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Database: UniProt
Entry: A0A1S3GHM8_DIPOR
LinkDB: A0A1S3GHM8_DIPOR
Original site: A0A1S3GHM8_DIPOR 
ID   A0A1S3GHM8_DIPOR        Unreviewed;       120 AA.
AC   A0A1S3GHM8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glycoprotein hormones alpha chain {ECO:0000256|ARBA:ARBA00017839, ECO:0000256|RuleBase:RU362129};
GN   Name=Cga {ECO:0000313|RefSeq:XP_012888311.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888311.1};
RN   [1] {ECO:0000313|RefSeq:XP_012888311.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888311.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00011162,
CC       ECO:0000256|RuleBase:RU362129}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU362129}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC       {ECO:0000256|ARBA:ARBA00009128, ECO:0000256|RuleBase:RU362129}.
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DR   RefSeq; XP_012888311.1; XM_013032857.1.
DR   AlphaFoldDB; A0A1S3GHM8; -.
DR   STRING; 10020.ENSDORP00000025928; -.
DR   GeneID; 105998206; -.
DR   KEGG; dord:105998206; -.
DR   CTD; 1081; -.
DR   InParanoid; A0A1S3GHM8; -.
DR   OMA; MMQGCPE; -.
DR   OrthoDB; 4182331at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0016914; C:follicle-stimulating hormone complex; IEA:Ensembl.
DR   GO; GO:0016913; F:follicle-stimulating hormone activity; IEA:Ensembl.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0046884; P:follicle-stimulating hormone secretion; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0008406; P:gonad development; IEA:Ensembl.
DR   GO; GO:0032275; P:luteinizing hormone secretion; IEA:Ensembl.
DR   GO; GO:0046621; P:negative regulation of organ growth; IEA:Ensembl.
DR   GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR   GO; GO:0010893; P:positive regulation of steroid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR   GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
DR   Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR000476; Glyco_hormone.
DR   PANTHER; PTHR11509; GLYCOPROTEIN HORMONE ALPHA CHAIN; 1.
DR   PANTHER; PTHR11509:SF0; GLYCOPROTEIN HORMONES ALPHA CHAIN; 1.
DR   Pfam; PF00236; Hormone_6; 1.
DR   PRINTS; PR00274; GLYCOHORMONE.
DR   SMART; SM00067; GHA; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 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 {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|RuleBase:RU362129};
KW   Hormone {ECO:0000256|ARBA:ARBA00022702, ECO:0000256|RuleBase:RU362129};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362129};
KW   Signal {ECO:0000256|RuleBase:RU362129}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU362129"
FT   CHAIN           25..120
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /evidence="ECO:0000256|RuleBase:RU362129"
FT                   /id="PRO_5010000508"
SQ   SEQUENCE   120 AA;  13573 MW;  1797844C92C9126E CRC64;
     MDYYRKYAAV ILVMLSVFLH ILHSFPDGDF TMQGCPECKL KENKYFSKLG APIYQCMGCC
     FSRAYPTPAR SKKTMLVPKN ITSEATCCVA KAFTKATVMG NARVENHTEC HCSTCYYHKS
//
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