ID   TSHB_MONDO              Reviewed;         138 AA.
AC   Q95J88;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 82.
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   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Kacsoh B.;
RT   "Cloning and characterization of the cDNA encoding pituitary thyroid
RT   stimulating hormone (TSH, thyrotropin) beta of the marsupial, Monodelphis
RT   domestica.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Indispensable for the control of thyroid structure and
CC       metabolism. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AY048589; AAL05938.1; -; mRNA.
DR   RefSeq; NP_001028146.1; NM_001032974.1.
DR   AlphaFoldDB; Q95J88; -.
DR   SMR; Q95J88; -.
DR   STRING; 13616.ENSMODP00000005917; -.
DR   GeneID; 503501; -.
DR   KEGG; mdo:503501; -.
DR   CTD; 7252; -.
DR   eggNOG; ENOG502S2JW; Eukaryota.
DR   InParanoid; Q95J88; -.
DR   OrthoDB; 1362225at2759; -.
DR   Proteomes; UP000002280; Unplaced.
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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..132
FT                   /note="Thyrotropin subunit beta"
FT                   /id="PRO_0000042869"
FT   PROPEP          133..138
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042870"
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;  15398 MW;  6DC6B2098B333FB1 CRC64;
     MTATFLMSLL FGLAFGQTMS LCVPTGYTMH IERRECAYCL TINTTICAGY CMTRDSNGKL
     FLPKSALSQD VCTYRDVIYR TVVMPGCPPH VIPYISYPVA VSCRCGKCNT DYIDCIHESV
     TTNYCTKPQK PYLVGFPV