GLHA_SHEEP
ID GLHA_SHEEP Reviewed; 120 AA.
AC P01218;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=LH alpha 3;
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 Contains:
DE RecName: Full=LH alpha 1-1;
DE Contains:
DE RecName: Full=LH alpha 1-2;
DE Contains:
DE RecName: Full=LH alpha 1-3;
DE Flags: Precursor;
GN Name=CGA;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2481272; DOI=10.1093/nar/17.24.10494;
RA Bello P.A., Mountford P.S., Brandon M.R., Adams T.E.;
RT "Cloning and DNA sequence analysis of the cDNA for the common alpha-subunit
RT of the ovine pituitary glycoprotein hormones.";
RL Nucleic Acids Res. 17:10494-10494(1989).
RN [2]
RP PROTEIN SEQUENCE OF 25-120.
RX PubMed=5064343; DOI=10.1016/s0021-9258(19)45082-5;
RA Liu W.-K., Nahm H.S., Sweeney C.M., Lamkin W.M., Baker H.N., Ward D.N.;
RT "The primary structure of ovine luteinizing hormone. I. The amino acid
RT sequence of the reduced and S-aminoethylated S-subunit (LH-alpha).";
RL J. Biol. Chem. 247:4351-4364(1972).
RN [3]
RP PROTEIN SEQUENCE OF 25-120.
RX PubMed=4676903; DOI=10.1016/0003-9861(72)90374-8;
RA Sairam M.R., Papkoff H., Li C.H.;
RT "The primary structure of ovine interstitial cell-stimulating hormone. I.
RT The alpha-subunit.";
RL Arch. Biochem. Biophys. 153:554-571(1972).
RN [4]
RP PROTEIN SEQUENCE OF 25-120.
RX PubMed=6798968; DOI=10.1042/bj1970535;
RA Sairam M.R.;
RT "Primary structure of the ovine pituitary follitropin alpha-subunit.";
RL Biochem. J. 197:535-539(1981).
RN [5]
RP PROTEIN SEQUENCE OF 25-41, FUNCTION, AND SUBUNIT.
RX PubMed=2456202; DOI=10.1210/endo-123-2-700;
RA Nomura K., Tsunasawa S., Ohmura K., Sakiyama F., Shizume K.;
RT "Renotropic activity in ovine luteinizing hormone isoform(s).";
RL Endocrinology 123:700-712(1988).
RN [6]
RP PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
RA Chung D., Sairam M.R., Li C.H.;
RT "The primary structure of ovine interstitial cell-stimulating hormone. III.
RT Disulfide bridges of the alpha-subunit.";
RL Arch. Biochem. Biophys. 159:678-682(1973).
RN [7]
RP STRUCTURE OF CARBOHYDRATES, AND GLYCOSYLATION AT ASN-80 AND ASN-106.
RX PubMed=2209620; DOI=10.1111/j.1432-1033.1990.tb19285.x;
RA Weisshaar G., Hiyama J., Renwick A.G.C.;
RT "Site-specific N-glycosylation of ovine lutropin. Structural analysis by
RT one- and two-dimensional 1H-NMR spectroscopy.";
RL Eur. J. Biochem. 192:741-751(1990).
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 (By similarity). The alpha chain can also be
CC formed by LH alpha 1-1, LH alpha 1-2 and LH alpha 1-3.
CC {ECO:0000250|UniProtKB:P01215, ECO:0000269|PubMed:2456202}.
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; X16977; CAA34848.1; -; mRNA.
DR PIR; S06935; UTSHA.
DR RefSeq; NP_001009464.1; NM_001009464.1.
DR AlphaFoldDB; P01218; -.
DR SMR; P01218; -.
DR STRING; 9940.ENSOARP00000014092; -.
DR GlyConnect; 195; 9 N-Linked glycans (2 sites).
DR GlyConnect; 348; 3 N-Linked glycans.
DR Ensembl; ENSOART00000014299; ENSOARP00000014092; ENSOARG00000013153.
DR Ensembl; ENSOART00020023245; ENSOARP00020019277; ENSOARG00020015174.
DR GeneID; 443538; -.
DR KEGG; oas:443538; -.
DR CTD; 1081; -.
DR eggNOG; ENOG502S1PK; Eukaryota.
DR HOGENOM; CLU_148106_0_0_1; -.
DR OMA; ATVMGNT; -.
DR OrthoDB; 1430707at2759; -.
DR Proteomes; UP000002356; Chromosome 8.
DR Bgee; ENSOARG00000013153; Expressed in pituitary gland and 12 other tissues.
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|PubMed:2456202,
FT ECO:0000269|PubMed:4676903, ECO:0000269|PubMed:5064343,
FT ECO:0000269|PubMed:6798968"
FT CHAIN 25..120
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011652"
FT CHAIN 28..120
FT /note="LH alpha 1-1"
FT /id="PRO_0000011653"
FT CHAIN 30..120
FT /note="LH alpha 1-2"
FT /id="PRO_0000011654"
FT CHAIN 31..120
FT /note="LH alpha 1-3"
FT /id="PRO_0000011655"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2209620"
FT /id="CAR_000038"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2209620"
FT /id="CAR_000039"
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"
FT CONFLICT 27
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="E -> Q (in Ref. 2; AA sequence, 3; AA sequence and
FT 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..113
FT /note="CS -> SC (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13588 MW; 1F06F784F2420181 CRC64;
MDYYRKYAAA ILAILSLFLQ ILHSFPDGEF TMQGCPECKL KENKYFSKPD APIYQCMGCC
FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVMG NVRVENHTEC HCSTCYYHKS
