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   25-MAY-2022, entry version 90.
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   GeneID; 100389264; -.
DR   KEGG; cjc:100389264; -.
DR   CTD; 1081; -.
DR   eggNOG; ENOG502S1PK; Eukaryota.
DR   InParanoid; P51499; -.
DR   OrthoDB; 1430707at2759; -.
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; -; 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_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