LEP_MOUSE
ID LEP_MOUSE Reviewed; 167 AA.
AC P41160;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Leptin;
DE AltName: Full=Obesity factor;
DE Flags: Precursor;
GN Name=Lep; Synonyms=Ob;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7984236; DOI=10.1038/372425a0;
RA Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.;
RT "Positional cloning of the mouse obese gene and its human homologue.";
RL Nature 372:425-432(1994).
RN [2]
RP ERRATUM OF PUBMED:7984236.
RA Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.;
RL Nature 374:479-479(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RA Chehab F.F., Lim M.E.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8589726; DOI=10.1038/ng0396-318;
RA Chehab F.F., Lim M.E., Lu R.;
RT "Correction of the sterility defect in homozygous obese female mice by
RT treatment with the human recombinant leptin.";
RL Nat. Genet. 12:318-320(1996).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9732873; DOI=10.1038/29795;
RA Lord G.M., Matarese G., Howard J.K., Baker R.J., Bloom S.R., Lechler R.I.;
RT "Leptin modulates the T-cell immune response and reverses starvation-
RT induced immunosuppression.";
RL Nature 394:897-901(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10660043; DOI=10.1016/s0092-8674(00)81558-5;
RA Ducy P., Amling M., Takeda S., Priemel M., Schilling A.F., Beil F.T.,
RA Shen J., Vinson C., Rueger J.M., Karsenty G.;
RT "Leptin inhibits bone formation through a hypothalamic relay: a central
RT control of bone mass.";
RL Cell 100:197-207(2000).
RN [7]
RP FUNCTION.
RX PubMed=11373681; DOI=10.1038/35078085;
RA Cowley M.A., Smart J.L., Rubinstein M., Cerdan M.G., Diano S.,
RA Horvath T.L., Cone R.D., Low M.J.;
RT "Leptin activates anorexigenic POMC neurons through a neural network in the
RT arcuate nucleus.";
RL Nature 411:480-484(2001).
RN [8]
RP FUNCTION.
RX PubMed=12594516; DOI=10.1038/nature01388;
RA Bates S.H., Stearns W.H., Dundon T.A., Schubert M., Tso A.W., Wang Y.,
RA Banks A.S., Lavery H.J., Haq A.K., Maratos-Flier E., Neel B.G.,
RA Schwartz M.W., Myers M.G. Jr.;
RT "STAT3 signalling is required for leptin regulation of energy balance but
RT not reproduction.";
RL Nature 421:856-859(2003).
RN [9]
RP REVIEW OF FUNCTION IN IMMUNITY.
RX PubMed=15122202; DOI=10.1038/nri1350;
RA La Cava A., Matarese G.;
RT "The weight of leptin in immunity.";
RL Nat. Rev. Immunol. 4:371-379(2004).
RN [10]
RP FUNCTION.
RX PubMed=15899045; DOI=10.1186/ar1708;
RA Otero M., Lago R., Lago F., Reino J.J., Gualillo O.;
RT "signaling pathway involved in nitric oxide synthase type II activation in
RT chondrocytes: synergistic effect of leptin with interleukin-1.";
RL Arthritis Res. Ther. 7:R581-R591(2005).
RN [11]
RP FUNCTION.
RX PubMed=16825198; DOI=10.1074/jbc.m601991200;
RA Gonzalez R.R., Cherfils S., Escobar M., Yoo J.H., Carino C., Styer A.K.,
RA Sullivan B.T., Sakamoto H., Olawaiye A., Serikawa T., Lynch M.P.,
RA Rueda B.R.;
RT "Leptin signaling promotes the growth of mammary tumors and increases the
RT expression of vascular endothelial growth factor (VEGF) and its receptor
RT type two (VEGF-R2).";
RL J. Biol. Chem. 281:26320-26328(2006).
RN [12]
RP FUNCTION.
