ID   TSHB_ANGJA              Reviewed;         147 AA.
AC   Q7ZZV4;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 53.
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   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Han Y.-S., Liao I.-C., Tzeng W.-N., Huang Y.-S., Yu J.Y.-L.;
RT   "Molecular cloning of the genomic DNA and cDNA encoding thyroid stimulating
RT   hormone beta subunit of the Japanese eel and its gene expression.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Nagae M., Qu X.C., Kazeto Y., Ijiri S., Ito F., Adachi S., Yamauchi K.;
RT   "Molecular cloning of Japanese eel TSH beta.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AY158008; AAO17791.1; -; Genomic_DNA.
DR   EMBL; AB175833; BAD14300.1; -; mRNA.
DR   AlphaFoldDB; Q7ZZV4; -.
DR   SMR; Q7ZZV4; -.
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; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..147
FT                   /note="Thyrotropin subunit beta"
FT                   /id="PRO_0000011758"
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..126
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;  16088 MW;  5EF2E159E1BCCDDB CRC64;
     MRVVLLASGV LCLLAGQVLS ICSPVDYTLY VEKPECDFCV AINTTICMGF CYSLDPNVVG
     PAVKRLAVQR GCTYQAVEYR TAELPGCPPH VDPRFSYPVA LHCTCRACDP ARDECTHRAS
     ADGDRCSKPL LLHMHAYPGQ SNHIQTL