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Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)]

 GHR_RAT                 Reviewed;         638 AA.
P16310; Q64236; Q80XW9;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
12-SEP-2018, entry version 163.
RecName: Full=Growth hormone receptor;
Short=GH receptor;
AltName: Full=Somatotropin receptor;
Contains:
RecName: Full=Growth hormone-binding protein;
Short=GH-binding protein;
Short=GHBP;
AltName: Full=Serum-binding protein;
Flags: Precursor;
Name=Ghr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2722883;
Mathews L.S., Enberg B., Norstedt G.;
"Regulation of rat growth hormone receptor gene expression.";
J. Biol. Chem. 264:9905-9910(1989).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
PubMed=2792761; DOI=10.1101/gad.3.8.1199;
Baumbach W.R., Horner D.L., Logan J.S.;
"The growth hormone-binding protein in rat serum is an alternatively
spliced form of the rat growth hormone receptor.";
Genes Dev. 3:1199-1205(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Adipose tissue;
PubMed=1446642; DOI=10.1210/endo.131.6.1446642;
Frick G.P., Goodman H.M.;
"Characterization of the short isoform of the growth hormone receptor
synthesized by rat adipocytes.";
Endocrinology 131:3083-3090(1992).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=8921876; DOI=10.1016/0378-1119(96)00277-6;
Zhou Y., He L., Kopchick J.J.;
"Structural comparison of a portion of the rat and mouse growth
hormone receptor/binding protein genes.";
Gene 177:257-259(1996).
[5]
DOMAIN JAK2 BINDING.
PubMed=8063815;
VanderKuur J.A., Wang X., Zhang L., Campbell G.S., Allevato G.,
Billestrup N., Norstedt G., Carter-Su C.;
"Domains of the growth hormone receptor required for association and
activation of JAK2 tyrosine kinase.";
J. Biol. Chem. 269:21709-21717(1994).
[6]
ENDOCYTOSIS SIGNAL, AND MUTAGENESIS OF PHE-346.
PubMed=7615519; DOI=10.1074/jbc.270.29.17210;
Allevato G., Billestrup N., Goujon L., Galsgaard E.D., Norstedt G.,
Postel-Vinay M.-C., Kelly P.A., Nielsen J.H.;
"Identification of phenylalanine 346 in the rat growth hormone
receptor as being critical for ligand-mediated internalization and
down-regulation.";
J. Biol. Chem. 270:17210-17214(1995).
[7]
INTERACTION WITH SOCS FAMILY PROTEINS.
PubMed=10585430; DOI=10.1074/jbc.274.50.35553;
Ram P.A., Waxman D.J.;
"SOCS/CIS protein inhibition of growth hormone-stimulated STAT5
signaling by multiple mechanisms.";
J. Biol. Chem. 274:35553-35561(1999).
[8]
PHOSPHORYLATION BY JAK2.
PubMed=7545168; DOI=10.1074/jbc.270.37.21738;
VanderKuur J.A., Wang X., Zhang L., Allevato G., Billestrup N.,
Carter-Su C.;
"Growth hormone-dependent phosphorylation of tyrosine 333 and/or 338
of the growth hormone receptor.";
J. Biol. Chem. 270:21738-21744(1995).
[9]
PHOSPHORYLATION, AND STAT5 ACTIVATION.
PubMed=9231797; DOI=10.1210/endo.138.8.5332;
Smit L.S., Vanderkuur J.A., Stimage A., Han Y., Luo G., Yu-Lee L.-Y.,
Schwartz J., Carter-Su C.;
"Growth hormone-induced tyrosyl phosphorylation and deoxyribonucleic
acid binding activity of Stat5A and Stat5B.";
Endocrinology 138:3426-3434(1997).
-!- FUNCTION: Receptor for pituitary gland growth hormone involved in
regulating postnatal body growth. On ligand binding, couples to,
and activates the JAK2/STAT5 pathway.
-!- FUNCTION: The soluble form (GHBP) acts as a reservoir of growth
hormone in plasma and may be a modulator/inhibitor of GH
signaling.
