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Protein

Leptin receptor

Gene

Lepr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for hormone LEP/leptin (Probable). 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 (PubMed:8690163). 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 (By similarity). 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-cells. Leptin increases Th1 and suppresses Th2 cytokine production (By similarity).By similarity1 Publication1 Publication
Isoform A: May transport LEP across the blood-brain barrier. Binds LEP and mediates LEP endocytosis (PubMed:10698121). Does not induce phosphorylation of and activate STAT3 (By similarity).By similarity1 Publication
Isoform E: Antagonizes Isoform A and isoform B-mediated LEP binding and endocytosis.By similarity

GO - Molecular functioni

  • leptin receptor activity Source: UniProtKB
  • peptide hormone binding Source: RGD
  • protein-hormone receptor activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • angiogenesis Source: UniProtKB
  • bone growth Source: UniProtKB
  • cellular response to organic substance Source: RGD
  • eating behavior Source: RGD
  • energy homeostasis Source: UniProtKB
  • female pregnancy Source: RGD
  • generation of precursor metabolites and energy Source: RGD
  • glucose homeostasis Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: GOC
  • leptin-mediated signaling pathway Source: RGD
  • male gonad development Source: RGD
  • negative regulation of autophagy Source: UniProtKB
  • negative regulation of eating behavior Source: RGD
  • negative regulation of locomotor rhythm Source: RGD
  • ovulation from ovarian follicle Source: RGD
  • phagocytosis Source: UniProtKB
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: RGD
  • positive regulation of MAPK cascade Source: RGD
  • regulation of bone remodeling Source: UniProtKB
  • regulation of energy homeostasis Source: UniProtKB
  • regulation of feeding behavior Source: UniProtKB
  • response to dexamethasone Source: RGD
  • response to estrogen Source: RGD
  • response to hypoxia Source: RGD
  • response to leptin Source: RGD
  • response to lipid Source: RGD
  • response to nicotine Source: RGD
  • response to nutrient Source: RGD
  • sexual reproduction Source: UniProtKB
  • T cell differentiation Source: UniProtKB
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Leptin receptor
Short name:
LEP-R
Alternative name(s):
OB receptor
Short name:
OB-R
CD_antigen: CD295
Gene namesi
Name:Lepr
Synonyms:Fa, Obr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3001. Lepr.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Basolateral cell membrane By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 839818ExtracellularSequence analysisAdd
BLAST
Transmembranei840 – 86021HelicalSequence analysisAdd
BLAST
Topological domaini861 – 1162302CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB-SubCell
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

The fatty (Fa) mutation produces profound obesity of early onset caused by hyperphagia, defective non-shivering thermogenesis, and preferential deposition of energy into adipose tissue.

Keywords - Diseasei

Disease mutation, Obesity

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 11621141Leptin receptorPRO_0000010908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 90By similarity
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence analysis
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi89 ↔ 99By similarity
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence analysis
Disulfide bondi131 ↔ 142By similarity
Disulfide bondi186 ↔ 195By similarity
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi188 ↔ 193By similarity
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi350 ↔ 410By similarity
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence analysis
Disulfide bondi411 ↔ 416By similarity
Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence analysis
Disulfide bondi434 ↔ 445By similarity
Disulfide bondi471 ↔ 526By similarity
Disulfide bondi486 ↔ 496By similarity
Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence analysis
Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence analysis
Glycosylationi657 – 6571N-linked (GlcNAc...)Sequence analysis
Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence analysis
Glycosylationi686 – 6861N-linked (GlcNAc...)Sequence analysis
Glycosylationi695 – 6951N-linked (GlcNAc...)Sequence analysis
Glycosylationi698 – 6981N-linked (GlcNAc...)Sequence analysis
Glycosylationi726 – 7261N-linked (GlcNAc...)Sequence analysis
Modified residuei880 – 8801PhosphoserineBy similarity
Modified residuei985 – 9851Phosphotyrosine; by JAK2By similarity
Modified residuei1077 – 10771PhosphotyrosineBy similarity
Modified residuei1138 – 11381Phosphotyrosine; by JAK2By similarity

Post-translational modificationi

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ62959.
PRIDEiQ62959.

