ID   GLHA_BALAC              Reviewed;          96 AA.
AC   P37036;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   07-OCT-2020, entry version 64.
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;
GN   Name=CGA;
OS   Balaenoptera acutorostrata (Common minke whale) (Balaena rostrata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=9767;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Karasev V.S., Pankov Y.A.;
RT   "Amino acid sequence of reduced and carboxymethylated alpha- and beta-
RT   subunits of the little picked whale luteinizing hormone.";
RL   Biokhimiia 50:1972-1986(1985).
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   PIR; PN0138; PN0138.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone; Secreted.
FT   CHAIN           1..96
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000149029"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        11..35
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        14..64
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        32..86
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        36..88
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
FT   DISULFID        63..91
FT                   /evidence="ECO:0000250|UniProtKB:P01215"
SQ   SEQUENCE   96 AA;  10721 MW;  4901C08422FD66D5 CRC64;
     FPBGZFTMZG CPZCKLKZBK YFSKLGAPIY ZCMGCCFSRA YPTPARSKKT MLVPKNITSZ
     ATCCVAKAFT KATVMGBARV ZNHTZCHCST CYYHKS