ID   GLHA_HYPMO              Reviewed;         118 AA.
AC   P37037;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, 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;
OS   Hypophthalmichthys molitrix (Silver carp) (Leuciscus molitrix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Xenocyprididae; Xenocypridinae; Hypophthalmichthys.
OX   NCBI_TaxID=13095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Pituitary;
RX   PubMed=2332148; DOI=10.1016/0016-6480(90)90043-l;
RA   Chang Y.S., Huang C.J., Huang F.-L., Liu C.S., Lo T.-B.;
RT   "Purification, characterization, and molecular cloning of gonadotropin
RT   subunits of silver carp (Hypophthalmichthys molitrix).";
RL   Gen. Comp. Endocrinol. 78:23-33(1990).
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   PIR; A60626; A60626.
DR   AlphaFoldDB; P37037; -.
DR   SMR; P37037; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..118
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000011664"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        34..58
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        37..87
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        55..108
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        59..110
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        86..113
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
SQ   SEQUENCE   118 AA;  13435 MW;  54F3297F7A4074FF CRC64;
     MFWTRYAGAS ILLFLMLIHL GQVYPRNDIT NFGCEECKLK ENNIFSKPGA PVYQCMGCCF
     SRAYPTPLRS KKTMLVPKNI TSEATCCVAK EVKRVLVNDV KLVNHTDCHC STCYYHKS