GLHA_MOUSE
ID GLHA_MOUSE Reviewed; 120 AA.
AC P01216; P11963; Q5M8P4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 168.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6272299; DOI=10.1073/pnas.78.9.5329;
RA Chin W.W., Kronenberg H.M., Dee P.C., Maloof F., Habener J.F.;
RT "Nucleotide sequence of the mRNA encoding the pre-alpha-subunit of mouse
RT thyrotropin.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:5329-5333(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2466623; DOI=10.1089/dna.1988.7.679;
RA Gordon D.F., Wood W.M., Ridgway E.C.;
RT "Organization and nucleotide sequence of the mouse alpha-subunit gene of
RT the pituitary glycoprotein hormones.";
RL DNA 7:679-690(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=JF1; TISSUE=Pituitary;
RX PubMed=12112597; DOI=10.1002/mrd.10120;
RA Suzuki O., Mochida K., Yamamoto Y., Noguchi Y., Takano K., Matsuda J.,
RA Ogura A.;
RT "Comparison of glycoprotein hormone alpha-subunits of laboratory animals.";
RL Mol. Reprod. Dev. 62:335-342(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC -!- CAUTION: PubMed:6177696 sequence was originally thought to originate
CC from rat. {ECO:0000305}.
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DR EMBL; J00643; AAA96700.1; -; mRNA.
DR EMBL; V01253; CAA24566.1; -; mRNA.
DR EMBL; M22991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M22992; AAA99228.1; -; Genomic_DNA.
DR EMBL; AF307151; AAG30279.1; -; mRNA.
DR EMBL; BC087926; AAH87926.1; -; mRNA.
DR CCDS; CCDS18035.1; -.
DR PIR; A31598; TTMSA.
DR RefSeq; NP_034019.1; NM_009889.2.
DR RefSeq; XP_006537649.1; XM_006537586.2.
DR AlphaFoldDB; P01216; -.
DR SMR; P01216; -.
DR STRING; 10090.ENSMUSP00000029975; -.
DR GlyGen; P01216; 2 sites.
DR iPTMnet; P01216; -.
DR PhosphoSitePlus; P01216; -.
DR PaxDb; P01216; -.
DR PeptideAtlas; P01216; -.
DR PRIDE; P01216; -.
DR ProteomicsDB; 268832; -.
DR Antibodypedia; 18627; 1524 antibodies from 39 providers.
DR DNASU; 12640; -.
DR Ensembl; ENSMUST00000029975; ENSMUSP00000029975; ENSMUSG00000028298.
DR Ensembl; ENSMUST00000108130; ENSMUSP00000103765; ENSMUSG00000028298.
DR GeneID; 12640; -.
DR KEGG; mmu:12640; -.
DR UCSC; uc008sgq.1; mouse.
DR CTD; 1081; -.
DR MGI; MGI:88390; Cga.
DR VEuPathDB; HostDB:ENSMUSG00000028298; -.
DR eggNOG; ENOG502S1PK; Eukaryota.
DR GeneTree; ENSGT00390000012242; -.
DR HOGENOM; CLU_148106_0_0_1; -.
DR InParanoid; P01216; -.
DR OMA; ATVMGNT; -.
DR OrthoDB; 1430707at2759; -.
DR PhylomeDB; P01216; -.
DR TreeFam; TF332733; -.
DR Reactome; R-MMU-193048; Androgen biosynthesis.
DR Reactome; R-MMU-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-MMU-209822; Glycoprotein hormones.
DR Reactome; R-MMU-209968; Thyroxine biosynthesis.
DR Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR BioGRID-ORCS; 12640; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Chga; mouse.
DR PRO; PR:P01216; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P01216; protein.
DR Bgee; ENSMUSG00000028298; Expressed in pituitary gland and 24 other tissues.
DR ExpressionAtlas; P01216; baseline and differential.
DR Genevisible; P01216; MM.
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:MGI.
DR GO; GO:0016913; F:follicle-stimulating hormone activity; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0046884; P:follicle-stimulating hormone secretion; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; IMP:MGI.
DR GO; GO:0032275; P:luteinizing hormone secretion; IMP:MGI.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI.
DR GO; GO:0035265; P:organ growth; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0006590; P:thyroid hormone generation; IMP:MGI.
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_0000011648"
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 5..6
FT /note="RK -> KR (in Ref. 2; CAA24566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13565 MW; F2FA2E4632716DBC CRC64;
MDYYRKYAAV ILVMLSMFLH ILHSLPDGDF IIQGCPECKL KENKYFSKLG APIYQCMGCC
FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVMG NARVENHTEC HCSTCYYHKS
