ID H3BA31_LATCH Unreviewed; 689 AA.
AC H3BA31;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Thyrotropin receptor {ECO:0000256|ARBA:ARBA00017324, ECO:0000256|RuleBase:RU361222};
GN Name=TSHR {ECO:0000256|RuleBase:RU361222,
GN ECO:0000313|Ensembl:ENSLACP00000018752.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000018752.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000018752.1}
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 EMBL; AFYH01041682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BA31; -.
DR STRING; 7897.ENSLACP00000018752; -.
DR Ensembl; ENSLACT00000018885.1; ENSLACP00000018752.1; ENSLACG00000016507.1.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000156510; -.
DR HOGENOM; CLU_006130_1_1_1; -.
DR InParanoid; H3BA31; -.
DR OMA; TRDMRQS; -.
DR TreeFam; TF316814; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000016507; Expressed in pectoral fin and 3 other cell types or tissues.
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; cd15964; 7tmA_TSH-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; 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 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 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:UP000008672};
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 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 501..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 353..600
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 637..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 78165 MW; AB62E3B5476A46B5 CRC64;
YIQLDCIFLL FLPSFFFYKL TSVTQKEIRN AKSLNYIHPD AFQNLPLLKY LGIFNTGLTL
FPDLTKVYSA DVNFLLEIAE NPHISTVPAN ALYGLSNESL TLKLYNNGFT VVRSFAFNGT
KLDAVYLHKN RYLTLIEEDV FGGVHSGPTL LDVSQTSVST LPTKGLENLR EFMAKNTWTL
KKLPPIKNFL HLIRADLSYP SHCCAFKNWK RYKGILESVM CNQTTISGLR QKRAVNGLNI
PYYQDYREDD MDRSNAIYDE NSRFRDFHSS SHHYYVFYET EGEGDLGFGT ELKNPQKGNV
SDFDTQYDYT VCGGMEDMVC IPEPDEFNPC EDIMGYKFLR IIVWFVNLLA ILGNIFVLLI
LLTSHYKLTV PRFLMCNLAF ADFCMGIYLL LIASVDLHTQ SEYYNRAIDW QTGPGCNAAG
FFTVFASELS VYTLTVITLE RWYAITFAMR LDRKIRLRHA SAIMLGGWLF CFLLAILPLV
GVSSYAKVSI CLPMDTETLL AQVYVICVLM LNIIAFIIIC ACYIKIYITV RNPHYKSGNK
DTKIAKRMAI LIFTDFICMA PISFYALSAI LNKPLITVTN SKILLVLFYP LNSCANPFLY
AIFTKAFRRD VFILLSKLGF CEHQAQVYRG QTITGKNSSG SYGQRGSGGT GQTLTNINDP
SKPEQYASYR PAVTAHGKVI PETCKLTQM
//
