ID GLHA_MONDO Reviewed; 120 AA.
AC Q6YNX4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 101.
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;
DE Flags: Precursor;
GN Name=CGA;
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Kacsoh B.;
RT "Cloning and characterization of the cDNA encoding the anterior pituitary
RT glycoprotein hormone common alpha subunit in the marsupial, Monodelphis
RT domestica.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein
CC hormones thyrotropin/thyroid stimulating hormone/TSH,
CC lutropin/luteinizing hormone/LH and follitropin/follicle stimulating
CC hormone/FSH. These hormones bind specific receptors on target cells
CC that in turn activate downstream signaling pathways.
CC {ECO:0000250|UniProtKB:P01215}.
CC -!- SUBUNIT: Heterodimer. The active hormones thyrotropin, lutropin and
CC follitropin are heterodimers composed of CGA, a common alpha chain
CC described here and a unique beta chain which confers their biological
CC specificity to the hormones: TSHB for thyrotropin, LHB for lutropin and
CC FSHB for follitropin. {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 EMBL; AY048590; AAL05939.1; -; mRNA.
DR RefSeq; NP_001028162.1; NM_001032990.1.
DR RefSeq; XP_007483980.1; XM_007483918.2.
DR AlphaFoldDB; Q6YNX4; -.
DR SMR; Q6YNX4; -.
DR STRING; 13616.ENSMODP00000056565; -.
DR GlyCosmos; Q6YNX4; 2 sites, No reported glycans.
DR Ensembl; ENSMODT00000023249.3; ENSMODP00000022844.1; ENSMODG00000018321.3.
DR GeneID; 554198; -.
DR KEGG; mdo:554198; -.
DR CTD; 1081; -.
DR eggNOG; ENOG502S1PK; Eukaryota.
DR GeneTree; ENSGT00390000012242; -.
DR HOGENOM; CLU_148106_0_0_1; -.
DR InParanoid; Q6YNX4; -.
DR OrthoDB; 4182331at2759; -.
DR TreeFam; TF332733; -.
DR Proteomes; UP000002280; Chromosome 2.
DR Bgee; ENSMODG00000018321; Expressed in ovary and 9 other cell types or tissues.
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 GO; GO:0006590; P:thyroid hormone generation; IBA:GO_Central.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000476; Glyco_hormone.
DR PANTHER; PTHR11509; GLYCOPROTEIN HORMONE ALPHA CHAIN; 1.
DR PANTHER; PTHR11509:SF0; GLYCOPROTEIN HORMONES ALPHA CHAIN; 1.
DR Pfam; PF00236; Hormone_6; 1.
DR PRINTS; PR00274; GLYCOHORMONE.
DR SMART; SM00067; GHA; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000042877"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 35..59
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 38..88
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 56..110
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 60..112
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 87..115
FT /evidence="ECO:0000250|UniProtKB:P01215"
SQ SEQUENCE 120 AA; 13513 MW; 837F323310E280CB CRC64;
MDYYRKYAAV ILATLSVFLH ILHSFPDGEF IMQGCPECKL KENKYFSKLG APIYQCMGCC
FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVMG NAKVENHTEC HCSTCYYHKS
//
