ID G3Q431_GASAC Unreviewed; 659 AA.
AC G3Q431;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Thyrotropin receptor {ECO:0000256|ARBA:ARBA00017324, ECO:0000256|RuleBase:RU361222};
GN Name=TSHR {ECO:0000256|RuleBase:RU361222,
GN ECO:0000313|Ensembl:ENSGACP00000024635.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000024635.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000024635.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000024635.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for the thyroid-stimulating hormone (TSH) or
CC thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein
CC hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor
CC is mediated by G proteins which activate adenylate cyclase. Plays a
CC central role in controlling thyroid cell metabolism.
CC {ECO:0000256|RuleBase:RU361222}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004554}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361222}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034693}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000256|RuleBase:RU361222}.
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DR AlphaFoldDB; G3Q431; -.
DR Ensembl; ENSGACT00000024684.1; ENSGACP00000024635.1; ENSGACG00000018635.1.
DR GeneTree; ENSGT00940000156510; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004996; F:thyroid-stimulating hormone receptor activity; IEA:InterPro.
DR CDD; cd15136; 7tmA_Glyco_hormone_R; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002131; Gphrmn_rcpt_fam.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002274; TSH_rcpt.
DR PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24372:SF0; THYROTROPIN RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF13306; LRR_5; 2.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01145; TSHRECEPTOR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361222};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU361222};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361222};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361222};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU361222};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361222};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361222}.
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 400..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 486..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 529..554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 575..597
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 379..626
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 659 AA; 74138 MW; 6240CE8674BA7329 CRC64;
EYCPIHCKCD WDIYSVSCVG AEAMPVFHSS TQEVWLVGTK LSSLPPNAFA NLANIVHIQL
TGIKTLSYID QEAFKNLPNL NYLGITNTGL TSFPGLQYIQ STKDDFILEI VENVFLQSIP
ANSFNGISKN ALTIMLNSNG VKEIQQYAFN GSRLEELYLH RNVDLERIDE FAFHGVIHGP
THLDLSETKV SSLPSMGMET IEKLQAKNTW DLKELPPLKA FLHLQSAELT FPSHCCGLKM
LKRWRGNSEA VICNLTGNAL GKLRESSVAF SQRYLGNKIY HHLNDSFGLP SAKSRNHTHT
NTPICPTEQC ENEGLFYVEL PTEHPNEGFD FEMCDEVHTE SHGLLCTPLP DALNPCEDVL
SQGFLRVLVW VVSPLAILAN FLVLFILLTS QQKMSVTRFL MGHLAFADFC MGIYLLLVAS
VDLYTRSHYY HYAIAWQTEG GCNLAGTISV FASELSVYTL TLISLQRWHA IFYAMRADRK
IRLRHAAVLM LVGWLLCALL AMLPLVGVSS YQKVSICLPM DTETTAARVY VVSVLMVNVI
AFMVVCLCYI HIYYMVHNPQ HQSSSSDTSM AKRMAVLIFT NFLCLAPICF YGLSAAFQQP
LMTITDSKVL LVLFYPLNSC AHPFFYAILT KAFHRDILML LNRMGLCQRQ AHLYRSQLV
//
