GLHA_HORSE
ID GLHA_HORSE Reviewed; 120 AA.
AC P01220;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glycoprotein hormones alpha chain;
DE AltName: Full=Anterior pituitary glycoprotein hormones common subunit alpha;
DE AltName: Full=Follicle-stimulating hormone alpha chain;
DE Short=FSH-alpha;
DE AltName: Full=Follitropin alpha chain;
DE AltName: Full=Luteinizing hormone alpha chain;
DE Short=LSH-alpha;
DE AltName: Full=Lutropin alpha chain;
DE AltName: Full=Thyroid-stimulating hormone alpha chain;
DE Short=TSH-alpha;
DE AltName: Full=Thyrotropin alpha chain;
DE Flags: Precursor;
GN Name=CGA;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hokkaido; TISSUE=Placenta;
RA Min K., Shinozaki M., Miyazawa K., Nishimura R., Sasaki N., Shiota K.,
RA Ogawa T.;
RT "Nucleotide sequence of eCG alpha-subunit cDNA and its expression in the
RT equine placenta.";
RL J. Reprod. Dev. 40:301-305(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-120.
RX PubMed=3437252; DOI=10.1677/joe.0.1150341;
RA Stewart F., Thomson J.A., Leigh S.E.A., Warwick J.M.;
RT "Nucleotide (cDNA) sequence encoding the horse gonadotrophin alpha-
RT subunit.";
RL J. Endocrinol. 115:341-346(1987).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 25-120.
RA Moore W.T. Jr., Ward D.N., Burleigh B.D.;
RT "Primary structure of pregnant mare serum gonadotropin alpha subunit.";
RL Fed. Proc. 38:462-462(1979).
RN [4]
RP PROTEIN SEQUENCE OF 39-120.
RX PubMed=670201; DOI=10.1016/s0021-9258(17)30378-2;
RA Rathnam P., Fujiki Y., Landefeld T.D., Saxena B.B.;
RT "Isolation and amino acid sequence of the alpha-subunit of follicle-
RT stimulating hormone from equine pituitary glands.";
RL J. Biol. Chem. 253:5355-5362(1978).
CC -!- FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein
CC hormones thyrotropin/thyroid stimulating hormone/TSH,
CC lutropin/luteinizing hormone/LH and follitropin/follicle stimulating
CC hormone/FSH. These hormones bind specific receptors on target cells
CC that in turn activate downstream signaling pathways.
CC {ECO:0000250|UniProtKB:P01215}.
CC -!- SUBUNIT: Heterodimer. The active hormones thyrotropin, lutropin and
CC follitropin are heterodimers composed of CGA, a common alpha chain
CC described here and a unique beta chain which confers their biological
CC specificity to the hormones: TSHB for thyrotropin, LHB for lutropin and
CC FSHB for follitropin. {ECO:0000250|UniProtKB:P01215}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01215}.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; AB000200; BAA19068.1; -; mRNA.
DR EMBL; M27462; AAA57252.1; -; mRNA.
DR PIR; A28576; TTHOA.
DR RefSeq; NP_001093233.1; NM_001099763.1.
DR RefSeq; XP_005596847.1; XM_005596790.2.
DR RefSeq; XP_005596848.1; XM_005596791.2.
DR AlphaFoldDB; P01220; -.
DR SMR; P01220; -.
DR STRING; 9796.ENSECAP00000034031; -.
DR GeneID; 100034174; -.
DR KEGG; ecb:100034174; -.
DR CTD; 1081; -.
DR InParanoid; P01220; -.
DR OrthoDB; 1430707at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016914; C:follicle-stimulating hormone complex; ISS:UniProtKB.
DR GO; GO:0016913; F:follicle-stimulating hormone activity; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0006590; P:thyroid hormone generation; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000476; Glyco_hormone.
DR PANTHER; PTHR11509; PTHR11509; 1.
DR Pfam; PF00236; Hormone_6; 1.
DR PRINTS; PR00274; GLYCOHORMONE.
DR SMART; SM00067; GHA; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00779; GLYCO_HORMONE_ALPHA_1; 1.
DR PROSITE; PS00780; GLYCO_HORMONE_ALPHA_2; 1.
DR PROSITE; PS50277; GLYCO_HORMONE_ALPHA_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011639"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 35..59
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 38..88
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 56..110
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 60..112
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 87..115
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT CONFLICT 43
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> M (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="I -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13809 MW; 8A633823F93ACFA6 CRC64;
MDYYRKHAAV ILATLSVFLH ILHSFPDGEF TTQDCPECKL RENKYFFKLG VPIYQCKGCC
FSRAYPTPAR SRKTMLVPKN ITSESTCCVA KAFIRVTVMG NIKLENHTQC YCSTCYHHKI
