ID   GLHA_COTJA              Reviewed;         120 AA.
AC   P68242; P37035;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
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   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=7515015; DOI=10.1006/gcen.1994.1040;
RA   Ando H., Ishii S.;
RT   "Molecular cloning of complementary deoxyribonucleic acids for the
RT   pituitary glycoprotein hormone alpha-subunit and luteinizing hormone beta-
RT   subunit precursor molecules of Japanese quail (Coturnix coturnix
RT   japonica).";
RL   Gen. Comp. Endocrinol. 93:357-368(1994).
CC   -!- FUNCTION: Shared alpha chain of heterodimeric glycoprotein hormones.
CC       These hormones bind specific receptors on target cells that in turn
CC       activate downstream signaling pathways. {ECO:0000250|UniProtKB:P01215}.
CC   -!- SUBUNIT: Heterodimer. Glycoprotein hormones are heterodimers composed
CC       of a common alpha chain described here and a unique beta chain which
CC       confers their biological specificity to the different hormones.
CC       {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; S70833; AAB30866.1; -; mRNA.
DR   RefSeq; XP_015714368.1; XM_015858882.1.
DR   AlphaFoldDB; P68242; -.
DR   SMR; P68242; -.
DR   Ensembl; ENSCJPT00005007202; ENSCJPP00005004271; ENSCJPG00005004279.
DR   Ensembl; ENSCJPT00005007204; ENSCJPP00005004273; ENSCJPG00005004279.
DR   Ensembl; ENSCJPT00005007205; ENSCJPP00005004274; ENSCJPG00005004279.
DR   GeneID; 107311949; -.
DR   KEGG; cjo:107311949; -.
DR   CTD; 1081; -.
DR   GeneTree; ENSGT00390000012242; -.
DR   OrthoDB; 1430707at2759; -.
DR   Proteomes; UP000694412; Chromosome 3.
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:0000255"
FT   CHAIN           25..120
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000011657"
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;  13591 MW;  F4662BA0CB6005EB CRC64;
     MDCYRKYAAV TLTILSVFLH LLHTFPDGEF LMQGCPECKL GENRFFSKPG APIYQCTGCC
     FSRAYPTPMR SKKTMLVPKN ITSEATCCVA KAFTKITLKD NVKIENHTDC HCSTCYYHKS