PTM databases

PhosphoSiteiQ62959.

Expressioni

Tissue specificityi

Isoform B is expressed in kidney, liver, lung, ovary, spleen and uterus. Increased level in uterus during gestation (PubMed:8772180). Isoform A and isoform C are predominantly expressed in cerebral microvessels and choroid plexus, with lower levels in cortex, cerebellum and hypothalamus but also liver and lung (PubMed:11861497). Isoform F is expressed at high levels in brain, liver and spleen and less in stomach, kidney, thymus, heart, lung and hypothalamus (PubMed:11861497, PubMed:8772180).2 Publications

Interactioni

Subunit structurei

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). Interaction with SOCS3 inhibits JAK/STAT signaling and MAPK cascade (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi246689. 1 interaction.
STRINGi10116.ENSRNOP00000046647.

Structurei

3D structure databases

ProteinModelPortaliQ62959.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini238 – 33194Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini537 – 63296Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini637 – 72993Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini738 – 83194Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni465 – 48218Leptin-bindingBy similarityAdd
BLAST
Regioni891 – 8966Required for JAK2 activationBy similarity
Regioni896 – 9049Required for STAT3 phosphorylationBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi620 – 6245WSXWS motif
Motifi869 – 8779Box 1 motif

Domaini

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
The box 1 motif is required for JAK interaction and/or activation.

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKH4. Eukaryota.
ENOG4110JZP. LUCA.
HOVERGENiHBG000140.
InParanoidiQ62959.
KOiK05062.
PhylomeDBiQ62959.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003961. FN3_dom.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR010457. IgC2-like_lig-bd.
IPR015752. Lep_receptor.
[Graphical view]
PANTHERiPTHR23036:SF109. PTHR23036:SF109. 3 hits.
PfamiPF06328. Lep_receptor_Ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 3 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: Q62959-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTCQKFYVVL LHWEFLYVIT ALNLAYPTSP WRFKLFCAPP STTDDSFLSP
60 70 80 90 100
AGVPNNTSSL KGASEALVEA KFNSTGIYVS ELSKTIFHCC FGNEQGQNCS
110 120 130 140 150
ALTGNTEGKT LASVVKPLVF RQLGVNWDIE CWMKGDLTLF ICHMEPLLKN
160 170 180 190 200
PFKNYDSKVH LLYDLPEVID DLPLPPLKDS FQTVQCNCSV RECECHVPVP
210 220 230 240 250
RAKVNYALLM YLEITSAGVS FQSPLMSLQP MLVVKPDPPL GLRMEVTDDG
260 270 280 290 300
NLKISWDSQT KAPFPLQYQV KYLENSTIVR EAAEIVSDTS LLVDSVLPGS
310 320 330 340 350
SYEVQVRSKR LDGSGVWSDW SLPQLFTTQD VMYFPPKILT SVGSNASFCC
360 370 380 390 400
IYKNENQTIS SKQIVWWMNL AEKIPETQYN TVSDHISKVT FSNLKATRPR
410 420 430 440 450
GKFTYDAVYC CNEQACHHRY AELYVIDVNI NISCETDGYL TKMTCRWSPS
460 470 480 490 500
TIQSLVGSTV QLRYHRRSLY CPDNPSIRPT SELKNCVLQT DGFYECVFQP
510 520 530 540 550
IFLLSGYTMW IRINHSLGSL DSPPTCVLPD SVVKPLPPSN VKAEITINTG
560 570 580 590 600
LLKVSWEKPV FPENNLQFQI RYGLNGKEIQ WKTHEVFDAK SKSASLPVSD
610 620 630 640 650
LCAVYVVQVR CRRLDGLGYW SNWSSPAYTL VMDVKVPMRG PEFWRIMDGD
660 670 680 690 700
ITKKERNVTL LWKPLMKNDS LCSVRRYVVK HRTAHNGTWS QDVGNQTNLT
710 720 730 740 750
FLWAESAHTV TVLAINSIGA SLVNFNLTFS WPMSKVNAVQ SLSAYPLSSS
760 770 780 790 800
CVILSWTLSP NDYSLLYLVI EWKNLNDDDG MKWLRIPSNV NKYYIHDNFI
810 820 830 840 850
PIEKYQFSLY PVFMEGVGKP KIINGFTKDD IAKQQNDAGL YVIVPIIISS
860 870 880 890 900
CVLLLGTLLI SHQRMKKLFW DDVPNPKNCS WAQGLNFQKP ETFEHLFTKH
910 920 930 940 950
AESVIFGPLL LEPEPVSEEI SVDTAWKNKD EMVPAAMVSL LLTTPDSTRG
960 970 980 990 1000
SICISDQCNS ANFSGAQSTQ GTCEDECQSQ PSVKYATLVS NVKTVETDEE
1010 1020 1030 1040 1050
QGAIHSSVSQ CIARKHSPLR QSFSSNSWEI EAQAFFLLSD HPPNVISPQL
1060 1070 1080 1090 1100
SFSGLDELLE LEGNFPEENH GEKSVYYLGV SSGNKRENDM LLTDEAGVLC
1110 1120 1130 1140 1150
PFPAHCLFSD IRILQESCSH FVENNLNLGT SGKNFVPYMP QFQSCSTHSH
1160
KIIENKMCDL TV
Length:1,162
Mass (Da):130,833
Last modified:November 1, 1996 - v1
Checksum:iBA7AC2CA2D2E62AF
GO
Isoform A (identifier: Q62959-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     890-894: PETFE → RADTL
     895-1162: Missing.

