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Leptin receptor (LEP-R) (OB receptor) (OB-R) (CD antigen CD295)

 LEPR_MACMU              Reviewed;        1163 AA.
Q9MYL0; Q9MYK9; Q9MYL1; Q9MYL2;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
19-OCT-2002, sequence version 2.
23-MAY-2018, entry version 115.
RecName: Full=Leptin receptor;
Short=LEP-R;
AltName: Full=OB receptor;
Short=OB-R;
AltName: CD_antigen=CD295;
Flags: Precursor;
Name=LEPR; Synonyms=OBR;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Adipose tissue;
PubMed=9738551; DOI=10.1002/j.1550-8528.1998.tb00363.x;
Hotta K., Gustafson T.A., Ortmeyer H.K., Bodkin N.L., Hansen B.C.;
"Monkey leptin receptor mRNA: sequence, tissue distribution, and mRNA
expression in the adipose tissue of normal, hyperinsulinemic, and type
2 diabetic rhesus monkeys.";
Obes. Res. 6:353-360(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Adipose tissue;
Hotta K., Gustafson T.A., Ortmeyer H.K., Bodkin N.L., Hansen B.C.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Gustafson T.A., Ortmeyer H.K., Bodkin N.L., Hansen B.C.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Receptor for hormone LEP/leptin (By similarity). 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. 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).
{ECO:0000250|UniProtKB:P48356, ECO:0000250|UniProtKB:P48357}.
-!- FUNCTION: Isoform A: May transport LEP across the blood-brain
barrier. Binds LEP and mediates LEP endocytosis. Does not induce
phosphorylation of and activate STAT3.
{ECO:0000250|UniProtKB:P48356}.
-!- SUBUNIT: Present as a mixture of monomers and dimers. 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). {ECO:0000250|UniProtKB:P48356,
ECO:0000250|UniProtKB:P48357}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P48357}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P48357}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P48357}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B;
IsoId=Q9MYL0-1; Sequence=Displayed;
Name=A;
IsoId=Q9MYL0-2; Sequence=VSP_001695, VSP_001696;
-!- TISSUE SPECIFICITY: Widely expressed. High expression of isoform B
in liver, adipose tissue, hypothalamus and choroid plexus.
-!- DOMAIN: The cytoplasmic domain may be essential for intracellular
signal transduction by activation of JAK tyrosine kinase and
STATs.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
tyrosine residues (isoform B only) by JAK2. Tyr-984 is required
for complete binding and activation of PTPN11, ERK/FOS activation
and, for interaction with SOCS3. Phosphorylation on Tyr-1139 is
required for STAT3 binding/activation (By similarity).
{ECO:0000250}.
-!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
tyrosine residues (isoform B only) by JAK2. Tyr-984 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-1139 is
required for STAT3 binding/activation. Phosphorylation of Tyr-1077
has a more accessory role. {ECO:0000250|UniProtKB:P48356}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF225874; AAF35388.1; -; mRNA.
EMBL; AF225875; AAF35389.1; -; mRNA.
EMBL; AF225873; AAF35387.1; -; mRNA.
EMBL; AF222960; AAF34683.1; -; mRNA.
RefSeq; NP_001027991.1; NM_001032819.1.
UniGene; Mmu.1248; -.
ProteinModelPortal; Q9MYL0; -.
PRIDE; Q9MYL0; -.
GeneID; 574126; -.
KEGG; mcc:574126; -.
CTD; 3953; -.
HOGENOM; HOG000231995; -.
HOVERGEN; HBG000140; -.
InParanoid; Q9MYL0; -.
KO; K05062; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0038021; F:leptin receptor activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0098868; P:bone growth; ISS:UniProtKB.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
GO; GO:0044321; P:response to leptin; ISS:UniProtKB.
GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
InterPro; IPR015752; Lep_receptor.
PANTHER; PTHR23036:SF109; PTHR23036:SF109; 3.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 3.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Membrane; Obesity; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1163 Leptin receptor.
/FTId=PRO_0000010905.
TOPO_DOM 22 837 Extracellular. {ECO:0000255}.
TRANSMEM 838 860 Helical. {ECO:0000255}.
TOPO_DOM 861 1163 Cytoplasmic. {ECO:0000255}.
DOMAIN 237 331 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 537 632 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 637 730 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 738 831 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 465 482 Leptin-binding.
{ECO:0000250|UniProtKB:P48357}.
REGION 891 896 Required for JAK2 activation.
{ECO:0000250|UniProtKB:P48356}.
REGION 896 904 Required for STAT3 phosphorylation.
{ECO:0000250|UniProtKB:P48356}.
MOTIF 620 624 WSXWS motif.
MOTIF 869 877 Box 1 motif.
MOD_RES 880 880 Phosphoserine.
