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Database: UniProt
Entry: GLHA_AILME
LinkDB: GLHA_AILME
Original site: GLHA_AILME 
ID   GLHA_AILME              Reviewed;         120 AA.
AC   Q8WN20;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 65.
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   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=12654531; DOI=10.1016/s0378-4320(02)00275-0;
RA   Liao M.J., Zhu M.Y., Zhang Z.H., Zhang A.J., Li G.H., Sheng F.J.;
RT   "Cloning and sequence analysis of FSH and LH in the giant panda (Ailuropoda
RT   melanoleuca).";
RL   Anim. Reprod. Sci. 77:107-116(2003).
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}.
DR   EMBL; AF448453; AAL41020.1; -; mRNA.
DR   RefSeq; NP_001291847.1; NM_001304918.1.
DR   SMR; Q8WN20; -.
DR   STRING; 9646.ENSAMEP00000012113; -.
DR   PRIDE; Q8WN20; -.
DR   GeneID; 100480190; -.
DR   KEGG; aml:100480190; -.
DR   CTD; 1081; -.
DR   eggNOG; ENOG410IWI0; Eukaryota.
DR   eggNOG; ENOG4111Q75; LUCA.
DR   HOGENOM; HOG000232008; -.
DR   InParanoid; Q8WN20; -.
DR   KO; K08522; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
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_0000042872"
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;  13573 MW;  40794E8E253C243D CRC64;
     MDYYRKYAAV ILTTLSVFLH ILHSFPDGEF TMQGCPECKL KENKYFSKLG APIYQCMGCC
     FSRAYPTPAR SKKTMLVPKN ITLEATCCVA KAFTKATVMG NTKVENHTDC HCSTCYYHKS
//
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