RX PubMed=20620997; DOI=10.1016/j.cmet.2010.05.010;
RA Ramadori G., Fujikawa T., Fukuda M., Anderson J., Morgan D.A.,
RA Mostoslavsky R., Stuart R.C., Perello M., Vianna C.R., Nillni E.A.,
RA Rahmouni K., Coppari R.;
RT "SIRT1 deacetylase in POMC neurons is required for homeostatic defenses
RT against diet-induced obesity.";
RL Cell Metab. 12:78-87(2010).
RN [13]
RP REVIEW OF FUNCTION.
RX PubMed=25232147; DOI=10.1530/joe-14-0404;
RA Allison M.B., Myers M.G. Jr.;
RT "20 years of leptin: connecting leptin signaling to biological function.";
RL J. Endocrinol. 223:T25-T35(2014).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25060689; DOI=10.1016/j.metabol.2014.06.010;
RA Cassano S., Pucino V., La Rocca C., Procaccini C., De Rosa V., Marone G.,
RA Matarese G.;
RT "Leptin modulates autophagy in human CD4+CD25- conventional T cells.";
RL Metabolism 63:1272-1279(2014).
RN [15]
RP FUNCTION.
RX PubMed=25383904; DOI=10.1038/nn.3861;
RA Flak J.N., Patterson C.M., Garfield A.S., D'Agostino G., Goforth P.B.,
RA Sutton A.K., Malec P.A., Wong J.M., Germani M., Jones J.C., Rajala M.,
RA Satin L., Rhodes C.J., Olson D.P., Kennedy R.T., Heisler L.K.,
RA Myers M.G. Jr.;
RT "Leptin-inhibited PBN neurons enhance responses to hypoglycemia in negative
RT energy balance.";
RL Nat. Neurosci. 17:1744-1750(2014).
CC -!- FUNCTION: Key player in the regulation of energy balance and body
CC weight control. Once released into the circulation, has central and
CC peripheral effects by binding LEPR, found in many tissues, which
CC results in the activation of several major signaling pathways
CC (PubMed:15899045, PubMed:16825198, PubMed:11373681, PubMed:12594516,
CC PubMed:20620997). In the hypothalamus, acts as an appetite-regulating
CC factor that induces a decrease in food intake and an increase in energy
CC consumption by inducing anorexinogenic factors and suppressing
CC orexigenic neuropeptides, also regulates bone mass and secretion of
CC hypothalamo-pituitary-adrenal hormones. In the periphery, increases
CC basal metabolism, influences reproductive function, regulates
CC pancreatic beta-cell function and insulin secretion, is pro-angiogenic
CC for endothelial cell and affects innate and adaptive immunity (By
CC similarity) (PubMed:8589726, PubMed:10660043, PubMed:25383904,
CC PubMed:25060689, PubMed:9732873, PubMed:12594516). In the arcuate
CC nucleus of the hypothalamus, activates by depolarization POMC neurons
CC inducing FOS and SOCS3 expression to release anorexigenic peptides and
CC inhibits by hyperpolarization NPY neurons inducing SOCS3 with a
CC consequent reduction on release of orexigenic peptides (By similarity)
CC (PubMed:20620997, PubMed:11373681). In addition to its known satiety
CC inducing effect, has a modulatory role in nutrient absorption. In the
CC intestine, reduces glucose absorption by enterocytes by activating PKC
CC and leading to a sequential activation of p38, PI3K and ERK signaling
CC pathways which exerts an inhibitory effect on glucose absorption. Acts
CC as a growth factor on certain tissues, through the activation of
CC different signaling pathways increases expression of genes involved in
CC cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA,
CC via MAPK1/3 and PI3K-AKT1 pathways (By similarity) (PubMed:16825198,
CC PubMed:20620997). May also play an apoptotic role via JAK2-STAT3
CC pathway and up-regulation of BIRC5 expression (By similarity). Pro-
CC angiogenic, has mitogenic activity on vascular endothelial cells and
CC plays a role in matrix remodeling by regulating the expression of
CC matrix metalloproteinases (MMPs) and tissue inhibitors of
CC metalloproteinases (TIMPs) (PubMed:16825198). In innate immunity,
CC modulates the activity and function of neutrophils by increasing
CC chemotaxis and the secretion of oxygen radicals. Increases phagocytosis
CC by macrophages and enhances secretion of pro-inflammatory mediators.
