GLHA_ICTPU
ID GLHA_ICTPU Reviewed; 116 AA.
AC Q9YGP3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Kansas;
RX PubMed=9284560;
RA Liu Z., Li P., Argue B.J., Dunham R.A.;
RT "Gonadotropin alpha-subunit glycoprotein from channel catfish (Ictalurus
RT punctatus) and its expression during hormone-induced ovulation.";
RL Mol. Mar. Biol. Biotechnol. 6:217-227(1997).
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; AF112190; AAD18004.1; -; mRNA.
DR RefSeq; NP_001187007.1; NM_001200078.1.
DR AlphaFoldDB; Q9YGP3; -.
DR SMR; Q9YGP3; -.
DR STRING; 7998.ENSIPUP00000008246; -.
DR GeneID; 100304479; -.
DR KEGG; ipu:100304479; -.
DR CTD; 1081; -.
DR OrthoDB; 1430707at2759; -.
DR Proteomes; UP000221080; Chromosome 9.
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; IPI:AgBase.
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_0000011667"
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; 13089 MW; C87498B2515B39BA CRC64;
MILILKYTGA TIILLSVLIE IGQLFPNNDF GCEECKLKEN NIFSKPGAPV YQCMGCCFSR
AYPTPLRSEK TMLVPKNITS EATCCVAKEV KRVIVNDVKL MNHTDCHCST CYYHKF
