GLHA1_CYPCA
ID GLHA1_CYPCA Reviewed; 118 AA.
AC P01221;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Glycoprotein hormones alpha chain 1;
DE AltName: Full=GTH-alpha;
DE AltName: Full=Gonadotropin alpha chain 1;
DE Flags: Precursor;
GN Name=cgaa;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3246480; DOI=10.1111/j.1399-3011.1988.tb01387.x;
RA Chang Y.S., Huang C.-J., Huang F.-L., Lo T.-B.;
RT "Primary structures of carp gonadotropin subunits deduced from cDNA
RT nucleotide sequences.";
RL Int. J. Pept. Protein Res. 32:556-564(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1370380; DOI=10.1016/0167-4781(92)90496-m;
RA Huang C.J., Huang F.-L., Wang Y.C., Chang Y.S., Lo T.-B.;
RT "Organization and nucleotide sequence of carp gonadotropin alpha subunit
RT genes.";
RL Biochim. Biophys. Acta 1129:239-242(1992).
RN [3]
RP PROTEIN SEQUENCE OF 24-56 AND 114-118.
RX PubMed=607993; DOI=10.1016/s0300-9084(78)80704-4;
RA Jolles J., Burzawa-Gerard E., Fontaine Y.-A., Jolles P.;
RT "The evolution of gonadotropins: some molecular data concerning a non-
RT mammalian pituitary gonadotropin, the hormone from a teleost fish (Cyprinus
RT carpio L.).";
RL Biochimie 59:893-898(1977).
CC -!- FUNCTION: Involved in gametogenesis and steroidogenesis.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Secreted.
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; M37379; AAA49209.1; -; mRNA.
DR EMBL; X56497; CAA39852.1; -; Genomic_DNA.
DR PIR; S20607; UTCAA.
DR RefSeq; XP_018951691.1; XM_019096146.1.
DR AlphaFoldDB; P01221; -.
DR SMR; P01221; -.
DR Ensembl; ENSCCRT00015084486; ENSCCRP00015081810; ENSCCRG00015033087.
DR GeneID; 109081150; -.
DR KEGG; ccar:109081150; -.
DR CTD; 1081; -.
DR OrthoDB; 1430707at2759; -.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization 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..23
FT /evidence="ECO:0000269|PubMed:607993"
FT CHAIN 24..118
FT /note="Glycoprotein hormones alpha chain 1"
FT /id="PRO_0000011665"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 34..58
FT /evidence="ECO:0000250"
FT DISULFID 37..87
FT /evidence="ECO:0000250"
FT DISULFID 55..108
FT /evidence="ECO:0000250"
FT DISULFID 59..110
FT /evidence="ECO:0000250"
FT DISULFID 86..113
FT /evidence="ECO:0000250"
SQ SEQUENCE 118 AA; 13533 MW; 2B123327556017E5 CRC64;
MFWTRYAGAS ILLFFMLIRL GQLYPRNDMN NFGCEECKLK ENNIFSKPGA PVYQCMGCCF
SRAYPTPLRS KKTMLVPKNI TSEATCCVAK EVKRVLVNDV KLVNHTDCHC STCYYHKS
