GLHA_ANGAN
ID GLHA_ANGAN Reviewed; 117 AA.
AC P27794;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Glycoprotein hormones alpha chain;
DE AltName: Full=GTH-alpha;
DE AltName: Full=Gonadotropin alpha chain;
DE Flags: Precursor;
GN Name=cga;
OS Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7936;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=1698669; DOI=10.1016/0303-7207(90)90030-c;
RA Querat B., Jutisz M., Fontaine Y.-A., Counis R.;
RT "Cloning and sequence analysis of the cDNA for the pituitary glycoprotein
RT hormone alpha-subunit of the European eel.";
RL Mol. Cell. Endocrinol. 71:253-259(1990).
CC -!- FUNCTION: Shared alpha chain of heterodimeric glycoprotein hormones.
CC These hormones bind specific receptors on target cells that in turn
CC activate downstream signaling pathways. Involved in gametogenesis and
CC steroidogenesis. {ECO:0000250|UniProtKB:P37204}.
CC -!- SUBUNIT: Heterodimer. Glycoprotein hormones are heterodimers composed
CC of a common alpha chain described here and a unique beta chain which
CC confers their biological specificity to the different hormones.
CC {ECO:0000250|UniProtKB:P37204}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P37204}.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; X61038; CAA43373.1; -; mRNA.
DR PIR; A37198; A37198.
DR AlphaFoldDB; P27794; -.
DR SMR; P27794; -.
DR OMA; ATVMGNT; -.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..117
FT /note="Glycoprotein hormones alpha chain"
FT /id="PRO_0000011660"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT CARBOHYD 103
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..107
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 60..109
FT /evidence="ECO:0000250|UniProtKB:P01215"
FT DISULFID 87..112
FT /evidence="ECO:0000250|UniProtKB:P01215"
SQ SEQUENCE 117 AA; 13206 MW; D5D9A7B49D401E09 CRC64;
MMVCPGKPGA SLLMLSMLFH IIDSYPNNEM ARGGCDECRL QENKIFSKPS APIFQCVGCC
FSRAYPTPLR SKKTMLVPKN ITSEATCCVA REVTRLDNMK LENHTDCHCS TCYYHKF