TSHB_MOUSE
ID TSHB_MOUSE Reviewed; 138 AA.
AC P12656;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Thyrotropin subunit beta;
DE AltName: Full=Thyroid-stimulating hormone subunit beta;
DE Short=TSH-B;
DE Short=TSH-beta;
DE AltName: Full=Thyrotropin beta chain;
DE Flags: Precursor;
GN Name=Tshb;
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 [GENOMIC DNA].
RX PubMed=3349902; DOI=10.1089/dna.1988.7.17;
RA Gordon D.F., Wood W.M., Ridgway E.C.;
RT "Organization and nucleotide sequence of the gene encoding the beta-subunit
RT of murine thyrotropin.";
RL DNA 7:17-26(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2824501; DOI=10.1016/s0021-9258(18)49298-8;
RA Wolf O., Kourides I.A., Gurr J.A.;
RT "Expression of the gene for the beta subunit of mouse thyrotropin results
RT in multiple mRNAs differing in their 5'-untranslated regions.";
RL J. Biol. Chem. 262:16596-16603(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6207569; DOI=10.1016/b978-0-12-571140-1.50007-4;
RA Kourides I.A., Gurr J.A., Wolf O.;
RT "The regulation and organization of thyroid stimulating hormone genes.";
RL Recent Prog. Horm. Res. 40:79-120(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-8.
RC STRAIN=LAF1;
RX PubMed=2484718; DOI=10.1210/mend-1-12-875;
RA Wood W.M., Gordon D.F., Ridgway E.C.;
RT "Expression of the beta-subunit gene of murine thyrotropin results in
RT multiple messenger ribonucleic acid species which are generated by
RT alternative exon splicing.";
RL Mol. Endocrinol. 1:875-883(1987).
CC -!- FUNCTION: Indispensable for the control of thyroid structure and
CC metabolism.
CC -!- SUBUNIT: Heterodimer of a common alpha chain and a unique beta chain
CC which confers biological specificity to thyrotropin, lutropin,
CC follitropin and gonadotropin.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
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DR EMBL; M20537; AAA40494.1; -; Genomic_DNA.
DR EMBL; M20536; AAA40494.1; JOINED; Genomic_DNA.
DR EMBL; M22740; AAA40493.1; -; Genomic_DNA.
DR EMBL; M35719; AAA37307.1; -; mRNA.
DR EMBL; M35720; AAA37308.1; -; mRNA.
DR EMBL; M35721; AAA37309.1; -; mRNA.
DR EMBL; M35723; AAA37310.1; -; mRNA.
DR EMBL; M54943; AAA40492.1; -; mRNA.
DR CCDS; CCDS17689.1; -.
DR PIR; A29479; A29479.
DR AlphaFoldDB; P12656; -.
DR SMR; P12656; -.
DR STRING; 10090.ENSMUSP00000029450; -.
DR GlyGen; P12656; 1 site.
DR PaxDb; P12656; -.
DR PRIDE; P12656; -.
DR MGI; MGI:98848; Tshb.
DR eggNOG; ENOG502S2JW; Eukaryota.
DR InParanoid; P12656; -.
DR PhylomeDB; P12656; -.
DR Reactome; R-MMU-209822; Glycoprotein hormones.
DR Reactome; R-MMU-209968; Thyroxine biosynthesis.
DR Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR PRO; PR:P12656; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P12656; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 InterPro; IPR018245; Gonadotropin_bsu_CS.
DR PANTHER; PTHR11515; PTHR11515; 1.
DR Pfam; PF00007; Cys_knot; 1.
DR SMART; SM00068; GHB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1.
DR PROSITE; PS00689; GLYCO_HORMONE_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT CHAIN 21..132
FT /note="Thyrotropin subunit beta"
FT /id="PRO_0000011750"
FT PROPEP 133..138
FT /id="PRO_0000011751"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..72
FT /evidence="ECO:0000250"
FT DISULFID 36..87
FT /evidence="ECO:0000250"
FT DISULFID 39..125
FT /evidence="ECO:0000250"
FT DISULFID 47..103
FT /evidence="ECO:0000250"
FT DISULFID 51..105
FT /evidence="ECO:0000250"
FT DISULFID 108..115
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15373 MW; 44386FF3E17C5BEB CRC64;
MSAAVLLSVL FALACGQAAS FCIPTEYTMY VDRRECAYCL TINTTICAGY CMTRDINGKL
FLPKYALSQD VCTYRDFIYR TVEIPGCPHH VTPYFSFPVA VSCKCGKCNT DNSDCIHEAV
RTNYCTKPQS FYLGGFSV
