TSHR_ICTPU
ID TSHR_ICTPU Reviewed; 778 AA.
AC Q6QMG1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Thyrotropin receptor {ECO:0000305};
DE AltName: Full=Thyroid-stimulating hormone receptor {ECO:0000303|PubMed:19523396};
DE Short=TSH-R;
DE Flags: Precursor;
GN Name=tshr {ECO:0000303|PubMed:19523396};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19523396; DOI=10.1016/j.ygcen.2009.01.009;
RA Goto-Kazeto R., Kazeto Y., Trant J.M.;
RT "Molecular cloning, characterization and expression of thyroid-stimulating
RT hormone receptor in channel catfish.";
RL Gen. Comp. Endocrinol. 161:313-319(2009).
CC -!- FUNCTION: Receptor for the thyroid-stimulating hormone (TSH) or
CC thyrotropin (PubMed:19523396). Also acts as a receptor for the
CC heterodimeric glycoprotein hormone thyrostimulin. The activity of this
CC receptor is mediated by G proteins which activate adenylate cyclase.
CC Plays a central role in controlling thyroid cell metabolism (By
CC similarity). {ECO:0000250|UniProtKB:P16473,
CC ECO:0000250|UniProtKB:P21463, ECO:0000269|PubMed:19523396}.
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 -!- TISSUE SPECIFICITY: Expressed in ventral aorta, testis and post-
CC vitellogenic ovary (at protein level). Also expressed in kidney.
CC Detected in unfertilized, but not fertilized eggs.
CC {ECO:0000269|PubMed:19523396}.
CC -!- INDUCTION: Ovarian expression levels tend to be low throughout
CC vitellogenesis. Expression levels increase at the anticipated spawning
CC period, and gradually decrease afterwards until the onset of ovarian
CC recrudescence. {ECO:0000269|PubMed:19523396}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY533543; AAS45557.1; -; mRNA.
DR RefSeq; NP_001187121.1; NM_001200192.1.
DR AlphaFoldDB; Q6QMG1; -.
DR SMR; Q6QMG1; -.
DR STRING; 7998.ENSIPUP00000007395; -.
DR GeneID; 100304626; -.
DR KEGG; ipu:100304626; -.
DR CTD; 7253; -.
DR OMA; HAGYKDN; -.
DR OrthoDB; 257031at2759; -.
DR Proteomes; UP000221080; Chromosome 2.
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:0016020; C:membrane; IDA:AgBase.
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; IMP:AgBase.
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:0007276; P:gamete generation; IEP:AgBase.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IMP:AgBase.
DR GO; GO:0097066; P:response to thyroid hormone; IMP:AgBase.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0038194; P:thyroid-stimulating hormone signaling pathway; IMP:AgBase.
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; IPR001611; Leu-rich_rpt.
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; 1.
DR Pfam; PF13855; LRR_8; 1.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Membrane; Receptor; Repeat; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..778
FT /note="Thyrotropin receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431959"
FT TOPO_DOM 19..420
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 421..441
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 451..471
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..494
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..515
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 540..560
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..581
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..602
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 626..646
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..660
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 661..681
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 50..73
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 99..123
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 124..149
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 151..173
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 175..198
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 199..222
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 224..247
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 775..777
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P16473"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P16473"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P16473"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P16473"
FT DISULFID 30..40
FT /evidence="ECO:0000250|UniProtKB:P16473"
FT DISULFID 494..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 778 AA; 87360 MW; 553E040DCE540955 CRC64;
MRLFALVLIF FFSTRTCTED VKSCPNGCEC TDWKGYYVSC TDIATLPIFP GNTETLRLYE
TRLSSVPQDA FVNMVNISLI YLSVDVTLRS LEKHSFFNLK KITHVEIRNT RSLMSIDPEA
FKDLPELKYL GLFNTGLTIF PALTRIHSHE SNFMLEITDN LYITEIPANA FQGITKDALT
VMLYSNGFTK IQHHAFNGTK LDAIYLHRNK ELTELSEDMF AETISGPVLL DVSDSGVTSL
PATGLESLRE LSARNVWALK KLPSVKTFRH LIGADMTYPS HCCAFKNLKK KKGYLDYIIC
NLTAMRGQHY ERSVGRITVP AVMDGTDKGI DISDPLLGNT YDHHDFLRSL HYHEFLGGHA
DYDMGFGDTL KNPQIATSQD FDSHYDYVVC EDGEAVTCAP APDDFNPCED IMGFSFLRVS
VWFVSLLAVL GNMVVLFVLL TSHYKLSVSR FLMCHLAIAD LCMGIYLLLI ASVDLYTQSE
YYNHAIDWQT GPWCTLAGFI SIFATELSVY TLTTITLERW HAINFAMQLD RKLRLSHASA
VMLGGWLLCL LLALMPVLGV SSYQKVSICL PMSTQNLLDQ VYILFILVIN IVAFVAICAC
YIKIYCAVHN PNYTSSRKDS SIAKRMAVLI FTNFLCIAPI SFYAISAALD HPLITISNSK
ILLVLFYPLN SCANPFLYAI FTKAFQGDVF ILLSKIGLCE QQAKLFRGQT ISTRASSGDT
NRRGIKTKIL TRWNVQATAT CHQSSVNKDN NTSRGRKCEP TANKSKHIQG MNSTMVFY
