ID   TSHB_ANGAN              Reviewed;         147 AA.
AC   Q08127;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 76.
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 anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8044698;
RA   Salmon C., Marchelidon J., Fontaine Y.-A., Huet J.-C., Querat B.;
RT   "Cloning and sequence of thyrotropin beta subunit of a teleost fish: the
RT   eel (Anguilla anguilla L.).";
RL   C. R. Acad. Sci. III, Sci. Vie 316:749-753(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-43.
RX   PubMed=1933511;
RA   Marchelidon J., Huet J.-C., Pernollet J.-C., Salmon C., Fontaine Y.-A.;
RT   "Purification and characterization of presumed thyrotropic hormone subunits
RT   of a teleost fish, the eel (Anguilla anguilla).";
RL   C. R. Acad. Sci. III, Sci. Vie 313:253-258(1991).
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   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; X73493; CAA51908.1; -; mRNA.
DR   PIR; S34148; S34148.
DR   AlphaFoldDB; Q08127; -.
DR   SMR; Q08127; -.
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:1933511"
FT   CHAIN           21..147
FT                   /note="Thyrotropin subunit beta"
FT                   /id="PRO_0000011757"
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;  16156 MW;  4286255473759DDB CRC64;
     MRVVLLASAV LCLLAGQVLS ICSPVDYTLY VEKPECDFCV AINTTICMGF CYSLDPNVVG
     PAVKRLVVQR GCTYQAVEYR TAELPGCPPH VDPRFSYPVA LHCTCRACDP ARDECTHRAS
     ADGDRCSKPL LLHMHAYPGQ SNYIQTL