GLHA_STRCA
ID GLHA_STRCA Reviewed; 96 AA.
AC P80665;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 67.
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 Struthio camelus (Common ostrich).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=8801;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=8925835; DOI=10.1111/j.1432-1033.1996.0262h.x;
RA Koide Y., Papkoff H., Kawauchi H.;
RT "Complete amino acid sequences of follitropin and lutropin in the ostrich,
RT Struthio camelus.";
RL Eur. J. Biochem. 240:262-267(1996).
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. {ECO:0000250|UniProtKB:P01215}.
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: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; S74086; S74086.
DR AlphaFoldDB; P80665; -.
DR SMR; P80665; -.
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_0000149031"
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; 10782 MW; 1D6D4CC67187BC37 CRC64;
FPDGEFLMQG CPECKLGENR FFSKPGAPVY QCTGCCFSRA YPTPLRSKKT MLVPKNITSE
ATCCVAKAFT KITLKDNVKI ENHTECHCST CYYHKS
