ID   GLHA_NIPNI              Reviewed;         120 AA.
AC   Q8JIE9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 58.
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   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kawasaki D., Kanai M., Aotsuka T., Ishii S.;
RT   "Cloning of the genes for the pituitary glycoprotein hormone alpha subunit
RT   and follicle-stimulating hormone beta subunit in the Japanese crested ibis,
RT   Nipponia nippon.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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; AB089503; BAC07315.1; -; Genomic_DNA.
DR   RefSeq; XP_009473874.1; XM_009475599.1.
DR   AlphaFoldDB; Q8JIE9; -.
DR   SMR; Q8JIE9; -.
DR   STRING; 128390.XP_009473874.1; -.
DR   GeneID; 104021959; -.
DR   KEGG; nni:104021959; -.
DR   CTD; 1081; -.
DR   eggNOG; ENOG502S1PK; Eukaryota.
DR   OrthoDB; 1430707at2759; -.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..120
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000042880"
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;  13404 MW;  DAD84619B9BDAFD2 CRC64;
     MGCYGKYAAV TLTILSVFLH LLHAFPDGEF LMQGCPECKL GENRFFSKPG APIYQCTGCC
     FSRAYPTPMR SKKTMLVPKN ITSEATCCVA KAFTKITLKD NVKIENHTDC HCSTCYYHKS