GLHA_RAT
ID GLHA_RAT Reviewed; 120 AA.
AC P11962; P70516;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 140.
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; Synonyms=Cga1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=6177696; DOI=10.1016/s0021-9258(18)34340-0;
RA Godine J.E., Chin W.W., Habener J.F.;
RT "Alpha subunit of rat pituitary glycoprotein hormones. Primary structure of
RT the precursor determined from the nucleotide sequence of cloned cDNAs.";
RL J. Biol. Chem. 257:8368-8371(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2467841; DOI=10.1016/0378-1119(88)90105-9;
RA Burnside J., Buckland P.R., Chin W.W.;
RT "Isolation and characterization of the gene encoding the alpha-subunit of
RT the rat pituitary glycoprotein hormones.";
RL Gene 70:67-74(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar Imamichi; TISSUE=Pituitary anterior lobe;
RA Kato Y., Ezashi T., Hirai T., Kato T.;
RT "Strain difference in nucleotide sequences of rat glycoprotein hormone
RT subunit cDNAs and gene fragment.";
RL Zool. Sci. 7:877-885(1990).
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; J00757; AAA97425.1; -; mRNA.
DR EMBL; M25543; AAB04669.1; -; Genomic_DNA.
DR EMBL; M22829; AAB04669.1; JOINED; Genomic_DNA.
DR EMBL; M25544; AAB04668.1; -; Genomic_DNA.
DR EMBL; D00575; BAA00453.1; -; mRNA.
DR PIR; JT0408; TTRTA.
DR RefSeq; XP_017448612.1; XM_017593123.1.
DR AlphaFoldDB; P11962; -.
DR SMR; P11962; -.
DR IntAct; P11962; 1.
DR STRING; 10116.ENSRNOP00000012385; -.
DR GlyGen; P11962; 2 sites.
DR PaxDb; P11962; -.
DR Ensembl; ENSRNOT00000012385; ENSRNOP00000012385; ENSRNOG00000009269.
DR GeneID; 116700; -.
DR UCSC; RGD:620436; rat.
DR CTD; 1081; -.
DR RGD; 620436; Cga.
DR eggNOG; ENOG502S1PK; Eukaryota.
DR GeneTree; ENSGT00390000012242; -.
DR HOGENOM; CLU_148106_0_0_1; -.
DR InParanoid; P11962; -.
DR OMA; ATVMGNT; -.
DR OrthoDB; 1430707at2759; -.
DR PhylomeDB; P11962; -.
DR TreeFam; TF332733; -.
DR Reactome; R-RNO-193048; Androgen biosynthesis.
DR Reactome; R-RNO-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-RNO-209822; Glycoprotein hormones.
DR Reactome; R-RNO-209968; Thyroxine biosynthesis.
DR Reactome; R-RNO-375281; Hormone ligand-binding receptors.
DR Reactome; R-RNO-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-RNO-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR PRO; PR:P11962; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009269; Expressed in ovary and 3 other tissues.
DR ExpressionAtlas; P11962; baseline and differential.
DR Genevisible; P11962; RN.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016914; C:follicle-stimulating hormone complex; ISS:UniProtKB.
DR GO; GO:0061696; C:pituitary gonadotropin complex; ISO:RGD.
DR GO; GO:0016913; F:follicle-stimulating hormone activity; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0046884; P:follicle-stimulating hormone secretion; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; ISO:RGD.
DR GO; GO:0032275; P:luteinizing hormone secretion; ISO:RGD.
DR GO; GO:0046621; P:negative regulation of organ growth; ISO:RGD.
DR GO; GO:0035265; P:organ growth; IEA:Ensembl.
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:0030878; P:thyroid gland development; ISO:RGD.
DR GO; GO:0006590; P:thyroid hormone generation; ISO:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011650"
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"
FT CONFLICT 84
FT /note="E -> Q (in Ref. 1; AAA97425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13453 MW; BE0E7F3C44C69ECB CRC64;
MDCYRRYAAV ILVMLSMVLH ILHSLPDGDL IIQGCPECKL KENKYFSKLG APIYQCMGCC
FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KSFTKATVMG NARVENHTDC HCSTCYYHKS