Show »
Length:894
Mass (Da):101,283
Checksum:iAB30482E47EE11F5
GO
Isoform C (identifier: Q62959-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     890-892: PET → VTV
     893-1162: Missing.

Show »
Length:892
Mass (Da):101,025
Checksum:iD052312E11F59B6C
GO
Isoform D (identifier: Q62959-6)

Sequence is not available
Length:
Mass (Da):
Isoform E (identifier: Q62959-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     797-805: DNFIPIEKY → GMCTVLLLN
     806-1162: Missing.

Show »
Length:805
Mass (Da):91,088
Checksum:iE8E5090C346530E5
GO
Isoform F (identifier: Q62959-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     890-895: PETFEH → IMPGRN
     896-1162: Missing.

Show »
Length:895
Mass (Da):101,395
Checksum:iFAE80985E513BE11
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → M in AAB06616 (Ref. 4) Curated
Sequence conflicti12 – 121H → P in BAA24899 (Ref. 8) Curated
Sequence conflicti34 – 341K → R in BAA24899 (Ref. 8) Curated
Sequence conflicti415 – 4173ACH → QCQ in AAB03088 (PubMed:8772180).Curated
Sequence conflicti422 – 4221E → D in AAB03088 (PubMed:8772180).Curated
Sequence conflicti493 – 4931F → L in AAB03088 (PubMed:8772180).Curated
Sequence conflicti498 – 4981F → S in AAB03088 (PubMed:8772180).Curated
Sequence conflicti612 – 6121R → Q in AAB03088 (PubMed:8772180).Curated
Sequence conflicti690 – 6901S → T in AAB03088 (PubMed:8772180).Curated
Sequence conflicti703 – 7042WA → SG in AAB03088 (PubMed:8772180).Curated
Sequence conflicti714 – 7141A → D in AAB03088 (PubMed:8772180).Curated
Sequence conflicti738 – 7392AV → GW in AAB03088 (PubMed:8772180).Curated
Sequence conflicti751 – 7522CV → SL in AAB40654 (Ref. 10) Curated
Sequence conflicti766 – 7661L → S in AAB63202 (PubMed:9268737).Curated
Sequence conflicti785 – 7851R → K in AAB63202 (PubMed:9268737).Curated
Sequence conflicti794 – 7941Y → N in AAB63202 (PubMed:9268737).Curated
Sequence conflicti846 – 8461I → V in AAB63201 (PubMed:9268737).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti269 – 2691Q → P in FA. 5 Publications

