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P48356

- LEPR_MOUSE

UniProt

P48356 - LEPR_MOUSE

Protein

Leptin receptor

Gene

Lepr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Receptor for obesity factor (leptin). On ligand binding, mediates signaling through JAK2/STAT3. Involved in the regulation of fat metabolism and, in a hematopoietic pathway, required for normal lymphopoiesis. May play a role in reproduction. Can also mediate the ERK/FOS signaling pathway.
    Isoform A may act to transport leptin to the cerebrospinal fluid.By similarity
    Isoform E could function as a transport protein.

    GO - Molecular functioni

    1. cytokine receptor activity Source: InterPro
    2. protein binding Source: BHF-UCL
    3. transmembrane signaling receptor activity Source: MGI

    GO - Biological processi

    1. cholesterol metabolic process Source: MGI
    2. negative regulation of gluconeogenesis Source: MGI
    3. negative regulation of hydrolase activity Source: MGI
    4. regulation of metabolic process Source: MGI
    5. signal transduction Source: MGI

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leptin receptor
    Short name:
    LEP-R
    Alternative name(s):
    B219
    OB receptor
    Short name:
    OB-R
    CD_antigen: CD295
    Gene namesi
    Name:Lepr
    Synonyms:Db, Obr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:104993. Lepr.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: MGI
    3. plasma membrane Source: Reactome
    4. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi985 – 9851Y → 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. 2 Publications
    Mutagenesisi1077 – 10771Y → F: No effect on EPO-induced tyrosine phosphorylation. 1 Publication
    Mutagenesisi1138 – 11381Y → 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. 2 Publications

    Keywords - Diseasei

    Obesity

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 11621141Leptin receptorPRO_0000010906Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi37 ↔ 90By similarity
    Glycosylationi41 – 411N-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
    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 residuei985 – 9851Phosphotyrosine; by JAK22 Publications
    Modified residuei1077 – 10771Phosphotyrosine1 Publication
    Modified residuei1138 – 11381Phosphotyrosine; by JAK21 Publication

    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 and, for interaction with SOCS3. Phosphorylation on Tyr-1138 is required for STAT3 binding/activation.2 Publications
    Phosphorylation of Tyr-985 is required for SOCS3 binding and SOCS3 mediated inhibition of leptin signaling, whereas phosphorylation of Tyr-1077 has a more accessory role.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP48356.
    PRIDEiP48356.

    PTM databases

    PhosphoSiteiP48356.

    Expressioni

    Tissue specificityi

    Isoform A: highest level of expression in lung and kidney, also present in kidney, heart, brain, spleen, liver, muscle, choroid plexus and hypothalamus. Isoform B: highest level of expression in hypothalamus and lower level in brain, testes and adipose tissue. Isoform E: expressed in adipose tissue, hypothalamus, heart, and testes.

    Gene expression databases

    ArrayExpressiP48356.
    BgeeiP48356.
    CleanExiMM_LEPR.
    GenevestigatoriP48356.

    Interactioni

    Subunit structurei

    On leptin stimulation, homodimerizes. The phosphorylated receptor binds a number of SH2 domain-containing proteins such as STAT3, PTPN11, and SOCS3. Interaction with SOCS3 inhibits JAK/STAT signaling.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BBS1Q8NFJ93EBI-6143588,EBI-1805484From a different organism.
    Plcg1Q620772EBI-2257257,EBI-300133

    Protein-protein interaction databases

    BioGridi201139. 3 interactions.
    DIPiDIP-42763N.
    IntActiP48356. 10 interactions.
    MINTiMINT-2569396.

    Structurei

    3D structure databases

    ProteinModelPortaliP48356.
    SMRiP48356. Positions 220-323, 359-830.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 839818ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini861 – 1162302CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei840 – 86021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini238 – 33194Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini329 – 42799Ig-likeAdd
    BLAST
    Domaini537 – 63296Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini637 – 72993Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini738 – 83295Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni465 – 48218Leptin-bindingBy similarityAdd
    BLAST
    Regioni891 – 8966Required for JAK2 activation

