ID GLHA_CALJA Reviewed; 120 AA.
AC P51499;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 24-JAN-2024, entry version 93.
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 Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7492691; DOI=10.1095/biolreprod53.2.380;
RA Simula A.P., Amato F., Faast R., Lopata A., Berka J., Norman R.J.;
RT "Luteinizing hormone/chorionic gonadotropin bioactivity in the common
RT marmoset (Callithrix jacchus) is due to a chorionic gonadotropin molecule
RT with a structure intermediate between human chorionic gonadotropin and
RT human luteinizing hormone.";
RL Biol. Reprod. 53:380-389(1995).
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:0000250|UniProtKB:P01215}.
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:0000250|UniProtKB:P01215}.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; U04446; AAC00030.1; -; mRNA.
DR PIR; G00021; G00021.
DR RefSeq; NP_001254689.1; NM_001267760.1.
DR AlphaFoldDB; P51499; -.
DR SMR; P51499; -.
DR STRING; 9483.ENSCJAP00000001086; -.
DR GlyCosmos; P51499; 2 sites, No reported glycans.
DR GeneID; 100389264; -.
DR KEGG; cjc:100389264; -.
DR CTD; 1081; -.
DR eggNOG; ENOG502S1PK; Eukaryota.
DR InParanoid; P51499; -.
DR OrthoDB; 4182331at2759; -.
DR Proteomes; UP000008225; Unplaced.
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 Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000476; Glyco_hormone.
DR PANTHER; PTHR11509; GLYCOPROTEIN HORMONE ALPHA CHAIN; 1.
DR PANTHER; PTHR11509:SF0; GLYCOPROTEIN HORMONES ALPHA CHAIN; 1.
DR Pfam; PF00236; Hormone_6; 1.
DR PRINTS; PR00274; GLYCOHORMONE.
DR SMART; SM00067; GHA; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 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_0000011634"
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; 13744 MW; 6EEF0638179D56F9 CRC64;
MDYYRKYAAI ILITLSVFLH ILHSLPDGEF TAEECPECKL KENKYFSRLG SPIYQCMGCC
FSRAYPTPLR SQKTMLVPKN VTSESTCCVA KAYTKATVMG NIRVENHTEC HCSTCYHHKF
//