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei797 – 8059DNFIPIEKY → GMCTVLLLN in isoform E. 2 PublicationsVSP_001709
Alternative sequencei806 – 1162357Missing in isoform E. 2 PublicationsVSP_001710Add
BLAST
Alternative sequencei890 – 8956PETFEH → IMPGRN in isoform F. 1 PublicationVSP_001711
Alternative sequencei890 – 8945PETFE → RADTL in isoform A. 3 PublicationsVSP_001705
Alternative sequencei890 – 8923PET → VTV in isoform C. 1 PublicationVSP_001707
Alternative sequencei893 – 1162270Missing in isoform C. 1 PublicationVSP_001708Add
BLAST
Alternative sequencei895 – 1162268Missing in isoform A. 3 PublicationsVSP_001706Add
BLAST
Alternative sequencei896 – 1162267Missing in isoform F. 1 PublicationVSP_001712Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52966 mRNA. Translation: AAC52587.1.
D84550 mRNA. Translation: BAA12697.1.
D84551 mRNA. Translation: BAA12698.1.
D85557 mRNA. Translation: BAA12830.1.
D85558 mRNA. Translation: BAA12831.1.
D85559 mRNA. Translation: BAA12832.1.
U60151 mRNA. Translation: AAB06616.1.
D84125 mRNA. Translation: BAA12230.1.
D84126 mRNA. Translation: BAA12231.1.
AF287268 mRNA. Translation: AAF89300.1.
U53144 mRNA. Translation: AAB03088.1.
AB011006 Genomic DNA. Translation: BAA24899.1.
AF007818 mRNA. Translation: AAB63201.1.
AF007819 mRNA. Translation: AAB63202.1.
U67207 mRNA. Translation: AAB40654.1.
AF304191 mRNA. Translation: AAG22823.1.
PIRiJC4895. PC4184.
S74225.
RefSeqiNP_036728.1. NM_012596.1. [Q62959-1]
UniGeneiRn.9891.

Genome annotation databases

GeneIDi24536.
KEGGirno:24536.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52966 mRNA. Translation: AAC52587.1.
D84550 mRNA. Translation: BAA12697.1.
D84551 mRNA. Translation: BAA12698.1.
D85557 mRNA. Translation: BAA12830.1.
D85558 mRNA. Translation: BAA12831.1.
D85559 mRNA. Translation: BAA12832.1.
U60151 mRNA. Translation: AAB06616.1.
D84125 mRNA. Translation: BAA12230.1.
D84126 mRNA. Translation: BAA12231.1.
AF287268 mRNA. Translation: AAF89300.1.
U53144 mRNA. Translation: AAB03088.1.
AB011006 Genomic DNA. Translation: BAA24899.1.
AF007818 mRNA. Translation: AAB63201.1.
AF007819 mRNA. Translation: AAB63202.1.
U67207 mRNA. Translation: AAB40654.1.
AF304191 mRNA. Translation: AAG22823.1.
PIRiJC4895. PC4184.
S74225.
RefSeqiNP_036728.1. NM_012596.1. [Q62959-1]
UniGeneiRn.9891.

3D structure databases

ProteinModelPortaliQ62959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246689. 1 interaction.
STRINGi10116.ENSRNOP00000046647.

PTM databases

PhosphoSiteiQ62959.

Proteomic databases

PaxDbiQ62959.
PRIDEiQ62959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24536.
KEGGirno:24536.

Organism-specific databases

CTDi3953.
RGDi3001. Lepr.

Phylogenomic databases

eggNOGiENOG410IKH4. Eukaryota.
ENOG4110JZP. LUCA.
HOVERGENiHBG000140.
InParanoidiQ62959.
KOiK05062.
PhylomeDBiQ62959.