CC Increases cytotoxic ability of NK cells (Probable). Plays a pro-
CC inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes
CC the production of IL6, IL8 and Prostaglandin E2, through a signaling
CC pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38
CC (PubMed:15899045). In adaptive immunity, promotes the switch of memory
CC T-cells towards T helper-1 cell immune responses (By similarity).
CC Increases CD4(+)CD25(-) T cells proliferation and reduces autophagy
CC during TCR (T cell receptor) stimulation, through MTOR signaling
CC pathway activation and BCL2 up-regulation (PubMed:25060689).
CC {ECO:0000250|UniProtKB:P41159, ECO:0000250|UniProtKB:P50596,
CC ECO:0000269|PubMed:10660043, ECO:0000269|PubMed:11373681,
CC ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:15899045,
CC ECO:0000269|PubMed:16825198, ECO:0000269|PubMed:20620997,
CC ECO:0000269|PubMed:25060689, ECO:0000269|PubMed:25383904,
CC ECO:0000269|PubMed:8589726, ECO:0000269|PubMed:9732873,
CC ECO:0000305|PubMed:15122202, ECO:0000305|PubMed:25232147}.
CC -!- INTERACTION:
CC P41160; P48356: Lepr; NbExp=6; IntAct=EBI-16108810, EBI-2257257;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25232147}.
CC -!- DISEASE: Note=Defects in Lep are the cause of profound obesity and type
CC II diabetes.
CC -!- DISRUPTION PHENOTYPE: Mutants are severely obese and sterile
CC (PubMed:8589726). Animals have an increased bone formation leading to
CC high bone mass (PubMed:10660043). Have impaired T-cell immunity, Th2
CC responses are favoured in mutants (PubMed:9732873). CD4(+)CD25(-) T-
CC cells of mutant mice show high levels of autophagy (PubMed:25060689).
CC {ECO:0000269|PubMed:10660043, ECO:0000269|PubMed:25060689,
CC ECO:0000269|PubMed:8589726, ECO:0000269|PubMed:9732873}.
CC -!- SIMILARITY: Belongs to the leptin family. {ECO:0000305}.
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DR EMBL; U18812; AAA64564.1; -; mRNA.
DR EMBL; U22421; AAA64213.1; -; Genomic_DNA.
DR CCDS; CCDS19955.1; -.
DR PIR; S50863; LTMS.
DR RefSeq; NP_032519.1; NM_008493.3.
DR AlphaFoldDB; P41160; -.
DR SMR; P41160; -.
DR BioGRID; 201138; 4.
DR CORUM; P41160; -.
DR DIP; DIP-60999N; -.
DR IntAct; P41160; 1.
DR STRING; 10090.ENSMUSP00000067046; -.
DR PhosphoSitePlus; P41160; -.
DR CPTAC; CPTAC-1473; -.
DR PaxDb; P41160; -.
DR PRIDE; P41160; -.
DR ProteomicsDB; 265060; -.
DR Antibodypedia; 3389; 1446 antibodies from 43 providers.
DR DNASU; 16846; -.
DR Ensembl; ENSMUST00000069789; ENSMUSP00000067046; ENSMUSG00000059201.
DR GeneID; 16846; -.
DR KEGG; mmu:16846; -.
DR UCSC; uc009bcv.1; mouse.
DR CTD; 3952; -.
DR MGI; MGI:104663; Lep.
DR VEuPathDB; HostDB:ENSMUSG00000059201; -.
DR eggNOG; ENOG502S5K5; Eukaryota.
