ID   GLHA_LITCT              Reviewed;          97 AA.
AC   P80051;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
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;
GN   Name=cga;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1730225; DOI=10.1111/j.1432-1033.1992.tb19845.x;
RA   Hayashi H., Hayashi T., Hanaoka Y.;
RT   "Amphibian lutropin and follitropin from the bullfrog Rana catesbeiana.
RT   Complete amino acid sequence of the alpha subunit.";
RL   Eur. J. Biochem. 203:185-191(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-28.
RX   PubMed=1701134; DOI=10.1210/endo-127-6-2985;
RA   Bergert E.R., Madden B., McCormick D.J., Papkoff H., Ryan R.J.;
RT   "The antigenic structure of the human glycoprotein hormone alpha-subunit:
RT   II. Cross-species comparisons.";
RL   Endocrinology 127:2985-2989(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: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   PIR; S20287; S20287.
DR   AlphaFoldDB; P80051; -.
DR   SMR; P80051; -.
DR   GlyConnect; 196; 3 N-Linked glycans (2 sites).
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.
FT   CHAIN           1..97
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000149032"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT                   /id="CAR_000040"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT                   /id="CAR_000041"
FT   DISULFID        11..36
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        14..65
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        33..87
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        37..89
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        64..92
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
SQ   SEQUENCE   97 AA;  11036 MW;  1B7D72AA1773A107 CRC64;
     FPDDNFLTPG CPECRLKENL RFSNMGIGRI YQCSGCCYSR AYPTPMRSKK TMLVPKNITS
     EAKCCVAKTQ YRVTVMDNVK IENHTACHCS TCLYHKS