-!- SUBUNIT: On growth hormone (GH) binding, forms homodimers and
binds JAK2 via a box 1-containing domain. Binding to SOCS3
inhibits JAK2 activation, binding to CIS and SOCS2 inhibits STAT5
activation.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=On growth hormone binding, GHR is ubiquitinated,
internalized, down-regulated and transported into a degradative or
non-degradative pathway.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted. Membrane. Note=Mainly
secreted. In adipose tissue, isoform 2 is mostly membrane
associated.
-!- SUBCELLULAR LOCATION: Growth hormone-binding protein: Secreted
{ECO:0000250}. Note=Complexed to a substantial fraction of
circulating GH. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P16310-1; Sequence=Displayed;
Name=2; Synonyms=Short from, GHBP;
IsoId=P16310-2; Sequence=VSP_010231, VSP_010232;
-!- TISSUE SPECIFICITY: Highest expression in liver. Also expressed in
heart, kidney and muscle.
-!- DEVELOPMENTAL STAGE: Expression is low at birth. Increases to
adult levels after 5 weeks.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding. {ECO:0000269|PubMed:8063815}.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation. {ECO:0000269|PubMed:8063815}.
-!- DOMAIN: The extracellular domain is the ligand-binding domain
representing the growth hormone-binding protein (GHBP).
{ECO:0000269|PubMed:8063815}.
-!- DOMAIN: The ubiquitination-dependent endocytosis motif (UbE) is
required for recruitment of the ubiquitin conjugation system on to
the receptor and for its internalization.
{ECO:0000269|PubMed:8063815}.
-!- PTM: On GH binding, phosphorylated on tyrosine residues in the
cytoplasmic domain by JAK2. Phosphorylation on either (or all of)
Tyr-534, Tyr-566 and/or Tyr-627 is required for STAT5 activation.
Phosphorylation on Tyr-333 would seem necessary for JAK2
activation. {ECO:0000269|PubMed:7545168,
ECO:0000269|PubMed:9231797}.
-!- PTM: On ligand binding, ubiquitinated on lysine residues in the
cytoplasmic domain. This ubiquitination is not sufficient for GHR
internalization (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04811; AAA41219.1; -; mRNA.
EMBL; S49003; AAP13886.1; -; mRNA.
EMBL; U44722; AAC52916.1; -; Genomic_DNA.
PIR; A32985; A33505.
PIR; B32985; B32985.
RefSeq; NP_058790.1; NM_017094.1. [P16310-1]
RefSeq; XP_008758976.1; XM_008760754.1. [P16310-1]
UniGene; Rn.2178; -.
ProteinModelPortal; P16310; -.
SMR; P16310; -.
BioGrid; 247275; 1.
DIP; DIP-63N; -.
IntAct; P16310; 3.
MINT; P16310; -.
STRING; 10116.ENSRNOP00000044119; -.
iPTMnet; P16310; -.
PhosphoSitePlus; P16310; -.
PaxDb; P16310; -.
PRIDE; P16310; -.
Ensembl; ENSRNOT00000046951; ENSRNOP00000044119; ENSRNOG00000015654. [P16310-1]
GeneID; 25235; -.
KEGG; rno:25235; -.
CTD; 2690; -.
RGD; 2687; Ghr.
eggNOG; ENOG410IFQI; Eukaryota.
eggNOG; ENOG410XTHJ; LUCA.
GeneTree; ENSGT00530000063112; -.
HOGENOM; HOG000015773; -.
HOVERGEN; HBG005836; -.
InParanoid; P16310; -.
KO; K05080; -.
OMA; IDFYAQV; -.
OrthoDB; EOG091G03CN; -.
PhylomeDB; P16310; -.
Reactome; R-RNO-1170546; Prolactin receptor signaling.
Reactome; R-RNO-982772; Growth hormone receptor signaling.
PRO; PR:P16310; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000015654; Expressed in 10 organ(s), highest expression level in liver.
ExpressionAtlas; P16310; baseline and differential.
