ID   TSHB_FELCA              Reviewed;         138 AA.
AC   Q52R90;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 65.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16122898; DOI=10.1016/j.domaniend.2005.07.002;
RA   Rayalam S., Eizenstat L.D., Hoenig M., Ferguson D.C.;
RT   "Cloning and sequencing of feline thyrotropin (fTSH): heterodimeric and
RT   yoked constructs.";
RL   Domest. Anim. Endocrinol. 30:203-217(2006).
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; AY972824; AAX85431.1; -; Genomic_DNA.
DR   RefSeq; NP_001041480.1; NM_001048015.1.
DR   AlphaFoldDB; Q52R90; -.
DR   SMR; Q52R90; -.
DR   STRING; 9685.ENSFCAP00000009656; -.
DR   GeneID; 554350; -.
DR   KEGG; fca:554350; -.
DR   CTD; 7252; -.
DR   eggNOG; ENOG502S2JW; Eukaryota.
DR   InParanoid; Q52R90; -.
DR   Proteomes; UP000011712; 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   3: Inferred from homology;
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_0000042883"
FT   PROPEP          133..138
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042884"
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;  15483 MW;  4EEC13E98C33E542 CRC64;
     MTAIYLMSVL FGLACGQAMS FCFPTEYMMH VERKECAYCL TINTTICAGY CMTRDINGKL
     FLPKYALSQD VCTYRDFLYK TVEIPGCPHH VTPYFSYPVA VSCKCGKCNT DYSDCIHEAI
     KTNDCTKPQK SDVVGVSI