{ECO:0000250|UniProtKB:P48357}.
MOD_RES 984 984 Phosphotyrosine; by JAK2.
{ECO:0000250|UniProtKB:P48356}.
MOD_RES 1077 1077 Phosphotyrosine.
{ECO:0000250|UniProtKB:P48356}.
MOD_RES 1139 1139 Phosphotyrosine; by JAK2.
{ECO:0000250|UniProtKB:P48356}.
CARBOHYD 23 23 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 726 726 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 748 748 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 88 {ECO:0000250|UniProtKB:P48357}.
DISULFID 87 97 {ECO:0000250|UniProtKB:P48357}.
DISULFID 129 140 {ECO:0000250|UniProtKB:P48357}.
DISULFID 184 194 {ECO:0000250|UniProtKB:P48357}.
DISULFID 350 410 {ECO:0000250|UniProtKB:P48357}.
DISULFID 411 416 {ECO:0000250|UniProtKB:P48357}.
DISULFID 434 445 {ECO:0000250|UniProtKB:P48357}.
DISULFID 471 526 {ECO:0000250|UniProtKB:P48357}.
DISULFID 486 496 {ECO:0000250|UniProtKB:P48357}.
VAR_SEQ 890 894 PETFE -> RTDIL (in isoform A).
{ECO:0000303|PubMed:9738551,
ECO:0000303|Ref.2}.
/FTId=VSP_001695.
VAR_SEQ 895 1163 Missing (in isoform A).
{ECO:0000303|PubMed:9738551,
ECO:0000303|Ref.2}.
/FTId=VSP_001696.
CONFLICT 889 889 K -> KIRGFVMLPRLVLNSQAQVIHPPRPPKVLELQ (in
Ref. 2; AAF35387/AAF34683).
{ECO:0000305}.
SEQUENCE 1163 AA; 132296 MW; 6B7B89108F851895 CRC64;
MICQKFCVVL LHWEFICVIT AFNLSYPITP WRFKLSCMPP NSTYDYFLLP AGLSKNTSNL
NGHYETAVEF NSSDTHFSNL SKTTFHCCFR SEQDRNCSLC ADNIEGKTFV STVNSSVFQQ
MGANWNIQCW LKGDLKLFIC YVESLFKNPF KNYKHKVHLL YVLPEVLEDS PLVPQKGSFQ
MVHCNCSVHE RCECLVPVPT AKLNDTLLMC LKITSGGVIF QSPLMSVQPI NMVKPDPPLG
LRMEITDDGN LKISWSSPPL VPFPLQYEVK YSENSTTVIR EADKIVSATS LLVDGILPGS
SYEVQVRGKR LDGPGIWSDW STPHVFTTQD VIYFPPKILT SVGSNVSFHC IYKNENKIVS
SKKIVWWMNL AEKIPQSQYD VVSDHVSKVT FFNLNETKPR GKFTYDAVYC CNEHECHHRY
AELYVIDVNI NISCETDGHL TKMTCRWSTN TIQSLAGSTL QLRYRRSSLY CFDIPSIHPI
SKPKDCYLQS DGFYECVFQP IFLLSGYTMW IRINHPLGSL DSPPTCVLPD SVVKPLPPSS
VKAEIIKNIG LLKISWEKPV FPENNLQFQI RYGLSGKEIQ WKMYDVYDAK SKSVSLPVPD
FCAVYAVQVR CKRSDGLGLW SNWSNPAYTV VMDIKVPMRG PEFWRIINGD TMKKEKNVTL
LWKPLMKNES LCSVQRYVIN HHTSCNGTWS EDVGNHTKFT FLWTEQAHTV TVLAINSIGA
SVANFNLTFS WPMSKVNIVQ SLSAYPLNSS CVILSWILSP SDYKLMYFII EWKNLNEDGE
IKWLRISSSV KKYYIHDHFI PIEKYQFSLY PIFMEGVGKP KIINSFAQDN TEKHQNDAGL
YVIVPVIISS SILLLGTLLI LHQRMKKLFW EDVPNPKNCS WAQGLNFQKP ETFEHLFIKH
TASVTCGPLL LEPETISEDI SVDTSWKNKD EMVPTTVVSL LSTTDLEKGS VCISDQFNSV
NFSEAEGTEV TCEDESQRQP FVKYATLISN SKPSETDEEQ GLINSSVTKC FSSKNSPLKD
SFSNSSWEIE AQAFFILSDQ RPNIILPHLT FSEGLDELLR LEGNFPEENN DEKSIYYLGV
TSIKKRESGV LLTDKSRVLC PFPAPCLFTD IRVLQDSCSH FVENNFNLGT SSKKTFASYM
PQFQTCSTQT HKIMENKMCD LTV


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