Genevisible; P16310; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0004903; F:growth hormone receptor activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO; GO:0019903; F:protein phosphatase binding; IMP:RGD.
GO; GO:0042169; F:SH2 domain binding; IDA:RGD.
GO; GO:0042976; P:activation of Janus kinase activity; IDA:BHF-UCL.
GO; GO:0000187; P:activation of MAPK activity; IDA:BHF-UCL.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD.
GO; GO:0007259; P:JAK-STAT cascade; IDA:BHF-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:0045597; P:positive regulation of cell differentiation; IEP:RGD.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IDA:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0032094; P:response to food; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0060416; P:response to growth hormone; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
GO; GO:0043278; P:response to morphine; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR025871; GHBP.
InterPro; IPR015152; Growth/epo_recpt_lig-bind.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
Pfam; PF09067; EpoR_lig-bind; 1.
Pfam; PF12772; GHBP; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endocytosis; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 638 Growth hormone receptor.
/FTId=PRO_0000010969.
CHAIN 19 256 Growth hormone-binding protein.
{ECO:0000250}.
/FTId=PRO_0000010970.
TOPO_DOM 19 265 Extracellular. {ECO:0000255}.
TRANSMEM 266 289 Helical. {ECO:0000255}.
TOPO_DOM 290 638 Cytoplasmic. {ECO:0000255}.
DOMAIN 151 254 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 295 380 Required for JAK2 binding.
MOTIF 240 244 WSXWS motif.
MOTIF 298 306 Box 1 motif.
MOTIF 341 350 UbE motif.
SITE 346 346 Required for endocytosis and down-
regulation.
MOD_RES 342 342 Phosphoserine.
{ECO:0000250|UniProtKB:P10912}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 66 {ECO:0000250}.
DISULFID 101 112 {ECO:0000250}.
DISULFID 126 140 {ECO:0000250}.
VAR_SEQ 263 279 DFRFPWFLIIIFGIFGV -> GPKFNSQHPHQEIDNHL
(in isoform 2).
{ECO:0000303|PubMed:1446642}.
/FTId=VSP_010231.
VAR_SEQ 280 638 Missing (in isoform 2).
{ECO:0000303|PubMed:1446642}.
/FTId=VSP_010232.
MUTAGEN 346 346 F->A: No internalization nor down-
regulation. No effect on transcriptional
signaling. {ECO:0000269|PubMed:7615519}.
SEQUENCE 638 AA; 71237 MW; 0D8E9AF759A21A3B CRC64;
MDLWRVFLTL ALAVSSDMFP GSGATPATLG KASPVLQRIN PSLRESSSGK PRFTKCRSPE
LETFSCYWTE GDDHNLKVPG SIQLYYARRI AHEWTPEWKE CPDYVSAGAN SCYFNSSYTS
IWIPYCIKLT TNGDLLDEKC FTVDEIVQPD PPIGLNWTLL NISLPGIRGD IQVSWQPPPS
ADVLKGWIIL EYEIQYKEVN ETKWKTMSPI WSTSVPLYSL RLDKEHEVRV RSRQRSFEKY
SEFSEVLRVT FPQMDTLAAC EEDFRFPWFL IIIFGIFGVA VMLFVVIFSK QQRIKMLILP
PVPVPKIKGI DPDLLKEGKL EEVNTILGIH DNYKPDFYND DSWVEFIELD IDDADEKTEE
SDTDRLLSDD QEKSAGILGA KDDDSGRTSC YDPDILDTDF HTSDMCDGTS EFAQPQKLKA
EADLLCLDQK NLKNSPYDAS LGSLHPSITL TMEDKPQPLL GSETESTHQL PSTPMSSPVS
LANIDFYAQV SDITPAGGVV LSPGQKIKAG LAQGNTQLEV AAPCQENYSM NSAYFCESDA
KKCIAAAPHM EATTCVKPSF NQEDIYITTE SLTTTARMSE TADTAPDAEP VPDYTTVHTV
KSPRGLILNA TALPLPDKKK FLSSCGYVST DQLNKIMQ


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