ID A3KEZ5_FUNHE Unreviewed; 698 AA.
AC A3KEZ5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Thyrotropin receptor {ECO:0000256|ARBA:ARBA00017324, ECO:0000256|RuleBase:RU361222};
GN Name=TSHR {ECO:0000256|RuleBase:RU361222};
OS Fundulus heteroclitus (Killifish) (Mummichog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX NCBI_TaxID=8078 {ECO:0000313|EMBL:BAF48336.1};
RN [1] {ECO:0000313|EMBL:BAF48336.1}
RP NUCLEOTIDE SEQUENCE.
RA Ohkubo M., Shimizu A.;
RT "Molecular cloning of cDNAs encoding 2 gonadotropin receptors from
RT mummichog Fundulus heteroclitus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 EMBL; AB295490; BAF48336.1; -; mRNA.
DR RefSeq; NP_001296925.1; NM_001309996.1.
DR GeneID; 105933778; -.
DR CTD; 2492; -.
DR OrthoDB; 1202285at2759; -.
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; IPR001611; Leu-rich_rpt.
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:SF74; LP13728P; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 1.
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; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361222};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU361222};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361222};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361222};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361222};
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 SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT CHAIN 17..698
FT /note="Thyrotropin receptor"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT /id="PRO_5005121378"
FT TRANSMEM 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 408..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 452..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 494..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 537..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 583..605
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 387..634
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 698 AA; 77770 MW; 51D5DA9B7E7B524E CRC64;
MVAVALIMLM TKMASASMPG SETDLKRRYG TGFPELDRSS CHLVGFGVRA IPSNISSNTQ
CLEVKQTQII EIHQHAFTNL QHLSKLQILQ NNILQSIGES AFAGLPQLSD VWISENLALE
TIKAFAFSNL PKLTDIEITK SKHLRSIHPD AFRNIVNLRR LTISNTGLRI FPDLSKIHSA
AQDFLFDLQD NIHIETVPAN AFRGLCTKTI TEIRLTRNGI KEVASDAFNG TKMYRLLLSG
NEQLTHISPD AFAGSSALVM LDVSHTAVSS LPDSILGGLR RLLARSAYRL KELPVVQRYT
KLYVANLTYP SHCCAFKNMH RNRSTWTSLC SHPQAKTIPA FFREHCSNST SISCSPQPDS
FNPCEDIMSP TPLRILIWII SVLALLGNAM VLLVLLGSRS KLTVPRFLMC HLAFADLCMG
VYLVVIATVD MLTHGRYYNH AVDWQTGFGC KAAGFFTVFA SELSVFTLTA ITVERWHTIT
NAMRLDRKLR LRHACIIMTI GWSFSLLAAL LPTVGVSSYG KVSICLPMDV ESVVSQVYVV
SLLILNILAF FCVCGCYLSI YLTYRKPSSA PAHADTRVAQ RMAVLIFTDF VCLAPISFFA
ISAALKLPLI TVSDTKLLLX LFYPINSCSN PFLYAFFTHT FRRDFFLLAA RFGLFKTQAQ
IYRTETSSCQ QPTWTSPKSS RVMYSLANTL SLDGKQEF
//