TSHR_PIG
ID TSHR_PIG Reviewed; 764 AA.
AC Q8SPP9; Q9BG55; Q9BG56;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Thyrotropin receptor;
DE AltName: Full=Thyroid-stimulating hormone receptor;
DE Short=TSH-R;
DE Flags: Precursor;
GN Name=TSHR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Thyroid;
RX PubMed=12880144; DOI=10.1515/cclm.2003.121;
RA Igarashi M., Nagata A.;
RT "Molecular cloning, sequencing and functional expression of porcine
RT thyrotropin (TSH) receptor cDNA).";
RL Clin. Chem. Lab. Med. 41:796-803(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thyroid;
RA Melen L.B., McNamara E.M., Hennen G.P., Igout A.;
RT "Porcine thyroid stimulating hormone receptor (TSHR) mRNA variant.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11847099; DOI=10.1093/emboj/21.4.504;
RA Costagliola S., Panneels V., Bonomi M., Koch J., Many M.C., Smits G.,
RA Vassart G.;
RT "Tyrosine sulfation is required for agonist recognition by glycoprotein
RT hormone receptors.";
RL EMBO J. 21:504-513(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8SPP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8SPP9-2; Sequence=VSP_018131;
CC -!- TISSUE SPECIFICITY: Expressed in thyroide cells (at protein level).
CC {ECO:0000269|PubMed:11847099}.
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; AY082015; AAL92560.1; -; mRNA.
DR EMBL; AF338249; AAK08510.1; -; mRNA.
DR EMBL; AF338250; AAK08511.1; -; mRNA.
DR RefSeq; NP_999462.1; NM_214297.1.
DR AlphaFoldDB; Q8SPP9; -.
DR SMR; Q8SPP9; -.
DR STRING; 9823.ENSSSCP00000027468; -.
DR PaxDb; Q8SPP9; -.
DR GeneID; 397560; -.
DR KEGG; ssc:397560; -.
DR CTD; 7253; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; Q8SPP9; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 1: Evidence at protein 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..764
FT /note="Thyrotropin receptor"
FT /id="PRO_0000233347"
FT TOPO_DOM 22..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..150
FT /note="LRR 1"
FT REPEAT 151..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 107..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018131"
FT CONFLICT 154
FT /note="F -> L (in Ref. 2; AAK08511)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="P -> T (in Ref. 1; AAL92560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 86644 MW; 1E8E8BDB617E7052 CRC64;
MSLTPLLQLA LLLALPRSLR GKGCPSPPCE CHQEDDFRVT CKDIHSIPPL PPNTQTLKFI
ETHLKTIPSR AFSNLPNISR IYLSIDATLQ QLESQSFYNL SKMTHIEIRN TRSLTYINPG
ALKDLPLLKF LGIFNTGLRI FPDLTKVYST DVFFILEITD NPYMTSIPAN AFQGLCNETL
TLKLYNNGFT SVQGHAFNGT KLDAVYLNKN KYLTVIDKDA FGGVFSGPTL LDVSYTSVTA
LPPKGLEHLK ELIARNTWTL KKLPLSLSFL HLTRADLSYP SHCCAFKNQK KIRGILESLM
CNESSIRSLR QRKSVNAVNG PFYQEYEEDL GDSSVGNKEN SKFQDTHSNS HYYVFFEEQE
DEIIGFGQEL KNPQEETLQA FDSHYDYTVC GGSEDMVCTP KSDEFNPCED IMGYRFLRIV
VWFVSLLALL GNVFVLVILL TSHYKLTVPR FLMCNLAFAD FCMGMYLLLI ASVDLYTQSE
YYNHAIDWQT GPGCNTAGFF TVFASELSVY TLTVITLERW YAITFAMRLD RKIRLRHAYA
IMAGGWVCCF LLALLPLVGI SSYAKVSICL PMDTETPLAL AYIILVLLLN IVAFTIVCSC
YVKIYITVRN PQYNPGDKDT KIAKRMAVLI FTDFMCMAPI SFYALSALMN KPLITVTNSK
ILLVLFYPLN SCANPFLYAI FTKAFQRDVF ILLSKFGFCK RQAQAYRGQR VSPKNSTGIQ
VQKVTQNMRQ SLPNMQDDYE LLENSHLTHK KHDQISKEYK QPVL