    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.1 Publication
    The box 1 motif is required for JAK interaction and/or activation.1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG29456.
    GeneTreeiENSGT00730000111209.
    HOVERGENiHBG000140.
    InParanoidiP48356.
    KOiK05062.
    OMAiSWAQGLN.
    OrthoDBiEOG7034GB.
    PhylomeDBiP48356.
    TreeFamiTF106501.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR003529. Hematopoietin_rcpt_Gp130_CS.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR010457. IgC2-like_lig-bd.
    IPR015752. Lep_receptor.
    [Graphical view]
    PANTHERiPTHR23036:SF11. PTHR23036:SF11. 1 hit.
    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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: P48356-1) [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

    MMCQKFYVVL LHWEFLYVIA ALNLAYPISP WKFKLFCGPP NTTDDSFLSP     50
    AGAPNNASAL KGASEAIVEA KFNSSGIYVP ELSKTVFHCC FGNEQGQNCS 100
    ALTDNTEGKT LASVVKASVF RQLGVNWDIE CWMKGDLTLF ICHMEPLPKN 150
    PFKNYDSKVH LLYDLPEVID DSPLPPLKDS FQTVQCNCSL RGCECHVPVP 200
    RAKLNYALLM YLEITSAGVS FQSPLMSLQP MLVVKPDPPL GLHMEVTDDG 250
    NLKISWDSQT MAPFPLQYQV KYLENSTIVR EAAEIVSATS LLVDSVLPGS 300
    SYEVQVRSKR LDGSGVWSDW SSPQVFTTQD VVYFPPKILT SVGSNASFHC 350
    IYKNENQIIS SKQIVWWRNL AEKIPEIQYS IVSDRVSKVT FSNLKATRPR 400
    GKFTYDAVYC CNEQACHHRY AELYVIDVNI NISCETDGYL TKMTCRWSPS 450
    TIQSLVGSTV QLRYHRRSLY CPDSPSIHPT SEPKNCVLQR DGFYECVFQP 500
    IFLLSGYTMW IRINHSLGSL DSPPTCVLPD SVVKPLPPSN VKAEITVNTG 550
    LLKVSWEKPV FPENNLQFQI RYGLSGKEIQ WKTHEVFDAK SKSASLLVSD 600
    LCAVYVVQVR CRRLDGLGYW SNWSSPAYTL VMDVKVPMRG PEFWRKMDGD 650
    VTKKERNVTL LWKPLTKNDS LCSVRRYVVK HRTAHNGTWS EDVGNRTNLT 700
    FLWTEPAHTV TVLAVNSLGA SLVNFNLTFS WPMSKVSAVE SLSAYPLSSS 750
    CVILSWTLSP DDYSLLYLVI EWKILNEDDG MKWLRIPSNV KKFYIHDNFI 800
    PIEKYQFSLY PVFMEGVGKP KIINGFTKDA IDKQQNDAGL YVIVPIIISS 850
    CVLLLGTLLI SHQRMKKLFW DDVPNPKNCS WAQGLNFQKP ETFEHLFTKH 900
    AESVIFGPLL LEPEPISEEI SVDTAWKNKD EMVPAAMVSL LLTTPDPESS 950
    SICISDQCNS ANFSGSQSTQ VTCEDECQRQ PSVKYATLVS NDKLVETDEE 1000
    QGFIHSPVSN CISSNHSPLR QSFSSSSWET EAQTFFLLSD QQPTMISPQL 1050
    SFSGLDELLE LEGSFPEENH REKSVCYLGV TSVNRRESGV LLTGEAGILC 1100
    TFPAQCLFSD IRILQERCSH FVENNLSLGT SGENFVPYMP QFQTCSTHSH 1150
    KIMENKMCDL TV 1162
    Length:1,162
    Mass (Da):130,789
    Last modified:February 1, 1996 - v1
    Checksum:i0E1E75B076BA60A2
    GO
    Isoform A (identifier: P48356-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:894
    Mass (Da):101,058
    Checksum:iDF9A7A0E5AC75A53
    GO
    Isoform C (identifier: P48356-3) [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):100,771
    Checksum:i726E5C075A53C9F3
    GO
    Isoform D (identifier: P48356-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         890-900: PETFEHLFTKH → DISFHEVFIFR
         901-1162: Missing.

    Show »
    Length:900
    Mass (Da):101,863
    Checksum:i7370A3C7BB5E7942
    GO
    Isoform E (identifier: P48356-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:805
    Mass (Da):90,887
    Checksum:i591B5DE008BDB898
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401F → I in AAC52705. (PubMed:8692797)Curated
    Sequence conflicti140 – 1401F → I in AAC52706. (PubMed:8692797)Curated
    Sequence conflicti140 – 1401F → I in AAC52707. (PubMed:8692797)Curated
    Sequence conflicti720 – 7201A → T in CAA71343. (PubMed:9322935)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti541 – 5411V → I in strain: NZO.
    Natural varianti600 – 6001D → N in strain: KK Obese. 1 Publication
    Natural varianti651 – 6511V → I in strain: NZO.
    Natural varianti1044 – 10441T → I in strain: NZO.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei797 – 8059DNFIPIEKY → GMCTVLFMD in isoform E. 1 PublicationVSP_001703
    Alternative sequencei806 – 1162357Missing in isoform E. 1 PublicationVSP_001704Add
    BLAST
    Alternative sequencei890 – 90011PETFEHLFTKH → DISFHEVFIFR in isoform D. 1 PublicationVSP_001701Add
    BLAST
    Alternative sequencei890 – 8945PETFE → RTDTL in isoform A. 3 PublicationsVSP_001697
    Alternative sequencei890 – 8923PET → VTV in isoform C. 2 PublicationsVSP_001699
    Alternative sequencei893 – 1162270Missing in isoform C. 2 PublicationsVSP_001700Add
    BLAST
    Alternative sequencei895 – 1162268Missing in isoform A. 3 PublicationsVSP_001698Add
    BLAST
    Alternative sequencei901 – 1162262Missing in isoform D. 1 PublicationVSP_001702Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42467 mRNA. Translation: AAA93014.1.
    U46135 mRNA. Translation: AAC52408.1.
    U49106 mRNA. Translation: AAC52420.1.
    U49107 mRNA. Translation: AAC52421.1.
    U49108 mRNA. Translation: AAC52422.1.
    U49109 mRNA. Translation: AAC52423.1.
    U49110 mRNA. Translation: AAC52424.1.
    U52915 mRNA. Translation: AAC52599.1.
    U58861 mRNA. Translation: AAC52705.1.
    U58862 mRNA. Translation: AAC52706.1.
    U58863 mRNA. Translation: AAC52707.1.
    Y10298 mRNA. Translation: CAA71343.1.
    AF039456
    , AF039443, AF039444, AF039445, AF039446, AF039447, AF039448, AF039449, AF039450, AF039451, AF039452, AF039453, AF039454, AF039455 Genomic DNA. Translation: AAB95334.1.
    AF039461
    , AF039443, AF039444, AF039445, AF039446, AF039447, AF039448, AF039449, AF039450, AF039451, AF039452, AF039453, AF039454, AF039455, AF039456, AF039457, AF039458, AF039459 Genomic DNA. Translation: AAB95333.1. Different termination.
    AF039459
    , AF039443, AF039444, AF039445, AF039446, AF039447, AF039448, AF039449, AF039450, AF039451, AF039452, AF039453, AF039454, AF039455, AF039456, AF039457, AF039458 Genomic DNA. Translation: AAB95335.1.
    AF039460
    , AF039443, AF039444, AF039445, AF039446, AF039447, AF039448, AF039449, AF039450, AF039451, AF039452, AF039453, AF039454, AF039455, AF039456, AF039457, AF039458, AF039459 Genomic DNA. Translation: AAB95332.1.
    Y10296 mRNA. Translation: CAA71342.1.
    AF098792 Genomic DNA. Translation: AAD13218.1.
    CCDSiCCDS18397.1. [P48356-3]
    CCDS51239.1. [P48356-2]
    CCDS51240.1. [P48356-1]
    PIRiS68437.
    S68438.
    S68439.
    S68440.
    S68441.
    RefSeqiNP_001116371.1. NM_001122899.1. [P48356-2]
    NP_034834.1. NM_010704.2. [P48356-3]
    NP_666258.2. NM_146146.2. [P48356-1]
    UniGeneiMm.259282.

    Genome annotation databases

    EnsembliENSMUST00000037552; ENSMUSP00000037385; ENSMUSG00000057722. [P48356-1]
    ENSMUST00000102777; ENSMUSP00000099838; ENSMUSG00000057722. [P48356-3]
    ENSMUST00000106921; ENSMUSP00000102534; ENSMUSG00000057722. [P48356-2]
    GeneIDi16847.
    KEGGimmu:16847.
    UCSCiuc008tvx.2. mouse. [P48356-1]
    uc008twa.1. mouse. [P48356-5]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42467 mRNA. Translation: AAA93014.1 .
    U46135 mRNA. Translation: AAC52408.1 .
    U49106 mRNA. Translation: AAC52420.1 .
    U49107 mRNA. Translation: AAC52421.1 .
    U49108 mRNA. Translation: AAC52422.1 .
    U49109 mRNA. Translation: AAC52423.1 .
    U49110 mRNA. Translation: AAC52424.1 .
    U52915 mRNA. Translation: AAC52599.1 .
    U58861 mRNA. Translation: AAC52705.1 .
    U58862 mRNA. Translation: AAC52706.1 .
    U58863 mRNA. Translation: AAC52707.1 .
    Y10298 mRNA. Translation: CAA71343.1 .
    AF039456
    , AF039443 , AF039444 , AF039445 , AF039446 , AF039447 , AF039448 , AF039449 , AF039450 , AF039451 , AF039452 , AF039453 , AF039454 , AF039455 Genomic DNA. Translation: AAB95334.1 .
    AF039461
    , AF039443 , AF039444 , AF039445 , AF039446 , AF039447 , AF039448 , AF039449 , AF039450 , AF039451 , AF039452 , AF039453 , AF039454 , AF039455 , AF039456 , AF039457 , AF039458 , AF039459 Genomic DNA. Translation: AAB95333.1 . Different termination.
    AF039459
    , AF039443 , AF039444 , AF039445 , AF039446 , AF039447 , AF039448 , AF039449 , AF039450 , AF039451 , AF039452 , AF039453 , AF039454 , AF039455 , AF039456 , AF039457 , AF039458 Genomic DNA. Translation: AAB95335.1 .
    AF039460
    , AF039443 , AF039444 , AF039445 , AF039446 , AF039447 , AF039448 , AF039449 , AF039450 , AF039451 , AF039452 , AF039453 , AF039454 , AF039455 , AF039456 , AF039457 , AF039458 , AF039459 Genomic DNA. Translation: AAB95332.1 .
    Y10296 mRNA. Translation: CAA71342.1 .
    AF098792 Genomic DNA. Translation: AAD13218.1 .
    CCDSi CCDS18397.1. [P48356-3 ]
    CCDS51239.1. [P48356-2 ]
    CCDS51240.1. [P48356-1 ]
    PIRi S68437.
    S68438.
    S68439.
    S68440.
    S68441.
    RefSeqi NP_001116371.1. NM_001122899.1. [P48356-2 ]
    NP_034834.1. NM_010704.2. [P48356-3 ]
    NP_666258.2. NM_146146.2. [P48356-1 ]
    UniGenei Mm.259282.

    3D structure databases

    ProteinModelPortali P48356.
    SMRi P48356. Positions 220-323, 359-830.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201139. 3 interactions.
    DIPi DIP-42763N.
    IntActi P48356. 10 interactions.
    MINTi MINT-2569396.

    PTM databases

    PhosphoSitei P48356.

    Proteomic databases

    PaxDbi P48356.
    PRIDEi P48356.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000037552 ; ENSMUSP00000037385 ; ENSMUSG00000057722 . [P48356-1 ]
    ENSMUST00000102777 ; ENSMUSP00000099838 ; ENSMUSG00000057722 . [P48356-3 ]
    ENSMUST00000106921 ; ENSMUSP00000102534 ; ENSMUSG00000057722 . [P48356-2 ]
    GeneIDi 16847.
    KEGGi mmu:16847.
    UCSCi uc008tvx.2. mouse. [P48356-1 ]
    uc008twa.1. mouse. [P48356-5 ]

    Organism-specific databases

    CTDi 3953.
    MGIi MGI:104993. Lepr.

    Phylogenomic databases

    eggNOGi NOG29456.
    GeneTreei ENSGT00730000111209.
    HOVERGENi HBG000140.
    InParanoidi P48356.
    KOi K05062.
    OMAi SWAQGLN.
    OrthoDBi EOG7034GB.
    PhylomeDBi P48356.
    TreeFami TF106501.

    Enzyme and pathway databases

    Reactomei REACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.

    Miscellaneous databases

    NextBioi 290776.
    PROi P48356.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48356.
    Bgeei P48356.
    CleanExi MM_LEPR.
    Genevestigatori P48356.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR003529. Hematopoietin_rcpt_Gp130_CS.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR010457. IgC2-like_lig-bd.
    IPR015752. Lep_receptor.
    [Graphical view ]
    PANTHERi PTHR23036:SF11. PTHR23036:SF11. 1 hit.
    Pfami PF06328. Lep_receptor_Ig. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 4 hits.
    PROSITEi PS50853. FN3. 3 hits.
    PS01353. HEMATOPO_REC_L_F2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
      Tissue: Choroid plexus.
    2. "Evidence that the diabetes gene encodes the leptin receptor: identification of a mutation in the leptin receptor gene in db/db mice."
      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.
      Cell 84:491-495(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
      Strain: C57BL/KsJ.
      Tissue: Hypothalamus.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).
      Strain: C57BL/Ks.
      Tissue: Hypothalamus.
    4. "Novel B219/OB receptor isoforms: possible role of leptin in hematopoiesis and reproduction."
      Cioffi J.A., Shafer A.W., Zupancic T.J., Smith-Gbur J., Mikhail A., Platika D., Snodgrass H.R.
      Nat. Med. 2:585-589(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
      Strain: BALB/c.
      Tissue: Liver.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
      Strain: FVB/N.
      Tissue: Spleen.
    6. "Hyperleptinemia, leptin resistance, and polymorphic leptin receptor in the New Zealand obese mouse."
      Igel M., Becker W., Herberg L., Joost H.G.
      Endocrinology 138:4234-4239(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
      Strain: NZO.
      Tissue: Hypothalamus.
    7. "Fine structure of the murine leptin receptor gene: splice site suppression is required to form two alternatively spliced transcripts."
      Chua S.C., Koutras I.K., Han L., Liu S.M., Kay J., Young S.J., Chung W.K., Leibel R.L.
      Genomics 45:264-270(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; B; C AND E).
      Strain: 129/J.
    8. "Hyperleptinemia and leptin receptor variant Asp600Asn in the obese, hyperinsulinemic KK mouse strain."
      Igel M., Taylor B.A., Phillips S.J., Becker W., Herberg L., Joost H.G.
      J. Endocrinol. 21:337-345(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT ASN-600.
      Strain: KK Obese.
      Tissue: Hypothalamus.
    9. "Murine leptin receptor genomic exon 18b and surrounding sequence."
      Banks A.S., Myers M.G. Jr.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 890-1162 (ISOFORM B).
      Strain: 129.
    10. "Identification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor."
      Eyckerman S., Broekaert D., Verhee A., Vandekerckhove J., Tavernier J.
      FEBS Lett. 486:33-37(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-985 AND TYR-1077.
    11. "Activation of downstream signals by the long form of the leptin receptor."
      Banks A.S., Davis S.M., Bates S.H., Myers M.G. Jr.
      J. Biol. Chem. 275:14563-14572(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-985 AND TYR-1138, STAT3 ACTIVATION, ERK/FOS ACTIVATION, MUTAGENESIS OF TYR-985; TYR-1077 AND TYR-1138.
    12. "SOCS3 mediates feedback inhibition of the leptin receptor via Tyr985."
      Bjorbaek C., Lavery H.J., Bates S.H., Olson R.K., Davis S.M., Flier J.S., Myers M.G. Jr.
      J. Biol. Chem. 275:40649-40657(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SOCS3, MUTAGENESIS OF TYR-985 AND TYR-1138.
    13. "Regulation of Jak kinases by intracellular leptin receptor sequences."
      Kloek C., Haq A.K., Dunn S.L., Lavery H.J., Banks A.S., Myers M.G. Jr.
      J. Biol. Chem. 277:41547-41555(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN JAK2 ACTIVATION.

    Entry informationi

    Entry nameiLEPR_MOUSE
    AccessioniPrimary (citable) accession number: P48356
    Secondary accession number(s): O35686
    , O54986, Q61215, Q64309, Q9QWG3, Q9QWV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 147 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3