ID   TSHB_CANLF              Reviewed;         138 AA.
AC   P54828;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Kania S.A., Frank L.A.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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; U51644; AAA97410.1; -; mRNA.
DR   RefSeq; NP_001003290.1; NM_001003290.1.
DR   AlphaFoldDB; P54828; -.
DR   SMR; P54828; -.
DR   STRING; 9615.ENSCAFP00000014272; -.
DR   PaxDb; P54828; -.
DR   GeneID; 403973; -.
DR   KEGG; cfa:403973; -.
DR   CTD; 7252; -.
DR   eggNOG; ENOG502S2JW; Eukaryota.
DR   InParanoid; P54828; -.
DR   Proteomes; UP000002254; Unplaced.
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: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                   /evidence="ECO:0000250"
FT   CHAIN           21..132
FT                   /note="Thyrotropin subunit beta"
FT                   /id="PRO_0000011742"
FT   PROPEP          133..138
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011743"
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;  15666 MW;  A3298FFDDF6A005F CRC64;
     MTAIYLMSML FGLACGQAMS FCFPTEYTMH VERKECAYCL TINTTICAGY CMTRDINGKL
     FLPKYALSQD VCTYRDFMYK TVEIPGCPRH VTPYFSYPVA VSCKCGKCNT DYSDCIHEAI
     KTNYCTKPQK SYVVGFSI