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GHR_AILME
ID   GHR_AILME               Reviewed;         638 AA.
AC   Q95JF2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Growth hormone receptor;
DE            Short=GH receptor;
DE   AltName: Full=Somatotropin receptor;
DE   Contains:
DE     RecName: Full=Growth hormone-binding protein;
DE              Short=GH-binding protein;
DE              Short=GHBP;
DE     AltName: Full=Serum-binding protein;
DE   Flags: Precursor;
GN   Name=GHR;
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Liao M.J., Zhu M.Y., Zhang A.J.;
RT   "Molecular cloning of growth hormone receptor in giant panda.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for pituitary gland growth hormone involved in
CC       regulating postnatal body growth. On ligand binding, couples to the
CC       JAK2/STAT5 pathway (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone
CC       in plasma and may be a modulator/inhibitor of GH signaling.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: On growth hormone (GH) binding, forms homodimers and binds
CC       JAK2 via a box 1-containing domain. Binding to SOCS3 inhibits JAK2
CC       activation, binding to CIS and SOCS2 inhibits STAT5 activation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=On growth hormone binding, GHR is
CC       ubiquitinated, internalized, down-regulated and transported into a
CC       degradative or non-degradative pathway. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted
CC       {ECO:0000250}. Note=Complexed to a substantial fraction of circulating
CC       GH. {ECO:0000250}.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-surface
CC       receptor binding.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- DOMAIN: The extracellular domain is the ligand-binding domain
CC       representing the growth hormone-binding protein (GHBP).
CC   -!- DOMAIN: The ubiquitination-dependent endocytosis motif (UbE) is
CC       required for recruitment of the ubiquitin conjugation system on to the
CC       receptor and for its internalization. {ECO:0000250}.
CC   -!- PTM: On GH binding, phosphorylated on tyrosine residues in the
CC       cytoplasmic domain by JAK2. {ECO:0000250}.
CC   -!- PTM: On ligand binding, ubiquitinated on lysine residues in the
CC       cytoplasmic domain. This ubiquitination is not sufficient for GHR
CC       internalization (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF395535; AAK72050.1; -; mRNA.
DR   RefSeq; NP_001291819.1; NM_001304890.1.
DR   AlphaFoldDB; Q95JF2; -.
DR   SMR; Q95JF2; -.
DR   STRING; 9646.ENSAMEP00000004058; -.
DR   GeneID; 100422780; -.
DR   KEGG; aml:100422780; -.
DR   CTD; 2690; -.
DR   eggNOG; KOG3555; Eukaryota.
DR   InParanoid; Q95JF2; -.
DR   OrthoDB; 346239at2759; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR025871; GHBP.
DR   InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF12772; GHBP; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endocytosis; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Secreted; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..638
FT                   /note="Growth hormone receptor"
FT                   /id="PRO_0000010947"
FT   CHAIN           19..256
FT                   /note="Growth hormone-binding protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000010948"
FT   TOPO_DOM        19..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          151..254
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          294..379
FT                   /note="Required for JAK2 binding"
FT                   /evidence="ECO:0000250"
FT   REGION          429..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           240..244
FT                   /note="WSXWS motif"
FT   MOTIF           297..305
FT                   /note="Box 1 motif"
FT   MOTIF           340..349
FT                   /note="UbE motif"
FT   SITE            345
FT                   /note="Required for endocytosis and down-regulation"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10912"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..140
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   638 AA;  70846 MW;  84FC629FA5EA0351 CRC64;
     MDLWQLLLTL AVAGSGNAVS GSEATPAILG RASQSLQRVN PGPGTNPSGK PQFTKCRSPE
     LETFSCHWTE GVHHGVKNPG SIQLFYIRRS TQEWTPEWKE CPDYVSAGEN SCYFNSSYTS
     IWIPYCIKLT SNGDTVDQKC FSVEEIVQPD PPIGLNWTLL NISLTGIHAD IQVRWEPPPN
     ADVQKGWIVL EYELQYKEVN ESQWKMMDPV LSTSVPVYSL RLDKEYEVRV RSRQRNSEKY
     GEFSEVLYVA LPQMSPFACE EDFQFPWFLI IIFGIFGLTM ILFLFIFSKQ QRIKMLILPP
     VPVPKIKGID SDLLKEGKLE EVSTILAIHD NYKPEFYNDD SWVEFIELDI DDPDEKTEGS
     DTDRLLSNDH EKSLNILGAK DDDSGRTSCY EPDILETDFN ASDVCDGTSE VAQPQRLKGE
     IDLLCLDQKN QSNSPSTDTA PNTQQPGVIL AKENKPRPLL ISGTESTHQA AHPQLSNPSS
     LANIDFYAQV SDITPAGSVV LSPGQKNKAG IAPCDMPPEV VSLCQANFIM DNAYFCEADA
     KKCITVAPHV EAESRGEPSF NQEDIYITTE SLTTVAGQPG TAERAPSSEI PVPDYTSIHI
     VQSPRGLVLN ATALPLPDKE FLSSCGYVST DQLNKIMP
 
 
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