GPHB5_MOUSE
ID GPHB5_MOUSE Reviewed; 130 AA.
AC Q812B2; Q8BJV2;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glycoprotein hormone beta-5;
DE AltName: Full=Thyrostimulin subunit beta;
DE Flags: Precursor;
GN Name=Gphb5; Synonyms=Gpb5, Zlut1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ;
RA Feldhaus A., Holloway J.L., O'Hogan S.L., Tackett M., Taft D., Thayer E.C.,
RA Webster P.;
RT "A novel glycoprotein hormone beta subunit.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP OVEREXPRESSION.
RX PubMed=16210345; DOI=10.1210/me.2005-0270;
RA Okada S.L., Ellsworth J.L., Durnam D.M., Haugen H.S., Holloway J.L.,
RA Kelley M.L., Lewis K.E., Ren H., Sheppard P.O., Storey H.M., Waggie K.S.,
RA Wolf A.C., Yao L.Y., Webster P.J.;
RT "A glycoprotein hormone expressed in corticotrophs exhibits unique binding
RT properties on thyroid-stimulating hormone receptor.";
RL Mol. Endocrinol. 20:414-425(2006).
CC -!- FUNCTION: Functions as a heterodimeric glycoprotein hormone with GPHA2
CC able to bind and activate the thyroid-stimulating hormone receptor
CC (TSHR), leading to increased cAMP production. Plays a central role in
CC controlling thyroid cell metabolism. {ECO:0000250|UniProtKB:Q86YW7}.
CC -!- SUBUNIT: Heterodimer with GPHA2; this heterodimer interacts with
CC thyroid-stimulating hormone receptor (TSHR), and hence stimulates cAMP
CC production. {ECO:0000250|UniProtKB:Q86YW7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the anterior lobe of pituitary.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86YW7}.
CC -!- MISCELLANEOUS: Overexpression of Gphb5 results in proptosis, elevated
CC serum T4 levels and significantly reduced body weight.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK078727; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF467771; AAO33391.1; -; mRNA.
DR EMBL; AK078727; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25982.1; -.
DR RefSeq; NP_783575.2; NM_175644.3.
DR RefSeq; XP_017170513.1; XM_017315024.1.
DR AlphaFoldDB; Q812B2; -.
DR STRING; 10090.ENSMUSP00000061488; -.
DR GlyGen; Q812B2; 1 site.
DR PaxDb; Q812B2; -.
DR PRIDE; Q812B2; -.
DR Antibodypedia; 73167; 63 antibodies from 12 providers.
DR DNASU; 217674; -.
DR Ensembl; ENSMUST00000051079; ENSMUSP00000061488; ENSMUSG00000048982.
DR GeneID; 217674; -.
DR KEGG; mmu:217674; -.
DR UCSC; uc007nxd.1; mouse.
DR CTD; 122876; -.
DR MGI; MGI:2156540; Gphb5.
DR VEuPathDB; HostDB:ENSMUSG00000048982; -.
DR eggNOG; ENOG502RZ3V; Eukaryota.
DR GeneTree; ENSGT00730000111179; -.
DR HOGENOM; CLU_126319_2_1_1; -.
DR InParanoid; Q812B2; -.
DR OMA; MAVRCDC; -.
DR OrthoDB; 1362225at2759; -.
DR PhylomeDB; Q812B2; -.
DR TreeFam; TF332940; -.
DR Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 217674; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q812B2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q812B2; protein.
DR Bgee; ENSMUSG00000048982; Expressed in primary oocyte and 2 other tissues.
DR ExpressionAtlas; Q812B2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0031531; F:thyrotropin-releasing hormone receptor binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IMP:MGI.
DR CDD; cd00069; GHB_like; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR001545; Gonadotropin_bsu.
DR PANTHER; PTHR11515; PTHR11515; 1.
DR Pfam; PF00007; Cys_knot; 1.
DR SMART; SM00068; GHB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..130
FT /note="Glycoprotein hormone beta-5"
FT /id="PRO_0000011762"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..84
FT /evidence="ECO:0000250"
FT DISULFID 50..99
FT /evidence="ECO:0000250"
FT DISULFID 60..115
FT /evidence="ECO:0000250"
FT DISULFID 64..117
FT /evidence="ECO:0000250"
FT DISULFID 120..127
FT /evidence="ECO:0000250"
SQ SEQUENCE 130 AA; 14249 MW; 8EFAF1EDF9514A65 CRC64;
MKLVYLVLGA VALLLLGGPD SVLSSSSGNL HTFVGCAVRE FTFMAKKPGC RGLRITTDAC
WGRCETWEKP ILEPPYIEAY HRVCTYNETR QVTVKLPNCA PGVDPFYTYP MAVRCDCGAC
STATTECETI
