ID   GLHA_CLAGA              Reviewed;         116 AA.
AC   P53542;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 69.
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   Clarias gariepinus (North African catfish) (Silurus gariepinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Clariidae; Clarias.
OX   NCBI_TaxID=13013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Rebers F.E.M., Tensen C.P., Schulz R.W., Goos H.J.T., Bogerd J.;
RL   Submitted (MAY-1996) 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; X97760; CAA66358.1; -; mRNA.
DR   AlphaFoldDB; P53542; -.
DR   SMR; P53542; -.
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:0046982; F:protein heterodimerization 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:0000250"
FT   CHAIN           25..116
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000011661"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        32..56
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        35..85
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        53..106
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        57..108
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        84..111
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
SQ   SEQUENCE   116 AA;  13060 MW;  C38F1E9FBC5D1DC4 CRC64;
     MTLIPKYTGA TILLLCVLIE IGQLYPNNDF GCEECKLKEN NIFSKPGAPV YQCMGCCFSR
     AYPTPLRSKK TMLVPKNITS EATCCVAKEV KRVIVNDVKL VNHTDCHCST CYYHKF