ID LEP_RAT Reviewed; 167 AA. AC P50596; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 66. DE RecName: Full=Leptin; DE AltName: Full=Obesity factor; DE Flags: Precursor; GN Name=Lep; Synonyms=Ob; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX MEDLINE=95386724; PubMed=7657834; RA Ogawa Y., Masuzaki H., Isse N., Okazaki T., Mori K., Shigemoto M., RA Satoh N., Tamura N., Hosoda K., Yoshimasa Y., Jingami H., Kawada T., RA Nakao K.; RT "Molecular cloning of rat obese cDNA and augmented gene expression in RT genetically obese Zucker fatty (fa/fa) rats."; RL J. Clin. Invest. 96:1647-1652(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue; RX MEDLINE=95314614; PubMed=7794258; DOI=10.1006/bbrc.1995.1837; RA Funahashi T., Shimomura I., Hiraoka H., Arai T., Takahashi M., RA Nakamura T., Nozaki S., Yamashita S., Takemura K., Tokunaga K.; RT "Enhanced expression of rat obese (ob) gene in adipose tissues of RT ventromedial hypothalamus (VMH)-lesioned rats."; RL Biochem. Biophys. Res. Commun. 211:469-475(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Leto, OLETF, and Zucker; TISSUE=Adipose tissue; RX MEDLINE=95251725; PubMed=7733988; DOI=10.1006/bbrc.1995.1589; RA Murakami T., Shima K.; RT "Cloning of rat obese cDNA and its expression in obese rats."; RL Biochem. Biophys. Res. Commun. 209:944-952(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-167. RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue; RA Donohoue P.A., Sivitz W.I., Bailey H.L.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May function as part of a signaling pathway that acts to CC regulate the size of the body fat depot. An increase in the level CC of Lep may act directly or indirectly on the CNS to inhibit food CC intake and/or regulate energy expenditure as part of a homeostatic CC mechanism to maintain constancy of the adipose mass. CC -!- SUBCELLULAR LOCATION: Secreted (Probable). CC -!- SIMILARITY: Belongs to the leptin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D45862; BAA08296.1; -; mRNA. DR EMBL; S78586; AAB34657.2; -; mRNA. DR EMBL; D49653; BAA08529.1; -; mRNA. DR EMBL; U48849; AAC52514.1; -; mRNA. DR IPI; IPI00199521; -. DR PIR; PC4034; LTRT. DR RefSeq; NP_037208.1; -. DR UniGene; Rn.44444; -. DR HSSP; P41159; 1AX8. DR SMR; P50596; 24-167. DR Ensembl; ENSRNOG00000006059; Rattus norvegicus. DR GeneID; 25608; -. DR KEGG; rno:25608; -. DR RGD; 3000; Lep. DR HOVERGEN; P50596; -. DR OMA; P50596; GLDFIPG. DR NextBio; 607339; -. DR ArrayExpress; P50596; -. DR GermOnline; ENSRNOG00000006059; Rattus norvegicus. DR GO; GO:0005615; C:extracellular space; IDA:HGNC. DR GO; GO:0005125; F:cytokine activity; TAS:RGD. DR GO; GO:0005179; F:hormone activity; IDA:RGD. DR GO; GO:0051428; F:peptide hormone receptor binding; IDA:RGD. DR GO; GO:0008343; P:adult feeding behavior; ISS:HGNC. DR GO; GO:0019933; P:cAMP-mediated signaling; TAS:RGD. DR GO; GO:0006112; P:energy reserve metabolic process; IDA:RGD. DR GO; GO:0009062; P:fatty acid catabolic process; IDA:RGD. DR GO; GO:0007259; P:JAK-STAT cascade; TAS:RGD. DR GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:RGD. DR GO; GO:0032099; P:negative regulation of appetite; ISS:HGNC. DR GO; GO:0009892; P:negative regulation of metabolic process; IDA:RGD. DR GO; GO:0001542; P:ovulation from ovarian follicle; IDA:RGD. DR GO; GO:0043410; P:positive regulation of MAPKKK cascade; IDA:RGD. DR InterPro; IPR012351; 4_helix_cytokine_core. DR InterPro; IPR000065; Leptin. DR Gene3D; G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1. DR PANTHER; PTHR11724; Leptin; 1. DR Pfam; PF02024; Leptin; 1. DR PIRSF; PIRSF001837; Leptin; 1. DR PRINTS; PR00495; LEPTIN. DR ProDom; PD005698; Leptin; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Obesity; Secreted; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 167 Leptin. FT /FTId=PRO_0000017690. FT DISULFID 117 167 By similarity. FT CONFLICT 32 32 K -> T (in Ref. 2). FT CONFLICT 163 163 L -> V (in Ref. 4; AAC52514). SQ SEQUENCE 167 AA; 18866 MW; 3B5B563DA42EC84E CRC64; MCWRPLCRFL WLWSYLSYVQ AVPIHKVQDD TKTLIKTIVT RINDISHTQS VSARQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQILTSLP SQNVLQIAHD LENLRDLLHL LAFSKSCSLP QTRGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDLSPEC //