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Database: UniProt
Entry: O02671
LinkDB: O02671
Original site: O02671 
ID   LEPR_PIG                Reviewed;        1165 AA.
AC   O02671; Q95257; Q9MZS2; Q9N1F9; Q9XSN9;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 3.
DT   11-MAY-2016, entry version 110.
DE   RecName: Full=Leptin receptor;
DE            Short=LEP-R;
DE   AltName: Full=OB receptor;
DE            Short=OB-R;
DE   AltName: CD_antigen=CD295;
DE   Flags: Precursor;
GN   Name=LEPR; Synonyms=OBR;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=10911396;
RX   DOI=10.1002/1098-2795(200008)56:4<465::AID-MRD4>3.0.CO;2-Q;
RA   Ruiz-Cortes Z.T., Men T., Palin M.-F., Downey B.R., Lacroix D.A.,
RA   Murphy B.D.;
RT   "Porcine leptin receptor: molecular structure and expression in the
RT   ovary.";
RL   Mol. Reprod. Dev. 56:465-474(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
RC   STRAIN=Yorkshire X Meishan;
RA   Lacroix D.A., Gevry N.Y., Ruiz-Cortes Z.T., Murphy B.D.;
RT   "Porcine leptin receptor intron 3, partial.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-854.
RC   TISSUE=Liver;
RA   Hu X., Dai R., Li N., Wu C.;
RT   "Expression, detection, and partial cloning of porcine leptin receptor
RT   (OBR) gene.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-159 AND 916-1088.
RC   TISSUE=Hypothalamus;
RA   Matteri R.L., Carroll J.A.;
RT   "Partial cDNA sequence of the porcine leptin receptor.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-123.
RX   PubMed=9800339;
RA   Stratil A., Kopecny M., Moser G., Schroffel J. Jr., Cepica S.;
RT   "HpaII and RsaI PCR-RFLPs within an intron of the porcine leptin
RT   receptor gene (LEPR) and its linkage mapping.";
RL   Anim. Genet. 29:405-406(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 408-470.
RX   PubMed=9069130; DOI=10.1007/s003359900397;
RA   Ernst C.W., Kapke P.A., Yerle M., Rothschild M.F.;
RT   "The leptin receptor gene (LEPR) maps to porcine chromosome 6.";
RL   Mamm. Genome 8:226-226(1997).
CC   -!- FUNCTION: Receptor for hormone LEP/leptin (By similarity). On
CC       ligand binding, mediates LEP central and peripheral effects
CC       through the activation of different signaling pathways such as
CC       JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as
CC       an appetite-regulating factor that induces a decrease in food
CC       intake and an increase in energy consumption by inducing
CC       anorexinogenic factors and suppressing orexigenic neuropeptides,
CC       also regulates bone mass and secretion of hypothalamo-pituitary-
CC       adrenal hormones. In the periphery, increases basal metabolism,
CC       influences reproductive function, regulates pancreatic beta-cell
CC       function and insulin secretion, is pro-angiogenic and affects
CC       innate and adaptive immunity (By similarity). Control of energy
CC       homeostasis and melanocortin production (stimulation of POMC and
CC       full repression of AgRP transcription) is mediated by STAT3
CC       signaling, whereas distinct signals regulate NPY and the control
CC       of fertility, growth and glucose homeostasis. Involved in the
CC       regulation of counter-regulatory response to hypoglycemia by
CC       inhibiting neurons of the parabrachial nucleus. Has a specific
CC       effect on T lymphocyte responses, differentially regulating the
CC       proliferation of naive and memory T-cells. Leptin increases Th1
CC       and suppresses Th2 cytokine production (By similarity).
CC       {ECO:0000250|UniProtKB:P48356, ECO:0000250|UniProtKB:P48357}.
CC   -!- SUBUNIT: Present as a mixture of monomers and dimers. The
CC       phosphorylated receptor binds a number of SH2 domain-containing
CC       proteins such as JAK2, STAT3, PTPN11, and SOCS3 (By similarity).
CC       Interaction with SOCS3 inhibits JAK/STAT signaling and MAPK
CC       cascade (By similarity). {ECO:0000250|UniProtKB:P48356,
CC       ECO:0000250|UniProtKB:P48357}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P48357}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P48357}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P48357}.
CC   -!- TISSUE SPECIFICITY: Kidney, liver, spleen, lung, brain, testis,
CC       uterus, ovary, corpus luteum, theca and granulosa cells.
CC   -!- DOMAIN: The cytoplasmic domain may be essential for intracellular
CC       signal transduction by activation of JAK tyrosine kinase and
CC       STATs.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-
CC       surface receptor binding.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
CC       tyrosine residues by JAK2. Tyr-986 is required for complete
CC       binding and activation of PTPN11, ERK/FOS activation,for
CC       interaction with SOCS3 and SOCS3 mediated inhibition of leptin
CC       signaling. Phosphorylation on Tyr-1141 is required for STAT3
CC       binding/activation. Phosphorylation of Tyr-1079 has a more
CC       accessory role. {ECO:0000250|UniProtKB:P48356}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
DR   EMBL; AF092422; AAC61766.1; -; mRNA.
DR   EMBL; AH009271; AAF66822.1; -; Genomic_DNA.
DR   EMBL; AF167719; AAF89633.1; -; mRNA.
DR   EMBL; AF036908; AAB88825.1; -; mRNA.
DR   EMBL; U67739; AAB07892.1; -; mRNA.
DR   EMBL; AJ223162; CAA11142.1; -; Genomic_DNA.
DR   EMBL; AJ223163; CAA11143.1; -; Genomic_DNA.
DR   EMBL; U72070; AAC48707.1; -; Genomic_DNA.
DR   RefSeq; NP_001019758.1; NM_001024587.1.
DR   UniGene; Ssc.263; -.
DR   ProteinModelPortal; O02671; -.
DR   STRING; 9823.ENSSSCP00000022838; -.
DR   PaxDb; O02671; -.
DR   GeneID; 396836; -.
DR   KEGG; ssc:396836; -.
DR   CTD; 3953; -.
DR   eggNOG; ENOG410IKH4; Eukaryota.
DR   eggNOG; ENOG4110JZP; LUCA.
DR   HOVERGEN; HBG000140; -.
DR   InParanoid; O02671; -.
DR   KO; K05062; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0038021; F:leptin receptor activity; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0098868; P:bone growth; ISS:UniProtKB.
DR   GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR   GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
DR   GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
DR   GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
DR   GO; GO:0044321; P:response to leptin; ISS:UniProtKB.
DR   GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
DR   GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR   InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR010457; IgC2-like_lig-bd.
DR   InterPro; IPR015752; Lep_receptor.
DR   PANTHER; PTHR23036:SF109; PTHR23036:SF109; 3.
DR   Pfam; PF06328; Lep_receptor_Ig; 1.
DR   SMART; SM00060; FN3; 4.
DR   SUPFAM; SSF49265; SSF49265; 4.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Membrane; Obesity; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   1165       Leptin receptor.
FT                                /FTId=PRO_0000010907.
FT   TOPO_DOM     22    838       Extracellular. {ECO:0000255}.
FT   TRANSMEM    839    861       Helical. {ECO:0000255}.
FT   TOPO_DOM    862   1165       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      239    332       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      539    634       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      642    736       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      740    834       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   REGION      467    484       Leptin-binding.
FT                                {ECO:0000250|UniProtKB:P48357}.
FT   REGION      892    897       Required for JAK2 activation.
FT                                {ECO:0000250|UniProtKB:P48356}.
FT   REGION      897    905       Required for STAT3 phosphorylation.
FT                                {ECO:0000250|UniProtKB:P48356}.
FT   MOTIF       622    626       WSXWS motif.
FT   MOTIF       870    878       Box 1 motif.
FT   MOD_RES     881    881       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48357}.
FT   MOD_RES     986    986       Phosphotyrosine; by JAK2.
FT                                {ECO:0000250|UniProtKB:P48356}.
FT   MOD_RES    1079   1079       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P48356}.
FT   MOD_RES    1141   1141       Phosphotyrosine; by JAK2.
FT                                {ECO:0000250|UniProtKB:P48356}.
FT   CARBOHYD     41     41       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     55     55       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     72     72       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     80     80       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    187    187       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    206    206       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    276    276       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    347    347       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    624    624       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    659    659       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    670    670       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    697    697       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    728    728       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    750    750       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     37     90       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID     89     99       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    131    142       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    186    196       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    188    193       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    352    412       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    413    418       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    436    447       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    473    528       {ECO:0000250|UniProtKB:P48357}.
FT   DISULFID    488    498       {ECO:0000250|UniProtKB:P48357}.
FT   CONFLICT      7      9       SVA -> CVV (in Ref. 3; AAF89633).
FT                                {ECO:0000305}.
FT   CONFLICT     69     69       T -> M (in Ref. 3; AAF89633 and 4;
FT                                AAB07892). {ECO:0000305}.
FT   CONFLICT     73     73       S -> I (in Ref. 1; AAC61766).
FT                                {ECO:0000305}.
FT   CONFLICT    283    283       E -> K (in Ref. 3; AAF89633).
FT                                {ECO:0000305}.
FT   CONFLICT    350    350       F -> L (in Ref. 3; AAF89633).
FT                                {ECO:0000305}.
FT   CONFLICT    362    362       S -> P (in Ref. 3; AAF89633).
FT                                {ECO:0000305}.
FT   CONFLICT    365    365       K -> E (in Ref. 3; AAF89633).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       G -> S (in Ref. 3; AAF89633).
FT                                {ECO:0000305}.
FT   CONFLICT    974    974       R -> C (in Ref. 4; AAB88825).
FT                                {ECO:0000305}.
FT   CONFLICT   1047   1047       T -> I (in Ref. 4; AAB88825).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1165 AA;  132523 MW;  9F02EADDEDC26D21 CRC64;
     MTCPKFSVAL LHWEFIYVIT AFDLAYPITP WKFKLSCMPP NTTYDFLLPA GISKNTSTLN
     GHDEAVVETE LNSSGTYLSN LSSKTTFHCC FWSEEDKNCS VHADNIAGKA FVSAVNSLVF
     QQTGANWNIQ CWMKEDLKLF ICYMESLFKN PFKNYDLKVH LLYVLLEVLE GSPLLPQKGS
     FQSVQCNCSA RECCECHVPV SAAKLNYTLL MYLKITSGGA VFHSPLMSVQ PINVVKPDPP
     LGLHMEITDT GNLKISWSSP TLVPFQLQYQ VKYSENSTTN MREADEIVSD TSLLVDSVLP
     GSSYEVQVRG KRLDGPGIWS DWSTPFTFTT QDVIYFPPKI LTSVGSNISF HCIYKNENKI
     VSSKKIVWWM NLAEKIPQSQ YDVVGDHVSK VTFPNMNATK PRGKFTYDAV YCCNEHECHH
     RYAELYVIDV NINISCETDG YLTKMTCRWS TNAIQSLVGS TLQLRYHRSS LYCSDVPSVH
     PISEPKDCQL QRDGFYECIF QPIFLLSGYT MWIRINHPLG SLDSPPTCVI PDSVVKPLPP
     SSVKAEITAK IGLLKISWEK PVFPENNLQF QIRYGLSGKE VQWKIYEVYD TKLKSTSLPV
     PDLCAVYAVQ VRCKRLDGLG YWSNWSTPAY TVVTDVKVPI RGPEFWRIIN EDATKKERNI
     TLLWKPLMKN DSLCSVRSYV VKHHTSRHGT WSEDVGNHTK LTFLWTEQAH SVTVLAVNSI
     GASSANFNLT FSWPMSKVNI VQSLSAYPLN SSCVGLSWLL SPSDYNLMYF ILEWKILNED
     HEIKWLRIPS SVKKYYIHDH FIPIEKYQFS LYPIFMEGVG KPKIINSFTQ DGEKHRNDAG
     LYVIVPIIIS SSILLLGTLL MSHQRMKKLF WEDVPNPKNC SWAQGLNFQK PETFEHLFIK
     HTESVTFGPL LLEPETISED ISVDTSWKNK DEMVPPTTVS LLLTTPDLEK SSICISDQRS
     SAHFSEAESM EITREDENRR QPSIKYATLL SSPKSGETEQ EQELVSSLVS RCFSSSNSLP
     KESFSNSSWE IETQAFFILS DQHPNMTSPH LSFSEGLDEL MKFEGNFPKE HNDERSVYYL
     GVTSIKKRES DVFLTDESRV RCPFPAHCLF ADIKILQESC SHLVENNFNL GTSGQKTFVS
     YMPQFQTCST QTQKIMENKM YDLTV
//
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