ID   TSHB_ONCMY              Reviewed;         147 AA.
AC   P37240;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 77.
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   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-30.
RC   TISSUE=Pituitary;
RX   PubMed=8327483; DOI=10.1073/pnas.90.13.6052;
RA   Ito M., Koide Y., Takamatsu N., Kawauchi H., Shiba T.;
RT   "cDNA cloning of the beta subunit of teleost thyrotropin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6052-6055(1993).
CC   -!- FUNCTION: Indispensable for the control of thyroid structure and
CC       metabolism. May play some role in the biological processes of the
CC       immature fishes.
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   -!- TISSUE SPECIFICITY: Pituitary gland. Higher levels seen in immature
CC       fishes than the mature fishes.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; D14692; BAA03518.1; -; mRNA.
DR   PIR; A48194; A48194.
DR   RefSeq; NP_001118015.1; NM_001124543.1.
DR   AlphaFoldDB; P37240; -.
DR   SMR; P37240; -.
DR   Ensembl; ENSOMYT00000076225; ENSOMYP00000069997; ENSOMYG00000032448.
DR   GeneID; 100136289; -.
DR   KEGG; omy:100136289; -.
DR   CTD; 353223; -.
DR   GeneTree; ENSGT00940000158152; -.
DR   OrthoDB; 1362225at2759; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:8327483"
FT   CHAIN           21..147
FT                   /note="Thyrotropin subunit beta"
FT                   /id="PRO_0000011759"
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..127
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   147 AA;  16440 MW;  0F1642BA9FCA35BA CRC64;
     MELSVAMYGL LCLLFSQAVP MCVPTDYTLY EERRECDFCV AINTTICMGF CYSRDSNMKE
     LAGPRFLIQR GCTYDQVEYR TVILPGCPLH ANPLFTYPVA LSCHCGTCNT DSDECAHKAS
     SGDGARCSKP LRHIYPYPGL NSYIHPN