TSHB_PIG
ID TSHB_PIG Reviewed; 138 AA.
AC P01224;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 117.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2473932; DOI=10.1016/0303-7207(89)90097-x;
RA Hirai T., Takikawa H., Kato Y.;
RT "Molecular cloning of cDNAs for precursors of porcine pituitary
RT glycoprotein hormone common alpha-subunit and of thyroid stimulating
RT hormone beta-subunit.";
RL Mol. Cell. Endocrinol. 63:209-217(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Meishan; TISSUE=Pituitary;
RX PubMed=8880412; DOI=10.2527/1996.7492104x;
RA Li M.D., Matteri R.L., Macdonald G.J., Wise T.H., Ford J.J.;
RT "Overexpression of beta-subunit of thyroid-stimulating hormone in Meishan
RT swine identified by differential display.";
RL J. Anim. Sci. 74:2104-2111(1996).
RN [3]
RP PROTEIN SEQUENCE OF 21-132.
RX PubMed=1245181; DOI=10.1111/j.1432-1033.1976.tb10006.x;
RA Maghuin-Rogister G., Hennen G., Closset J., Kopeyan C.;
RT "Porcine thyrotropin. The amino-acid sequence of the alpha and beta
RT subunits.";
RL Eur. J. Biochem. 61:157-163(1976).
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; U39816; AAA93182.1; -; mRNA.
DR PIR; B30339; TTPGB.
DR RefSeq; NP_999533.1; NM_214368.2.
DR AlphaFoldDB; P01224; -.
DR SMR; P01224; -.
DR STRING; 9823.ENSSSCP00000007199; -.
DR iPTMnet; P01224; -.
DR PaxDb; P01224; -.
DR Ensembl; ENSSSCT00025023082; ENSSSCP00025009629; ENSSSCG00025017097.
DR Ensembl; ENSSSCT00035056694; ENSSSCP00035022806; ENSSSCG00035042656.
DR Ensembl; ENSSSCT00040084814; ENSSSCP00040037026; ENSSSCG00040062231.
DR Ensembl; ENSSSCT00050059083; ENSSSCP00050025352; ENSSSCG00050043418.
DR Ensembl; ENSSSCT00055026937; ENSSSCP00055021413; ENSSSCG00055013684.
DR Ensembl; ENSSSCT00060101618; ENSSSCP00060044142; ENSSSCG00060074274.
DR Ensembl; ENSSSCT00070008652; ENSSSCP00070007126; ENSSSCG00070004588.
DR GeneID; 397658; -.
DR KEGG; ssc:397658; -.
DR CTD; 7252; -.
DR eggNOG; ENOG502S2JW; Eukaryota.
DR InParanoid; P01224; -.
DR OrthoDB; 1362225at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 4.
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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1245181"
FT CHAIN 21..132
FT /note="Thyrotropin subunit beta"
FT /id="PRO_0000011752"
FT PROPEP 133..138
FT /id="PRO_0000011753"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1245181"
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"
FT CONFLICT 42..44
FT /note="INT -> VNS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15761 MW; C75AE4326DAD0377 CRC64;
MTAIFLMSML FGLACGQAMS FCIPTEYMMH VERKECAYCL TINTTICAGY CMTRDFNGKL
FLPKYALSQD VCTYRDFMYK TVEIPGCPHH VTPYFSYPVA ISCKCGKCNT DYSDCIHEAI
KTNYCTKPQK SYVLEFSI
