GLHA_MELGA
ID GLHA_MELGA Reviewed; 120 AA.
AC P68241; P37035;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1723796; DOI=10.3382/ps.0702516;
RA Foster D.N., Foster L.K.;
RT "Cloning and sequence analysis of the common alpha-subunit complementary
RT deoxyribonucleic acid of turkey pituitary glycoprotein hormones.";
RL Poult. Sci. 70:2516-2523(1991).
RN [2]
RP PROTEIN SEQUENCE OF 34-61.
RX PubMed=1701134; DOI=10.1210/endo-127-6-2985;
RA Bergert E.R., Madden B., McCormick D.J., Papkoff H., Ryan R.J.;
RT "The antigenic structure of the human glycoprotein hormone alpha-subunit:
RT II. Cross-species comparisons.";
RL Endocrinology 127:2985-2989(1990).
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. {ECO:0000250|UniProtKB:P01215}.
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: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; M33698; AAA49629.1; -; mRNA.
DR PIR; A45585; A45585.
DR RefSeq; NP_001290106.1; NM_001303177.1.
DR RefSeq; XP_019468017.1; XM_019612472.1.
DR RefSeq; XP_019468018.1; XM_019612473.1.
DR AlphaFoldDB; P68241; -.
DR SMR; P68241; -.
DR Ensembl; ENSMGAT00000015400; ENSMGAP00000014464; ENSMGAG00000013689.
DR GeneID; 100303682; -.
DR KEGG; mgp:100303682; -.
DR CTD; 1081; -.
DR GeneTree; ENSGT00390000012242; -.
DR HOGENOM; CLU_148106_0_0_1; -.
DR InParanoid; P68241; -.
DR OMA; ATVMGNT; -.
DR OrthoDB; 1430707at2759; -.
DR TreeFam; TF332733; -.
DR Proteomes; UP000001645; Chromosome 2.
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:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0046884; P:follicle-stimulating hormone secretion; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; IEA:Ensembl.
DR GO; GO:0032275; P:luteinizing hormone secretion; IEA:Ensembl.
DR GO; GO:0046621; P:negative regulation of organ growth; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
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:0000255"
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011658"
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; 13591 MW; F4662BA0CB6005EB CRC64;
MDCYRKYAAV TLTILSVFLH LLHTFPDGEF LMQGCPECKL GENRFFSKPG APIYQCTGCC
FSRAYPTPMR SKKTMLVPKN ITSEATCCVA KAFTKITLKD NVKIENHTDC HCSTCYYHKS