GenomeNet

Database: UniProt
Entry: G3V6J1_RAT
LinkDB: G3V6J1_RAT
Original site: G3V6J1_RAT 
ID   G3V6J1_RAT              Unreviewed;       764 AA.
AC   G3V6J1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Thyrotropin receptor {ECO:0000256|ARBA:ARBA00017324, ECO:0000256|RuleBase:RU361222};
GN   Name=Tshr {ECO:0000313|Ensembl:ENSRNOP00000005671.2,
GN   ECO:0000313|RGD:3911}; Synonyms=TSHR {ECO:0000256|RuleBase:RU361222};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000005671.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000005671.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000005671.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000005671.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000005671.2};
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   AlphaFoldDB; G3V6J1; -.
DR   SMR; G3V6J1; -.
DR   Ensembl; ENSRNOT00000005671.5; ENSRNOP00000005671.2; ENSRNOG00000003972.7.
DR   RGD; 3911; Tshr.
DR   GeneTree; ENSGT00940000156510; -.
DR   HOGENOM; CLU_006130_1_1_1; -.
DR   OMA; TRDMRQS; -.
DR   OrthoDB; 1202285at2759; -.
DR   TreeFam; TF316814; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000003972; Expressed in kidney and 8 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   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
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; IPR026906; LRR_5.
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   Pfam; PF13306; LRR_5; 2.
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:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|RuleBase:RU361222};
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   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   CHAIN           22..764
FT                   /note="Thyrotropin receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT                   /id="PRO_5015019705"
FT   TRANSMEM        419..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        452..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        538..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        580..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        627..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
SQ   SEQUENCE   764 AA;  86604 MW;  84802EC142CB2095 CRC64;
     MRPGSLLQLT LLLALPRSLW GRGCTSPPCE CHQEDDFRVT CKELHRIPSL PPSTQTLKLI
     ETHLKTIPSL AFSSLPNISR IYLSIDATLQ RLEPHSFYNL SKMTHIEIRN TRSLTYIDPD
     ALTELPLLKF LGIFNTGLRI FPDLTKIYST DVFFILEITD NPYMTSVPEN AFQGLCNETL
     TLKLYNNGFT SIQGHAFNGT KLDAVYLNKN KYLTAIDKDA FGGVYSGPTL LDVSSTSVTA
     LPSKGLEHLK ELIAKNTWTL KKLPLSLSFL HLTRADLSYP SHCCAFKNQK KIRGILESLM
     CNESSIRNLR QRKSVNVMRG PVYQEYEEGL GDNHVGYKQN SKFQEGPSNS HYYVFFEEQE
     DEIIGFGQEL KNPQEETLQA FDSHYDYTVC GDNEDMVCTP KSDEFNPCED IMGYKFLRIV
     VWFVSLMALL GNVFVLFVLL TSHYKLTVPR FLMCNLAFAD FCMGVYLLLI ASVDLYTHTE
     YYNHAIDWQT GPGCNTAGFF TVFASELSVY TLTVITLERW YAITFAMRLD RKIRLRHAYT
     IMAGGWVSCF LLALLPMVGI SSYAKVSICL PMDTDTPLAL AYIALVLLLN VVAFVIVCSC
     YVKIYITVRN PQYNPRDKDT KIAKRMAVLI FTDFMCMAPI SFYALSALMN KPLITVTNSK
     ILLVLFYPLN SCANPFLYAI FTKAFQRDVF ILLSKFGLCK HQAQAYQAQR VCPNNNTGIQ
     IQKIPQDTRQ SLPNVQDTYE PLGSSHLTPK LQGRISEEYT QTAL
//
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