TSHB_BOVIN
ID TSHB_BOVIN Reviewed; 138 AA.
AC P01223;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6325416; DOI=10.1016/s0021-9258(17)42949-8;
RA Maurer R.A., Croyle M.L., Donelson J.E.;
RT "The sequence of a cloned cDNA for the beta subunit of bovine thyrotropin
RT predicts a protein containing both NH2- and COOH-terminal extensions.";
RL J. Biol. Chem. 259:5024-5027(1984).
RN [2]
RP PROTEIN SEQUENCE OF 21-132.
RX PubMed=5101174; DOI=10.1016/s0021-9258(18)62404-4;
RA Liao T.-H., Pierce J.G.;
RT "The primary structure of bovine thyrotropin. II. The amino acid sequences
RT of the reduced, S-carboxymethyl alpha and beta chains.";
RL J. Biol. Chem. 246:850-865(1971).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=5101173; DOI=10.1016/s0021-9258(18)62403-2;
RA Shome B., Liao T.-H., Howard S.M., Pierce J.G.;
RT "The primary structure of bovine thyrotropin. I. Isolation and partial
RT sequences of cyanogen bromide and tryptic peptides.";
RL J. Biol. Chem. 246:833-849(1971).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=8670056; DOI=10.1042/bj3140449;
RA Fairlie W.D., Stanton P.G., Hearn T.W.;
RT "The disulphide bond structure of thyroid-stimulating hormone beta-
RT subunit.";
RL Biochem. J. 314:449-455(1996).
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; K01939; AAA30796.1; -; mRNA.
DR PIR; I45985; TTBOB.
DR RefSeq; NP_776630.1; NM_174205.1.
DR RefSeq; XP_005204062.1; XM_005204005.3.
DR AlphaFoldDB; P01223; -.
DR SMR; P01223; -.
DR STRING; 9913.ENSBTAP00000008264; -.
DR BindingDB; P01223; -.
DR ChEMBL; CHEMBL3988581; -.
DR GlyConnect; 601; 37 N-Linked glycans.
DR PaxDb; P01223; -.
DR Ensembl; ENSBTAT00000008264; ENSBTAP00000008264; ENSBTAG00000006295.
DR GeneID; 281552; -.
DR KEGG; bta:281552; -.
DR CTD; 7252; -.
DR VEuPathDB; HostDB:ENSBTAG00000006295; -.
DR VGNC; VGNC:36418; TSHB.
DR eggNOG; ENOG502S2JW; Eukaryota.
DR GeneTree; ENSGT00940000158152; -.
DR HOGENOM; CLU_126319_0_2_1; -.
DR InParanoid; P01223; -.
DR OMA; PTEYMMH; -.
DR OrthoDB; 1362225at2759; -.
DR TreeFam; TF332940; -.
DR Reactome; R-BTA-209822; Glycoprotein hormones.
DR Reactome; R-BTA-209968; Thyroxine biosynthesis.
DR Reactome; R-BTA-375281; Hormone ligand-binding receptors.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000006295; Expressed in adenohypophysis and 61 other tissues.
DR ExpressionAtlas; P01223; baseline.
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; IMP:AgBase.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:5101174"
FT CHAIN 21..132
FT /note="Thyrotropin subunit beta"
FT /id="PRO_0000011740"
FT PROPEP 133..138
FT /id="PRO_0000011741"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 22..72
FT /evidence="ECO:0000269|PubMed:8670056"
FT DISULFID 36..87
FT /evidence="ECO:0000269|PubMed:8670056"
FT DISULFID 39..125
FT /evidence="ECO:0000269|PubMed:8670056"
FT DISULFID 47..103
FT /evidence="ECO:0000269|PubMed:8670056"
FT DISULFID 51..105
FT /evidence="ECO:0000269|PubMed:8670056"
FT DISULFID 108..115
FT /evidence="ECO:0000269|PubMed:8670056"
SQ SEQUENCE 138 AA; 15624 MW; 42D783B7C0E2EB98 CRC64;
MTATFLMSMI FGLACGQAMS FCIPTEYMMH VERKECAYCL TINTTVCAGY CMTRDVNGKL
FLPKYALSQD VCTYRDFMYK TAEIPGCPRH VTPYFSYPVA ISCKCGKCNT DYSDCIHEAI
KTNYCTKPQK SYMVGFSI
