ID   GLHA_FUNHE              Reviewed;         125 AA.
AC   P47744;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Glycoprotein hormones alpha chain;
DE   AltName: Full=GTH-alpha;
DE   AltName: Full=Gonadotropin alpha chain;
DE   Flags: Precursor;
GN   Name=cga; Synonyms=gth;
OS   Fundulus heteroclitus (Killifish) (Mummichog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX   NCBI_TaxID=8078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Lin Y.-P., Limesand S.W., Price D.A., Wallace R.A.;
RL   Submitted (AUG-1994) 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. Involved in gametogenesis and
CC       steroidogenesis. {ECO:0000250|UniProtKB:P37204}.
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:P37204}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P37204}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; U12923; AAB60605.1; -; mRNA.
DR   RefSeq; XP_012723236.1; XM_012867782.1.
DR   AlphaFoldDB; P47744; -.
DR   SMR; P47744; -.
DR   STRING; 8078.ENSFHEP00000011550; -.
DR   Ensembl; ENSFHET00000018557; ENSFHEP00000011542; ENSFHEG00000013002.
DR   Ensembl; ENSFHET00000031636; ENSFHEP00000011550; ENSFHEG00000013002.
DR   GeneID; 105929862; -.
DR   CTD; 1081; -.
DR   GeneTree; ENSGT00390000012242; -.
DR   OrthoDB; 1430707at2759; -.
DR   Proteomes; UP000265000; 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   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; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..125
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000011663"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        41..64
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        44..93
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        61..114
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        65..116
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        92..119
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   VARIANT         72
FT                   /note="T -> M"
FT   VARIANT         95
FT                   /note="A -> P"
SQ   SEQUENCE   125 AA;  13804 MW;  0247A8D885601868 CRC64;
     MVSAVTTMGC MKAAGVSLLL LYFLLNAADS HPNFDSSSMA CGECSLGLNR LFSRDRPLYQ
     CMGCCFSRAY PTPQTAIQTM AIPKNITSEA KCCVAKHSYE TKVDDITVRN HTECHCSTCY
     YHKLI