ID   GLHA_CAPHI              Reviewed;         120 AA.
AC   Q8WMW8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 63.
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   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li L.Q., Zhang Z., Guan G.H.;
RT   "Nucleotide sequence of cloned cDNA for alpha subunit of goat.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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; AF464001; AAL68841.1; -; mRNA.
DR   RefSeq; NP_001272613.1; NM_001285684.1.
DR   AlphaFoldDB; Q8WMW8; -.
DR   SMR; Q8WMW8; -.
DR   STRING; 9925.ENSCHIP00000019012; -.
DR   GeneID; 100860817; -.
DR   KEGG; chx:100860817; -.
DR   CTD; 1081; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
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   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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..120
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000042874"
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"
SQ   SEQUENCE   120 AA;  13588 MW;  08020177D8634FC3 CRC64;
     MDYYRKYAAV ILAVLSLFLQ ILHSFPDGEF MMQGCPECKL KENKYFSKPD APIYQCMGCC
     FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVTG NVRVENHTDC HCSTCYYHKS