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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_RABIT               Reviewed;         638 AA.
P19941;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
25-OCT-2017, entry version 138.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2825030; DOI=10.1038/330537a0;
Leung D.W., Spencer S.A., Cachianes G., Hammonds R.G., Collins C.,
Henzel W.J., Barnard R., Waters M.J., Wood W.I.;
"Growth hormone receptor and serum binding protein: purification,
cloning and expression.";
Nature 330:537-543(1987).
[2]
GHBP SHEDDING SITE, AND SUBCELLULAR LOCATION.
PubMed=12403792; DOI=10.1074/jbc.M208738200;
Wang X., He K., Gerhart M., Huang Y., Jiang J., Paxton R.J., Yang S.,
Lu C., Menon R.K., Black R.A., Baumann G., Frank S.J.;
"Metalloprotease-mediated GH receptor proteolysis and GHBP shedding.
Determination of extracellular domain stem region cleavage site.";
J. Biol. Chem. 277:50510-50519(2002).
[3]
INTERACTION WITH ADAM17.
PubMed=14519102; DOI=10.1042/BJ20031321;
Schantl J.A., Roza M., Van Kerkhof P., Strous G.J.;
"The growth hormone receptor interacts with its sheddase, the tumour
necrosis factor-alpha-converting enzyme (TACE).";
Biochem. J. 377:379-384(2004).
[4]
UBIQUITINATION-DEPENDENT ENDOCYTOSIS MOTIF, AND MUTAGENESIS OF
ASN-338; ASP-339; ASP-340; SER-341; TRP-342; VAL-343; GLU-344;
PHE-345; ILE-346; GLU-347; LEU-348; ASP-349; ILE-350; ASP-351 AND
ASP-352.
PubMed=9878047; DOI=10.1093/emboj/18.1.28;
Govers R., ten Broeke T., van Kerkhof P., Schwartz A.L., Strous G.J.;
"Identification of a novel ubiquitin conjugation motif, required for
ligand-induced internalization of the growth hormone receptor.";
EMBO J. 18:28-36(1999).
[5]
PROTEOLYTIC PROCESSING BY ADAM17.
PubMed=11108241; DOI=10.1210/endo.141.12.7858;
Zhang Y., Jiang J., Black R.A., Baumann G., Frank S.J.;
"Tumor necrosis factor-alpha converting enzyme (TACE) is a growth
hormone binding protein (GHBP) sheddase: the metalloprotease
TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and
GHBP generation.";
Endocrinology 141:4342-4348(2000).
[6]
UBIQUITINATION, ENDOCYTOSIS, AND DEGRADATION.
PubMed=11418602; DOI=10.1074/jbc.M103583200;
Alves dos Santos C.M., ten Broeke T., Strous G.J.;
"Growth hormone receptor ubiquitination, endocytosis, and degradation
are independent of signal transduction via Janus kinase 2.";
J. Biol. Chem. 276:32635-32641(2001).
-!- FUNCTION: Receptor for pituitary gland growth hormone involved in
regulating postnatal body growth. On ligand binding, couples to,
and activates the JAK2/STAT5 pathway (By similarity).
{ECO:0000250}.
-!- 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 (By similarity). Binding
to SOCS3 inhibits JAK2 activation, binding to CIS and SOCS2
inhibits STAT5 activation (By similarity). Interacts with ADAM17.
{ECO:0000250, ECO:0000269|PubMed:14519102}.
-!- INTERACTION:
P42230:Stat5a (xeno); NbExp=3; IntAct=EBI-7526279, EBI-617434;
P42232:Stat5b (xeno); NbExp=6; IntAct=EBI-7526279, EBI-617454;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=On growth hormone
binding, GHR is ubiquitinated, internalized, down-regulated and
transported into a degradative or non-degradative pathway.
{ECO:0000269|PubMed:12403792}.
-!- SUBCELLULAR LOCATION: Growth hormone-binding protein: Secreted.
Note=Complexed to a substantial fraction of circulating GH.
-!- 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.
-!- DOMAIN: The extracellular domain is the ligand-binding domain
representing the growth hormone-binding protein (GHBP).
-!- DOMAIN: The ubiquitination-dependent endocytosis motif (UbE) is
required for recruitment of the ubiquitin conjugation system on to
the receptor and for its internalization.
-!- PTM: The soluble form (GHBP) is produced by phorbol ester-promoted
proteolytic cleavage at the cell surface (shedding) by
ADAM17/TACE. Shedding is inhibited by growth hormone (GH) binding
to the receptor probably due to a conformational change in GHR
rendering the receptor inaccessible to ADAM17.
{ECO:0000269|PubMed:11108241}.
-!- PTM: On GH binding, phosphorylated on tyrosine residues in the
cytoplasmic domain by JAK2. {ECO:0000250}.
-!- PTM: On ligand binding, ubiquitinated on lysine residues in the
cytoplasmic domain. This ubiquitination is not sufficient for GHR
internalization. {ECO:0000269|PubMed:11418602,
ECO:0000269|PubMed:9878047}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF015252; AAB67613.1; -; mRNA.
