141 Y->F: No effect on PTPN11
phosphorylation; no STAT3
phosphorylation.
{ECO:0000269|PubMed:9600917}.
CONFLICT 85 85 T -> A (in Ref. 3; AAC50509/AAC50510/
AAC50511). {ECO:0000305}.
CONFLICT 976 976 D -> A (in Ref. 1; AAA93015 and 4;
AAB09673). {ECO:0000305}.
STRAND 435 438 {ECO:0000244|PDB:3V6O}.
STRAND 445 449 {ECO:0000244|PDB:3V6O}.
STRAND 461 468 {ECO:0000244|PDB:3V6O}.
STRAND 484 486 {ECO:0000244|PDB:3V6O}.
STRAND 488 490 {ECO:0000244|PDB:3V6O}.
STRAND 496 500 {ECO:0000244|PDB:3V6O}.
STRAND 509 517 {ECO:0000244|PDB:3V6O}.
STRAND 527 529 {ECO:0000244|PDB:3V6O}.
HELIX 531 534 {ECO:0000244|PDB:3V6O}.
STRAND 544 548 {ECO:0000244|PDB:3V6O}.
TURN 549 552 {ECO:0000244|PDB:3V6O}.
STRAND 553 557 {ECO:0000244|PDB:3V6O}.
STRAND 568 580 {ECO:0000244|PDB:3V6O}.
STRAND 584 588 {ECO:0000244|PDB:3V6O}.
STRAND 595 598 {ECO:0000244|PDB:3V6O}.
STRAND 607 615 {ECO:0000244|PDB:3V6O}.
SEQUENCE 1165 AA; 132494 MW; CAA03BEAF2602D0A CRC64;
MICQKFCVVL LHWEFIYVIT AFNLSYPITP WRFKLSCMPP NSTYDYFLLP AGLSKNTSNS
NGHYETAVEP KFNSSGTHFS NLSKTTFHCC FRSEQDRNCS LCADNIEGKT FVSTVNSLVF
QQIDANWNIQ CWLKGDLKLF ICYVESLFKN LFRNYNYKVH LLYVLPEVLE DSPLVPQKGS
FQMVHCNCSV HECCECLVPV PTAKLNDTLL MCLKITSGGV IFQSPLMSVQ PINMVKPDPP
LGLHMEITDD GNLKISWSSP PLVPFPLQYQ VKYSENSTTV IREADKIVSA TSLLVDSILP
GSSYEVQVRG KRLDGPGIWS DWSTPRVFTT QDVIYFPPKI LTSVGSNVSF HCIYKKENKI
VPSKEIVWWM NLAEKIPQSQ YDVVSDHVSK VTFFNLNETK PRGKFTYDAV YCCNEHECHH
RYAELYVIDV NINISCETDG YLTKMTCRWS TSTIQSLAES TLQLRYHRSS LYCSDIPSIH
PISEPKDCYL QSDGFYECIF QPIFLLSGYT MWIRINHSLG SLDSPPTCVL PDSVVKPLPP
SSVKAEITIN IGLLKISWEK PVFPENNLQF QIRYGLSGKE VQWKMYEVYD AKSKSVSLPV
PDLCAVYAVQ VRCKRLDGLG YWSNWSNPAY TVVMDIKVPM RGPEFWRIIN GDTMKKEKNV
TLLWKPLMKN DSLCSVQRYV INHHTSCNGT WSEDVGNHTK FTFLWTEQAH TVTVLAINSI
GASVANFNLT FSWPMSKVNI VQSLSAYPLN SSCVIVSWIL SPSDYKLMYF IIEWKNLNED
GEIKWLRISS SVKKYYIHDH FIPIEKYQFS LYPIFMEGVG KPKIINSFTQ DDIEKHQSDA
GLYVIVPVII SSSILLLGTL LISHQRMKKL FWEDVPNPKN CSWAQGLNFQ KPETFEHLFI
KHTASVTCGP LLLEPETISE DISVDTSWKN KDEMMPTTVV SLLSTTDLEK GSVCISDQFN
SVNFSEAEGT EVTYEDESQR QPFVKYATLI SNSKPSETGE EQGLINSSVT KCFSSKNSPL
KDSFSNSSWE IEAQAFFILS DQHPNIISPH LTFSEGLDEL LKLEGNFPEE NNDKKSIYYL
GVTSIKKRES GVLLTDKSRV SCPFPAPCLF TDIRVLQDSC SHFVENNINL GTSSKKTFAS
YMPQFQTCST QTHKIMENKM CDLTV


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