Miscellaneous databases

NextBioi603610.
PROiQ62959.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003961. FN3_dom.
IPR003529. Hematopoietin_rcpt_Gp130_CS.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR010457. IgC2-like_lig-bd.
IPR015752. Lep_receptor.
[Graphical view]
PANTHERiPTHR23036:SF109. PTHR23036:SF109. 3 hits.
PfamiPF06328. Lep_receptor_Ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 3 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Leptin receptor missense mutation in the fatty Zucker rat."
    Phillips M.S., Liu Q., Hammond H.A., Dugan V., Hey P.J., Caskey C.T., Hess J.F.
    Nat. Genet. 13:18-19(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT FA PRO-269.
    Strain: Zucker.
    Tissue: Hypothalamus.
  2. "Substitution at codon 269 (glutamine --> proline) of the leptin receptor (OB-R) cDNA is the only mutation found in the Zucker fatty (fa/fa) rat."
    Iida M., Murakami T., Ishida K., Mizuno A., Kuwajima M., Shima K.
    Biochem. Biophys. Res. Commun. 224:597-604(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT FA PRO-269.
    Strain: Sprague-Dawley and Zucker fatty.
    Tissue: Brain.
  3. "Molecular cloning of rat leptin receptor isoform complementary DNAs -- identification of a missense mutation in Zucker fatty (fa/fa) rats."
    Takaya K., Ogawa Y., Isse N., Okazaki T., Satoh N., Masuzaki H., Mori K., Tamura N., Hosoda K., Nakao K.
    Biochem. Biophys. Res. Commun. 225:75-83(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND E), VARIANT FA PRO-269.
    Strain: Sprague-Dawley and Zucker fatty.
  4. "Cloning of the rat leptin receptor."
    Karlsson C., Lindell K., Robinson I.C.A.F., Carlsson L.M.S., Carlsson B.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
  5. "Phenotype-linked amino acid alteration in leptin receptor cDNA from Zucker fatty (fa/fa) rat."
    Iida M., Murakami T., Ishida K., Mizuno A., Kuwajima M., Shima K.
    Biochem. Biophys. Res. Commun. 222:19-26(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT FA PRO-269.
    Strain: Sprague-Dawley and Zucker fatty.
  6. "Molecular cloning, sequencing, and recombinant expression of the long form of the rat leptin receptor isolated from whole spleen RNA."
    Park J.H., Ju S.K., Na S.Y., You K.H., Kim K.L.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Strain: Sprague-Dawley.
    Tissue: Spleen.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  8. "Analysis of rat leptin receptor gene."
    Morishita T., Hidaka T., Kuzuyama T., Noguchi T.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
  9. "Increase in serum leptin and uterine leptin receptor messenger RNA levels during pregnancy in rats."
    Chien E.K., Hara M., Rouard M., Yano H., Phillippe M., Polonsky K.S., Bell G.I.
    Biochem. Biophys. Res. Commun. 237:476-480(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 557-802 AND 843-892 (ISOFORMS C AND E).
    Strain: Sprague-Dawley.
  10. "Identification of a leptin receptor in islet."
    Ma Z.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 694-878.
    Strain: Sprague-Dawley.
    Tissue: Pancreas.
  11. "Leptin receptor gene expression in rat kidney."
    Totsune K., Takahashi K., Mackenzie H.S., Murakami O., Arihara Z., Sone M., Satoh F., Mouri T., Brenner B.M., Ito S.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 821-894 (ISOFORM A).
    Strain: Wistar Munich.
    Tissue: Kidney.
  12. "Decreased transport of leptin across the blood-brain barrier in rats lacking the short form of the leptin receptor."
    Kastin A.J., Pan W., Maness L.M., Koletsky R.J., Ernsberger P.
    Peptides 20:1449-1453(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM A).
  13. "Characterizaton of short isoforms of the leptin receptor in rat cerebral microvessels and of brain uptake of leptin in mouse models of obesity."
    Hileman S.M., Pierroz D.D., Masuzaki H., Bjoerbaek C., El-Haschimi K., Banks W.A., Flier J.S.
    Endocrinology 143:775-783(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "20 years of leptin: connecting leptin signaling to biological function."
    Allison M.B., Myers M.G. Jr.
    J. Endocrinol. 223:T25-T35(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, SUBUNIT.
  15. Cited for: VARIANT FA PRO-269.

Entry informationi

Entry nameiLEPR_RAT
AccessioniPrimary (citable) accession number: Q62959
Secondary accession number(s): O35772
, O35773, O54805, P70493, P70494, P70495, P97589, Q62960, Q63007, Q63385, Q63386, Q9ERI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.