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Database: UniProt
Entry: A3KEZ5_FUNHE
LinkDB: A3KEZ5_FUNHE
Original site: A3KEZ5_FUNHE 
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
//
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