GLHA_BOVIN
ID GLHA_BOVIN Reviewed; 120 AA.
AC P01217;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6314263; DOI=10.1093/nar/11.19.6873;
RA Goodwin R.G., Moncman C.L., Rottman F.M., Nilson J.H.;
RT "Characterization and nucleotide sequence of the gene for the common alpha
RT subunit of the bovine pituitary glycoprotein hormones.";
RL Nucleic Acids Res. 11:6873-6882(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6688736; DOI=10.1021/bi00289a036;
RA Erwin C., Croyle M.L., Donelson J., Maurer R.;
RT "Nucleotide sequence of cloned complementary deoxyribonucleic acid for the
RT alpha subunit of bovine pituitary glycoprotein hormones.";
RL Biochemistry 22:4856-4860(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-120.
RX PubMed=6187740; DOI=10.1016/s0021-9258(18)32472-4;
RA Nilson J.H., Thomason A.R., Cserbak M.T., Moncman C.L., Woychik R.P.;
RT "Nucleotide sequence of a cDNA for the common alpha subunit of the bovine
RT pituitary glycoprotein hormones. Conservation of nucleotides in the 3'-
RT untranslated region of bovine and human pre-alpha subunit mRNAs.";
RL J. Biol. Chem. 258:4679-4682(1983).
RN [4]
RP PROTEIN SEQUENCE OF 25-120.
RX PubMed=5101174; DOI=10.1016/s0021-9258(18)62404-4;
RA Liao T.-H., Pierce J.G.;
RT "The primary structure of bovine thyrotropin. II. The amino acid sequences
RT of the reduced, S-carboxymethyl alpha and beta chains.";
RL J. Biol. Chem. 246:850-865(1971).
RN [5]
RP PRELIMINARY PARTIAL PROTEIN SEQUENCE.
RX PubMed=5101175; DOI=10.1016/s0021-9258(18)62405-6;
RA Pierce J.G., Liao T.-H., Carlsen R.B., Reimo T.;
RT "Comparisons between the alpha chain of bovine thyrotropin and the CI chain
RT of luteinizing hormone. Compositions of tryptic peptides, cyanogen bromide
RT fragments, and carbohydrate moieties.";
RL J. Biol. Chem. 246:866-872(1971).
RN [6]
RP PROTEIN SEQUENCE OF 80-91 AND 100-120.
RX PubMed=5107231; DOI=10.1111/j.1432-1033.1971.tb01494.x;
RA Maghuin-Rogister G., Hennen G.P.;
RT "Bovine luteinizing hormone. Study of the primary structure around the
RT carbohydrate attachment sites of the luteinizing hormone alpha-subunit.";
RL Eur. J. Biochem. 21:489-497(1971).
RN [7]
RP PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
RX PubMed=4854483; DOI=10.1016/s0021-9258(19)42498-8;
RA Cornell J.S., Pierce J.G.;
RT "Studies on the disulfide bonds of glycoprotein hormones. Locations in the
RT alpha chain based on partial reductions and formation of 14C-labeled S-
RT carboxymethyl derivatives.";
RL J. Biol. Chem. 249:4166-4174(1974).
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; X00003; CAA24907.1; -; Genomic_DNA.
DR EMBL; X00004; CAA24907.1; JOINED; Genomic_DNA.
DR EMBL; X00050; CAA24932.1; -; mRNA.
DR PIR; A93489; TTBOA.
DR RefSeq; NP_776326.1; NM_173901.3.
DR AlphaFoldDB; P01217; -.
DR SMR; P01217; -.
DR STRING; 9913.ENSBTAP00000021481; -.
DR GlyConnect; 164; 2 N-Linked glycans.
DR GlyConnect; 193; 1 O-Linked glycan (1 site).
DR GlyConnect; 349; 6 N-Linked glycans.
DR GlyConnect; 601; 37 N-Linked glycans.
DR iPTMnet; P01217; -.
DR PaxDb; P01217; -.
DR Ensembl; ENSBTAT00000021481; ENSBTAP00000021481; ENSBTAG00000016138.
DR Ensembl; ENSBTAT00000078886; ENSBTAP00000065256; ENSBTAG00000016138.
DR GeneID; 280749; -.
DR KEGG; bta:280749; -.
DR CTD; 1081; -.
DR VEuPathDB; HostDB:ENSBTAG00000016138; -.
DR VGNC; VGNC:27257; CGA.
DR eggNOG; ENOG502S1PK; Eukaryota.
DR GeneTree; ENSGT00390000012242; -.
DR HOGENOM; CLU_148106_0_0_1; -.
DR InParanoid; P01217; -.
DR OMA; ATVMGNT; -.
DR OrthoDB; 1430707at2759; -.
DR TreeFam; TF332733; -.
DR Reactome; R-BTA-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-BTA-209822; Glycoprotein hormones.
DR Reactome; R-BTA-209968; Thyroxine biosynthesis.
DR Reactome; R-BTA-375281; Hormone ligand-binding receptors.
DR Reactome; R-BTA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-BTA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000016138; Expressed in adenohypophysis and 67 other tissues.
DR ExpressionAtlas; P01217; baseline.
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; -; 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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:5101174"
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011633"
FT CARBOHYD 67
FT /note="O-linked (GalNAc...) threonine"
FT /id="CAR_000035"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:5101174"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:5101174"
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 CONFLICT 13
FT /note="A -> T (in Ref. 2; CAA24932)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="P -> A (in Ref. 2; CAA24932)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..87
FT /note="EATC -> AZCT (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13616 MW; 246B415F86D04230 CRC64;
MDYYRKYAAV ILAILSLFLQ ILHSFPDGEF TMQGCPECKL KENKYFSKPD APIYQCMGCC
FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVMG NVRVENHTEC HCSTCYYHKS
