ID   GLHA_RABIT              Reviewed;         120 AA.
AC   P07474; Q9BGA0;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 125.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Japanese white; TISSUE=Pituitary;
RX   PubMed=12112597; DOI=10.1002/mrd.10120;
RA   Suzuki O., Mochida K., Yamamoto Y., Noguchi Y., Takano K., Matsuda J.,
RA   Ogura A.;
RT   "Comparison of glycoprotein hormone alpha-subunits of laboratory animals.";
RL   Mol. Reprod. Dev. 62:335-342(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-120.
RA   Glenn S.D., Nahm H.S., Ward D.N.;
RT   "The amino acid sequence of the rabbit glycoprotein hormone alpha
RT   subunit.";
RL   J. Protein Chem. 3:143-156(1984).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF318299; AAK06653.1; -; mRNA.
DR   PIR; A05096; A05096.
DR   RefSeq; NP_001076193.1; NM_001082724.1.
DR   RefSeq; XP_008260942.1; XM_008262720.2.
DR   AlphaFoldDB; P07474; -.
DR   SMR; P07474; -.
DR   STRING; 9986.ENSOCUP00000007243; -.
DR   Ensembl; ENSOCUT00000008384; ENSOCUP00000007243; ENSOCUG00000008386.
DR   GeneID; 100009481; -.
DR   KEGG; ocu:100009481; -.
DR   CTD; 1081; -.
DR   eggNOG; ENOG502S1PK; Eukaryota.
DR   GeneTree; ENSGT00390000012242; -.
DR   HOGENOM; CLU_148106_0_0_1; -.
DR   InParanoid; P07474; -.
DR   OMA; ATVMGNT; -.
DR   OrthoDB; 1430707at2759; -.
DR   TreeFam; TF332733; -.
DR   Proteomes; UP000001811; Chromosome 12.
DR   Bgee; ENSOCUG00000008386; Expressed in ovary and 1 other tissue.
DR   ExpressionAtlas; P07474; baseline.
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;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           25..120
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000042879"
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;  13413 MW;  B077BA3B936A890A CRC64;
     MGYYRKYAAV ILATLSVFLH ILHSFPDGEF AMQGCPECKL KENKYFSKLG APIYQCMGCC
     FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVMG NAKVENHTEC HCSTCYYHKS