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Database: UniProt
Entry: GHR_PAPAN
LinkDB: GHR_PAPAN
Original site: GHR_PAPAN 
ID   GHR_PAPAN               Reviewed;         638 AA.
AC   Q9XSZ1;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 106.
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   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=10425448; DOI=10.1677/jme.0.0230067;
RA   Zogopoulos G., Nathanielsz P., Hendy G.N., Goodyer C.G.;
RT   "The baboon: a model for the study of primate growth hormone receptor gene
RT   expression during development.";
RL   J. Mol. Endocrinol. 23:67-75(1999).
CC   -!- FUNCTION: Receptor for pituitary gland growth hormone involved in
CC       regulating postnatal body growth. On ligand binding, couples to, and
CC       activates the 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   -!- 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; AF150751; AAD39536.1; -; mRNA.
DR   RefSeq; NP_001106086.1; NM_001112616.1.
DR   AlphaFoldDB; Q9XSZ1; -.
DR   SMR; Q9XSZ1; -.
DR   STRING; 9555.ENSPANP00000000849; -.
DR   GlyCosmos; Q9XSZ1; 5 sites, No reported glycans.
DR   GeneID; 100126695; -.
DR   KEGG; panu:100126695; -.
DR   CTD; 2690; -.
DR   eggNOG; KOG3555; Eukaryota.
DR   OrthoDB; 5317462at2759; -.
DR   Proteomes; UP000028761; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   GO; GO:0060396; P:growth hormone receptor signaling pathway; IEA:UniProt.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR23037:SF41; CYTOKINE RECEPTOR-LIKE FACTOR 2-RELATED; 1.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF12772; GHBP; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 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_0000010963"
FT   CHAIN           19..256
FT                   /note="Growth hormone-binding protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000010964"
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          353..388
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   COMPBIAS        357..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  71407 MW;  9E2500C8E303E420 CRC64;
     MDLWQLLLTL ALAGSSDAFS GSEPTAAILS RASWSLQSVN PGLKTNSSKE PKFTKCRSPE
     RETFSCHWTD AVHHGSKSLG PIQLFYTRRN IQEWTQEWKE CPDYVSAGEN SCYFNSSFTS
     VWIPYCIKLT SNGDTVDGKC FSVDEIVQPD PPIALNWTLL NVSLTGIHAD IQVRWEAPPN
     ADIQKGWMVL EYELQYKEVN ETKWKMMDPI LSTSVPVYSL KVDKEYEVRV RSKRRNSGNY
     GEFSEVLYVT LPQMNQFTCE EDFYFPWLLI IIFGIFGLTV MLFVFLFSKQ QRIKMLILPP
     VPVPKIKGID PDLLKEGKLE EVNTILAIHD SYKPEFHSDD SWVEFIELDI DEPDEKNEGS
     DTDRLLSSDH QKSHSNLGVK DGDSGRTSCY EPDILETDFN ANNIHEGTSE VAQPQRLKGE
     ADLLCLDQKN QNKSPYHDAC PAAQQSSVIQ AEKNKPQPLP TDGAESTHQA AHIQLSNPSS
     LANIDFYAQV SDITPAGSVV LSPGQKNKAG MSQCDMHLEM VSLCQEDFIM DNAYFCEADA
     KKCIPVAPHI KVESHIEPSF NQEDIYITTE SLTTTAGRPG TTEHIPGSEM PVPDYTSIHI
     VQSPQGLILN ATALPLPGKE FLSSCGYVST DQLNKIMP
//
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