ID   GLHA_MORSA              Reviewed;         117 AA.
AC   Q91119;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Glycoprotein hormones alpha chain;
DE   AltName: Full=GTH-alpha;
DE   AltName: Full=Gonadotropin alpha chain;
DE   Flags: Precursor;
GN   Name=cga;
OS   Morone saxatilis (Striped bass) (Perca saxatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Morone.
OX   NCBI_TaxID=34816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=8546811; DOI=10.1677/jme.0.0150023;
RA   Hassin S., Elizur A., Zohar Y.;
RT   "Molecular cloning and sequence analysis of striped bass (Morone saxatilis)
RT   gonadotrophin-I and -II subunits.";
RL   J. Mol. Endocrinol. 15:23-35(1995).
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; L35071; AAB66489.1; -; mRNA.
DR   PIR; I50992; I50992.
DR   AlphaFoldDB; Q91119; -.
DR   SMR; Q91119; -.
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..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..117
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000011668"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        34..57
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        37..86
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        54..107
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        58..109
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        85..112
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
SQ   SEQUENCE   117 AA;  13066 MW;  62CCD867AE9A8C5D CRC64;
     MGSVKSAGLS LLLLSFILYV VDSYPSMDLS NMGCEECTLR KNSVFSRDRP VYQCMGCCFS
     RAYPTPLKAM KTMTIPKNIT SEATCCVAKH SYETEVAGIK VRNHTDCHCS TCYFHKI