ID   GLHA_THUOB              Reviewed;          94 AA.
AC   P37204;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
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;
GN   Name=cga;
OS   Thunnus obesus (Bigeye tuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX   NCBI_TaxID=8241;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Pituitary;
RX   PubMed=8138353; DOI=10.1111/j.1399-3011.1994.tb00377.x;
RA   Okada T., Kawazoe I., Kimura S., Sasamoto Y., Aida K., Kawauchi H.;
RT   "Purification and characterization of gonadotropin I and II from pituitary
RT   glands of tuna (Thunnus obesus).";
RL   Int. J. Pept. Protein Res. 43:69-80(1994).
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:0000269|PubMed:8138353}.
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:0000269|PubMed:8138353}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8138353}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P37204; -.
DR   SMR; P37204; -.
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..94
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000149034"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        11..34
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        14..63
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        31..84
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        35..86
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        62..89
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
SQ   SEQUENCE   94 AA;  10665 MW;  29CD7C06F5D4BD0E CRC64;
     YPNVDLSNMG CEECTLKKNN VFSRDRPIYQ CMGCCFSRAF PTPLKAMKTM TIPKNITSEA
     TCCVAKHSYE TEVAGIRVRN HTDCHCSTCY FHKS