PIR; S08544; B28176.
RefSeq; NP_001076105.1; NM_001082636.1.
UniGene; Ocu.2168; -.
ProteinModelPortal; P19941; -.
SMR; P19941; -.
BioGrid; 1172345; 4.
DIP; DIP-313N; -.
IntAct; P19941; 4.
MINT; MINT-1535520; -.
STRING; 9986.ENSOCUP00000007343; -.
iPTMnet; P19941; -.
GeneID; 100009325; -.
KEGG; ocu:100009325; -.
CTD; 2690; -.
eggNOG; ENOG410IFQI; Eukaryota.
eggNOG; ENOG410XTHJ; LUCA.
HOGENOM; HOG000015773; -.
HOVERGEN; HBG005836; -.
InParanoid; P19941; -.
KO; K05080; -.
PMAP-CutDB; P19941; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL.
GO; GO:0070064; F:proline-rich region binding; IPI:BHF-UCL.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
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; PF00041; fn3; 1.
Pfam; PF12772; GHBP; 1.
SMART; SM00060; FN3; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Endocytosis; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 18
CHAIN 19 638 Growth hormone receptor.
/FTId=PRO_0000010967.
CHAIN 19 256 Growth hormone-binding protein.
/FTId=PRO_0000010968.
TOPO_DOM 19 264 Extracellular. {ECO:0000255}.
TRANSMEM 265 288 Helical. {ECO:0000255}.
TOPO_DOM 289 638 Cytoplasmic. {ECO:0000255}.
DOMAIN 151 254 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 260 262 Required for ADAM17-mediated proteolysis.
REGION 294 379 Required for JAK2 binding. {ECO:0000250}.
MOTIF 240 244 WSXWS motif.
MOTIF 297 305 Box 1 motif.
MOTIF 340 349 UbE motif.
SITE 345 345 Required for endocytosis and down-
regulation.
MOD_RES 341 341 Phosphoserine.
{ECO:0000250|UniProtKB:P10912}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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}.
MUTAGEN 338 338 N->A: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 339 339 D->A: Slightly impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 340 340 D->A: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 341 341 S->A: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 341 341 S->L,T: Slightly impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 342 342 W->A: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 342 342 W->L: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 343 343 V->A: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 343 343 V->G: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 344 344 E->A: Impaired GHR-mediated GH
internalization. Greatly reduced
ubiquitination.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 344 344 E->D: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 345 345 F->A: Impaired GHR-mediated GH
internalization. Greatly reduced
ubiquitination.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 345 345 F->L,V: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 345 345 F->Y: No effect on GHR-mediated GH
internalization. No effect on
ubiquitination.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 346 346 I->A: Impaired GHR-mediated GH
internalization. Greatly reduced
ubiquitination.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 346 346 I->F: Slightly impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 346 346 I->L: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 347 347 E->A,D: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 348 348 L->A,V: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 349 349 D->A: Impaired GHR-mediated GH
internalization. Greatly reduced
ubiquitination.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 349 349 D->E: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 349 349 D->N: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 350 350 I->A: Impaired GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 351 351 D->A: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
MUTAGEN 352 352 D->A: No effect on GHR-mediated GH
internalization.
{ECO:0000269|PubMed:9878047}.
SEQUENCE 638 AA; 71077 MW; E05CCE1D7294624C CRC64;
MDLWQLLLTV ALAGSSDAFS GSEATPATLG RASESVQRVH PGLGTNSSGK PKFTKCRSPE
LETFSCHWTD GVHHGLKSPG SVQLFYIRRN TQEWTQEWKE CPDYVSAGEN SCYFNSSYTS
IWIPYCIKLT NNGGMVDQKC FSVEEIVQPD PPIGLNWTLL NVSLTGIHAD IQVRWEPPPN
ADVQKGWIVL EYELQYKEVN ETQWKMMDPV LSTSVPVYSL RLDKEYEVRV RSRQRSSEKY
GEFSEVLYVT LPQMSPFTCE EDFRFPWFLI IIFGIFGLTV MLFVFIFSKQ QRIKMLILPP
VPVPKIKGID PDLLKEGKLE EVNTILAIQD SYKPEFYNDD SWVEFIELDI DDPDEKTEGS
DTDRLLSNSH QKSLSVLAAK DDDSGRTSCY EPDILENDFN ASDGCDGNSE VAQPQRLKGE
ADLLCLDQKN QNNSPYHDVS PAAQQPEVVL AEEDKPRPLL TGEIESTLQA APSQLSNPNS
LANIDFYAQV SDITPAGSVV LSPGQKNKAG NSQCDAHPEV VSLCQTNFIM DNAYFCEADA
KKCIAVAPHV DVESRVEPSF NQEDIYITTE SLTTTAERSG TAEDAPGSEM PVPDYTSIHL
VQSPQGLVLN AATLPLPDKE FLSSCGYVST DQLNKILP


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