DR GeneTree; ENSGT00390000011772; -.
DR HOGENOM; CLU_132715_0_0_1; -.
DR InParanoid; P41160; -.
DR OMA; MRCGPLC; -.
DR OrthoDB; 1350528at2759; -.
DR PhylomeDB; P41160; -.
DR TreeFam; TF105086; -.
DR Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 16846; 0 hits in 74 CRISPR screens.
DR ChiTaRS; H2-Ob; mouse.
DR PRO; PR:P41160; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P41160; protein.
DR Bgee; ENSMUSG00000059201; Expressed in thoracic mammary gland and 50 other tissues.
DR ExpressionAtlas; P41160; baseline and differential.
DR Genevisible; P41160; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:1990460; F:leptin receptor binding; ISO:MGI.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IGI:MGI.
DR GO; GO:0008343; P:adult feeding behavior; IDA:HGNC-UCL.
DR GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; IDA:MGI.
DR GO; GO:0098868; P:bone growth; IMP:UniProtKB.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; ISO:MGI.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0071298; P:cellular response to L-ascorbic acid; IEA:Ensembl.
DR GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IGI:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:MGI.
DR GO; GO:0042755; P:eating behavior; IGI:MGI.
DR GO; GO:0051541; P:elastin metabolic process; IMP:MGI.
DR GO; GO:0006112; P:energy reserve metabolic process; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IGI:MGI.
DR GO; GO:0009062; P:fatty acid catabolic process; ISO:MGI.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IGI:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR GO; GO:0006114; P:glycerol biosynthetic process; ISO:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IGI:MGI.
DR GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032099; P:negative regulation of appetite; IDA:HGNC-UCL.
DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0061037; P:negative regulation of cartilage development; ISO:MGI.
DR GO; GO:0070093; P:negative regulation of glucagon secretion; IDA:BHF-UCL.
DR GO; GO:0046325; P:negative regulation of glucose import; ISS:UniProtKB.
DR GO; GO:2000486; P:negative regulation of glutamine transport; ISO:MGI.
DR GO; GO:0010888; P:negative regulation of lipid storage; ISO:MGI.
DR GO; GO:0009892; P:negative regulation of metabolic process; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0001542; P:ovulation from ovarian follicle; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
DR GO; GO:0001890; P:placenta development; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI.
DR GO; GO:1904651; P:positive regulation of fat cell apoptotic process; ISO:MGI.
DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IEA:Ensembl.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0043270; P:positive regulation of ion transport; ISO:MGI.
DR GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0032310; P:prostaglandin secretion; ISS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0046850; P:regulation of bone remodeling; IMP:UniProtKB.
DR GO; GO:0090335; P:regulation of brown fat cell differentiation; IDA:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IGI:MGI.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:MGI.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IDA:MGI.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; IGI:MGI.
DR GO; GO:0060587; P:regulation of lipoprotein lipid oxidation; ISO:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IMP:MGI.
DR GO; GO:0032814; P:regulation of natural killer cell activation; ISS:UniProtKB.
DR GO; GO:0042269; P:regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0032817; P:regulation of natural killer cell proliferation; ISS:UniProtKB.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IMP:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR GO; GO:0019953; P:sexual reproduction; IMP:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000065; Leptin.
DR PANTHER; PTHR11724; PTHR11724; 1.
DR Pfam; PF02024; Leptin; 1.
DR PIRSF; PIRSF001837; Leptin; 1.
DR PRINTS; PR00495; LEPTIN.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW Diabetes mellitus; Disulfide bond; Obesity; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..167
FT /note="Leptin"
FT /id="PRO_0000017687"
FT DISULFID 117..167
FT /evidence="ECO:0000250"
FT VARIANT 49
FT /note="Missing (in 30% the clones)"
SQ SEQUENCE 167 AA; 18709 MW; D6783E6C76FD7116 CRC64;
MCWRPLCRFL WLWSYLSYVQ AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL
DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP
QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC
