TSHR_FELCA
ID TSHR_FELCA Reviewed; 763 AA.
AC Q9BGN4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Thyrotropin receptor;
DE AltName: Full=Thyroid-stimulating hormone receptor;
DE Short=TSH-R;
DE Flags: Precursor;
GN Name=TSHR;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11796491; DOI=10.1210/endo.143.2.8622;
RA Nguyen L.Q., Arseven O.K., Gerber H., Stein B.S., Jameson J.L., Kopp P.;
RT "Cloning of the cat TSH receptor and evidence against an autoimmune
RT etiology of feline hyperthyroidism.";
RL Endocrinology 143:395-402(2002).
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 -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P16473}.
CC -!- PTM: Sulfated. Sulfation on Tyr-384 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; AF218264; AAK00133.1; -; mRNA.
DR RefSeq; NP_001009288.1; NM_001009288.1.
DR AlphaFoldDB; Q9BGN4; -.
DR SMR; Q9BGN4; -.
DR STRING; 9685.ENSFCAP00000010296; -.
DR GeneID; 493842; -.
DR KEGG; fca:493842; -.
DR CTD; 7253; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; Q9BGN4; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
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:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
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:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..763
FT /note="Thyrotropin receptor"
FT /id="PRO_0000233346"
FT TOPO_DOM 22..412
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..440
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..472
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..516
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..559
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..601
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..648
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..659
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..681
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 100..124
FT /note="LRR 1"
FT REPEAT 125..150
FT /note="LRR 2"
FT REPEAT 151..174
FT /note="LRR 3"
FT REPEAT 176..199
FT /note="LRR 4"
FT REPEAT 201..223
FT /note="LRR 5"
FT REPEAT 225..248
FT /note="LRR 6"
FT REPEAT 264..288
FT /note="LRR 7"
FT MOTIF 761..763
FT /note="PDZ-binding"
FT MOD_RES 384
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 493..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 763 AA; 86588 MW; 937F60A140487D60 CRC64;
MRQTPLLQLA LLLSLPRSLG GKGCPSPPCE CHQEDDFRVT CKDIHRIPSL PPSTQTLKFI
ETHLKTIPSR AFSNLPNISR IYLSIDATLQ RLESHSFYNL SKMTHIEIRN TRSLTYIDPG
ALKELPLLKF LGIFNTGLGV FPDLTKVYST DVFFILEITD NPYMTSIPAN AFQGLCNETL
TLKLYNNGFT SIQGHAFNGT KLDAVYLNKN KYLTAIDQDA FGGVYSGPTL LDVSYTSVTA
LPSKGLEHLK ELIARNTWTL KKLPLTLSFL HLTRADLSYP SHCCAFKNQK KIRGILESFM
CNDSSIRSLR QRKSVNALNG PFDQEYEEYL GDSHAGYKDN SKFQDTRSNS HYYVFFEEQD
EILGFGQELK NPQEETLQAF DSHYDYTVCG GNEDMVCTPK SDEFNPCEDI MGYKFLRIVV
WFVSLLALLG NVFVLIILLT SHYKLTVPRF LMCNLAFADF CMGMYLLLIA SVDLYTHSEY
YNHAIDWQTG PGCNAAGFFT VFASELSVYT LTVITLERWY AITFAMRLDR KMRLRHAYAI
MVGGWVCCFL LALLPLVGIS SYAKVSICLP MDTETPLALA YIILVLLLNI VAFIIVCSCY
VKIYITVRNP QYNTGDKDTK IAKRMAVLIF TDFMCMAPIS FYALSALMNK PLITVTNSKI
LLVLFYPLNS CANPFLYAIF TKTFQRDVFI LLSKFGICKR QAQAYRGQRV SPKNSTGIQV
QKVTRNMRQS LPNMQDDYEL LENSHLTPNK QSHISKEYNQ TVL
