GLHA_MACFA
ID GLHA_MACFA Reviewed; 120 AA.
AC Q9BEH3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Glycoprotein hormones alpha chain;
DE AltName: Full=Anterior pituitary glycoprotein hormones common subunit alpha;
DE AltName: Full=Choriogonadotropin alpha chain;
DE AltName: Full=Chorionic gonadotrophin subunit alpha;
DE Short=CG-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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Trophoblast;
RX PubMed=11793416; DOI=10.1002/ajp.1066;
RA Wilken J.A., Matsumoto K., Laughlin L.S., Lasley B.L., Bedows E.;
RT "Comparison of chorionic gonadotropin expression in human and macaque
RT (Macaca fascicularis) trophoblasts.";
RL Am. J. Primatol. 56:89-97(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Pituitary;
RX PubMed=10612425; DOI=10.1016/s0303-7207(99)00140-9;
RA Schmidt A., Gromoll J., Weinbauer G.F., Galla H.J., Chappel S., Simoni M.;
RT "Cloning and expression of cynomolgus monkey (Macaca fascicularis)
RT gonadotropins luteinizing hormone and follicle-stimulating hormone and
RT identification of two polymorphic sites in the luteinizing hormone beta
RT subunit.";
RL Mol. Cell. Endocrinol. 156:73-83(1999).
CC -!- FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein
CC hormones thyrotropin/thyroid stimulating hormone/TSH,
CC lutropin/luteinizing hormone/LH, follitropin/follicle stimulating
CC hormone/FSH and choriogonadotropin/CG. These hormones bind specific
CC receptors on target cells that in turn activate downstream signaling
CC pathways. {ECO:0000269|PubMed:10612425}.
CC -!- SUBUNIT: Heterodimer. The active hormones thyrotropin, lutropin,
CC follitropin and choriogonadotropin are heterodimers composed of CGA, a
CC common alpha chain described here and a unique beta chain which confers
CC their biological specificity to the hormones: TSHB for thyrotropin, LHB
CC for lutropin, FSHB for follitropin and choriogonadotropin subunit
CC beta/CGB for choriogonadotropin. {ECO:0000250|UniProtKB:P01215}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10612425}.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; AY026358; AAK08642.1; -; mRNA.
DR EMBL; AJ781394; CAH03728.1; -; mRNA.
DR RefSeq; NP_001271473.1; NM_001284544.1.
DR RefSeq; XP_015304325.1; XM_015448839.1.
DR AlphaFoldDB; Q9BEH3; -.
DR SMR; Q9BEH3; -.
DR GeneID; 102138376; -.
DR KEGG; mcf:102138376; -.
DR CTD; 1081; -.
DR VEuPathDB; HostDB:ENSMFAG00000037707; -.
DR OMA; ATVMGNT; -.
DR OrthoDB; 1430707at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016914; C:follicle-stimulating hormone complex; IDA:UniProtKB.
DR GO; GO:0016913; F:follicle-stimulating hormone activity; IDA:UniProtKB.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:UniProtKB.
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 /evidence="ECO:0000250"
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011641"
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; 13825 MW; 92E92D6428788866 CRC64;
MDYYRKYAAV ILVTLSVFLH ILHSFPDGEF TMQDCPECKP RENKFFSKPG APIYQCMGCC
FSRAYPTPLR SKKTMLVQKN VTSESTCCVA KSLTRVMVMG NVRVENHTQC HCSTCYYHKF
