TSHR_CANLF
ID TSHR_CANLF Reviewed; 764 AA.
AC P14763;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Thyrotropin receptor;
DE AltName: Full=Thyroid-stimulating hormone receptor;
DE Short=TSH-R;
DE Flags: Precursor;
GN Name=TSHR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2602159; DOI=10.1093/nar/17.24.10493;
RA Parmentier M., Libert F., Maenhaut C., Lefort A., Gerard C., Perret J.,
RA van Sande J., Dumont J.E., Vassart G.;
RT "Nucleotide sequence of the dog thyrotropin receptor cDNA.";
RL Nucleic Acids Res. 17:10493-10493(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2556796; DOI=10.1126/science.2556796;
RA Parmentier M., Libert F., Maenhaut C., Lefort A., Gerard C., Perret J.,
RA van Sande J., Dumont J.E., Vassart G.;
RT "Molecular cloning of the thyrotropin receptor.";
RL Science 246:1620-1622(1989).
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:0000250|UniProtKB:P16473, ECO:0000250|UniProtKB:P21463}.
CC -!- SUBUNIT: Interacts with heterodimer GPHA2:GPHB5; this interaction
CC stimulates cAMP production. Interacts (via the PDZ-binding motif) with
CC SCRIB; regulates TSHR trafficking and function.
CC {ECO:0000250|UniProtKB:P16473}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16473};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P16473}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P14763-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P14763-2; Sequence=VSP_001980;
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P16473}.
CC -!- PTM: Sulfated. Sulfation on Tyr-385 plays a role in thyrotropin
CC receptor binding and activation. {ECO:0000250|UniProtKB:P16473}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X17146; CAA35026.1; -; mRNA.
DR EMBL; X17147; CAA35027.1; -; mRNA.
DR EMBL; M29957; AAA30901.1; -; mRNA.
DR EMBL; M90047; AAA30902.1; -; mRNA.
DR PIR; A40077; A40077.
DR RefSeq; NP_001003285.1; NM_001003285.1. [P14763-1]
DR AlphaFoldDB; P14763; -.
DR SMR; P14763; -.
DR STRING; 9612.ENSCAFP00000025490; -.
DR PaxDb; P14763; -.
DR Ensembl; ENSCAFT00030007006; ENSCAFP00030006153; ENSCAFG00030003718. [P14763-1]
DR Ensembl; ENSCAFT00030007029; ENSCAFP00030006164; ENSCAFG00030003718. [P14763-2]
DR GeneID; 403968; -.
DR KEGG; cfa:403968; -.
DR CTD; 7253; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; P14763; -.
DR OrthoDB; 257031at2759; -.
DR Reactome; R-CFA-375281; Hormone ligand-binding receptors.
DR Reactome; R-CFA-418555; G alpha (s) signalling events.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0004996; F:thyroid-stimulating hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1904588; P:cellular response to glycoprotein; ISS:UniProtKB.
DR GO; GO:1905229; P:cellular response to thyrotropin-releasing hormone; ISS:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
DR GO; GO:0038194; P:thyroid-stimulating hormone signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 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:SF0; PTHR24372:SF0; 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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Leucine-rich repeat; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Sulfation; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT CHAIN 21..764
FT /note="Thyrotropin receptor"
FT /id="PRO_0000012785"
FT TOPO_DOM 21..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..441
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..473
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..517
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..560
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..602
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..649
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..660
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..682
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 125..149
FT /note="LRR 1"
FT REPEAT 150..174
FT /note="LRR 2"
FT REPEAT 176..199
FT /note="LRR 3"
FT REPEAT 201..223
FT /note="LRR 4"
FT REPEAT 225..248
FT /note="LRR 5"
FT REPEAT 250..271
FT /note="LRR 6"
FT MOTIF 762..764
FT /note="PDZ-binding"
FT MOD_RES 385
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16473"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 494..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 81..105
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001980"
SQ SEQUENCE 764 AA; 86483 MW; 49F03B3DBCB65512 CRC64;
MRPPPLLHLA LLLALPRSLG GKGCPSPPCE CHQEDDFRVT CKDIHRIPTL PPSTQTLKFI
ETQLKTIPSR AFSNLPNISR IYLSIDATLQ RLESHSFYNL SKMTHIEIRN TRSLTSIDPD
ALKELPLLKF LGIFNTGLGV FPDVTKVYST DVFFILEITD NPYMASIPAN AFQGLCNETL
TLKLYNNGFT SIQGHAFNGT KLDAVYLNKN KYLSAIDKDA FGGVYSGPTL LDVSYTSVTA
LPSKGLEHLK ELIARNTWTL KKLPLSLSFL HLTRADLSYP SHCCAFKNQK KIRGILESLM
CNESSIRSLR QRKSVNTLNG PFDQEYEEYL GDSHAGYKDN SQFQDTDSNS HYYVFFEEQE
DEILGFGQEL KNPQEETLQA FDSHYDYTVC GGNEDMVCTP KSDEFNPCED IMGYKFLRIV
VWFVSLLALL GNVFVLIVLL TSHYKLTVPR FLMCNLAFAD FCMGMYLLLI ASVDLYTHSE
YYNHAIDWQT GPGCNTAGFF TVFASELSVY TLTVITLERW YAITFAMRLD RKIRLRHAYA
IMVGGWVCCF LLALLPLVGI SSYAKVSICL PMDTETPLAL AYIILVLLLN IVAFIIVCSC
YVKIYITVRN PQYNPGDKDT KIAKRMAVLI FTDFMCMAPI SFYALSALMN KPLITVTNSK
ILLVLFYPLN SCANPFLYAI FTKAFQRDVF ILLSKFGICK RQAQAYRGQR VSPKNSAGIQ
IQKVTRDMRQ SLPNMQDEYE LLENSHLTPN KQGQISKEYN QTVL
