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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_PIG                 Reviewed;         638 AA.
P19756;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
25-OCT-2017, entry version 134.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Landrace X Yorkshire; TISSUE=Liver;
PubMed=2243805; DOI=10.1093/nar/18.21.6451;
Cioffi J.A., Wang X., Kopchick J.J.;
"Porcine growth hormone receptor cDNA sequence.";
Nucleic Acids Res. 18:6451-6451(1990).
[2]
PHOSPHORYLATION, STAT5 ACTIVATION, AND MUTAGENESIS OF TYR-332;
TYR-337; TYR-390; TYR-487; TYR-534; TYR-566; TYR-595 AND TYR-627.
PubMed=8647880; DOI=10.1074/jbc.271.21.12669;
Hansen L.H., Wang X., Kopchick J.J., Bouchelouche P., Nielsen J.H.,
Galsgaard E.D., Billestrup N.;
"Identification of tyrosine residues in the intracellular domain of
the growth hormone receptor required for transcriptional signaling and
Stat5 activation.";
J. Biol. Chem. 271:12669-12673(1996).
-!- 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. {ECO:0000250}.
-!- 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:0000250}.
-!- SUBCELLULAR LOCATION: Growth hormone-binding protein: Secreted
{ECO:0000250}. Note=Complexed to a substantial fraction of
circulating GH. {ECO:0000250}.
-!- 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. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
subfamily. {ECO:0000305}.
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EMBL; X54429; CAA38301.1; -; mRNA.
PIR; S12136; S12136.
UniGene; Ssc.93799; -.
ProteinModelPortal; P19756; -.
SMR; P19756; -.
DIP; DIP-650N; -.
STRING; 9823.ENSSSCP00000017873; -.
PaxDb; P19756; -.
PRIDE; P19756; -.
eggNOG; ENOG410IFQI; Eukaryota.
eggNOG; ENOG410XTHJ; LUCA.
HOGENOM; HOG000015773; -.
HOVERGEN; HBG005836; -.
InParanoid; P19756; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; 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; 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_0000010965.
CHAIN 19 256 Growth hormone-binding protein.
{ECO:0000250}.
/FTId=PRO_0000010966.
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 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 ubiquitin-dependent
internalization and down-regulation.
{ECO:0000250}.
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 332 332 Y->F: No effect.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 337 337 Y->F: No effect.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 390 390 Y->F: No effect.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 487 487 Y->F: No effect.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 534 534 Y->F: Loss of transcriptional signaling;
when associated with F-566 or F-627.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 566 566 Y->F: Loss of transcriptional signaling.
when associated with F-534 or F-627.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 595 595 Y->F: Loss of transcriptional signaling.
{ECO:0000269|PubMed:8647880}.
MUTAGEN 627 627 Y->F: Loss of transcriptional signaling.
when associated with F-534 or F-566.
{ECO:0000269|PubMed:8647880}.
SEQUENCE 638 AA; 71145 MW; BC7C66536F4DFF97 CRC64;
MDLWQLLLTL AVAGSSDAFS GSEATPAVLV RASQSLQRVH PGLETNSSGK PKFTKCRSPE
LETFSCHWTD GVRHGLQSPG SIQLFYIRRS TQEWTQEWKE CPDYVSAGEN SCYFNSSYTS
IWIPYCIKLT SNGGTVDQKC FSVEEIVQPD PPIGLNWTLL NISLTGIHAD IQVRWEPPPN
ADVQKGWIVL EYELQYKEVN ETQWKMMDPV LSTSVPVYSL RLDKEYEVRV RSRQRNSEKY
GEFSEVLYVT LPQMSPFACE EDFRFPWFLI IIFGIFGLTV ILFLLIFSKQ QRIKMLILPP
VPVPKIKGID PDLLKEGKLE EVNTILAIHD NYKHEFYSDD SWVEFIELDI DDPDEKTEGS
DTDRLLNNDH EKSLTILGAK EDDSGRTSCY EPDILETDFN ANDVCDGTAE VAQPQRLKGE
ADLLCLDQKN QNNSPSNDAA PATQQPSVIL AEENKPRPLI ISGTDSTHQT AHTQLSNPSS
LANIDFYAQV SDITPAGSVV LSPGQKNKAG ISQCDMHLEV VSPCPANFIM DNAYFCEADA
KKCIAMAPHV EVESRLAPSF NQEDIYITTE SLTTTAGRSA TAECAPSSEM PVPDYTSIHI
VQSPQGLVLN ATALPLPDKE FLSSCGYVST DQLNKIMP


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