ID   TSHB_PHOSU              Reviewed;         101 AA.
AC   Q62590;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 70.
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: Fragment;
GN   Name=TSHB;
OS   Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Phodopus.
OX   NCBI_TaxID=10044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=8612518; DOI=10.1210/endo.137.5.8612518;
RA   Bockmann J., Boeckers T.M., Vennemann B., Niklowitz P., Mueller J.,
RA   Wittkowski W., Sabel B., Kreutz M.R.;
RT   "Short photoperiod-dependent down-regulation of thyrotropin-alpha and -beta
RT   in hamster pars tuberalis-specific cells is prevented by pinealectomy.";
RL   Endocrinology 137:1804-1813(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; X90777; CAA62298.1; -; mRNA.
DR   AlphaFoldDB; Q62590; -.
DR   SMR; Q62590; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; Secreted.
FT   CHAIN           <1..101
FT                   /note="Thyrotropin subunit beta"
FT                   /id="PRO_0000149044"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..78
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   101 AA;  11353 MW;  E5AB4616FC4AE6FF CRC64;
     YCLTINTTIC AGYCMTRDIN GKLFLPKSAL SQDVCTYRDF TYRTVEIPGC PHHVAPYFSY
     PVAMSCKCGK CNTDYSDCIH EAVKTNYCTK PQTFYLGGFS V