CGHB_CALJA
ID CGHB_CALJA Reviewed; 164 AA.
AC P51500;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Choriogonadotropin subunit beta;
DE Short=CG-beta;
DE AltName: Full=Chorionic gonadotrophin chain beta;
DE Flags: Precursor;
GN Name=CGB;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7492691; DOI=10.1095/biolreprod53.2.380;
RA Simula A.P., Amato F., Faast R., Lopata A., Berka J., Norman R.J.;
RT "Luteinizing hormone/chorionic gonadotropin bioactivity in the common
RT marmoset (Callithrix jacchus) is due to a chorionic gonadotropin molecule
RT with a structure intermediate between human chorionic gonadotropin and
RT human luteinizing hormone.";
RL Biol. Reprod. 53:380-389(1995).
CC -!- FUNCTION: Stimulates the ovaries to synthesize the steroids that are
CC essential for the maintenance of pregnancy.
CC -!- SUBUNIT: Heterodimer of a common alpha chain and a unique beta chain
CC which confers biological specificity to thyrotropin, lutropin,
CC follitropin and gonadotropin.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Placenta.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
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DR EMBL; U04447; AAC00029.1; -; mRNA.
DR AlphaFoldDB; P51500; -.
DR SMR; P51500; -.
DR STRING; 9483.ENSCJAP00000044447; -.
DR Ensembl; ENSCJAT00000000391; ENSCJAP00000000359; ENSCJAG00000000216.
DR eggNOG; ENOG502S49V; Eukaryota.
DR GeneTree; ENSGT00940000163162; -.
DR InParanoid; P51500; -.
DR OrthoDB; 1362225at2759; -.
DR Proteomes; UP000008225; Chromosome 22.
DR Bgee; ENSCJAG00000000216; Expressed in frontal cortex and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR CDD; cd00069; GHB_like; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR001545; Gonadotropin_bsu.
DR InterPro; IPR018245; Gonadotropin_bsu_CS.
DR PANTHER; PTHR11515; PTHR11515; 1.
DR Pfam; PF00007; Cys_knot; 1.
DR SMART; SM00068; GHB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1.
DR PROSITE; PS00689; GLYCO_HORMONE_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..164
FT /note="Choriogonadotropin subunit beta"
FT /id="PRO_0000011675"
FT REGION 135..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 29..77
FT /evidence="ECO:0000250"
FT DISULFID 43..92
FT /evidence="ECO:0000250"
FT DISULFID 46..130
FT /evidence="ECO:0000250"
FT DISULFID 54..108
FT /evidence="ECO:0000250"
FT DISULFID 58..110
FT /evidence="ECO:0000250"
FT DISULFID 113..120
FT /evidence="ECO:0000250"
SQ SEQUENCE 164 AA; 17713 MW; 0CD92EDDC2618FA6 CRC64;
MEMLQGLLLC LLLSTGGAWA SKEPLRPLCR PVNAILAAEK EGCPVCVAFN TTICAGYCSS
MVRVLQTILP PLPQSVCNYH ELRFTSVRLP GCRPGVDPVV SMPVALSCRC GLCRRSYSDC
GSLRNEPLGC DYSTFQDSSS KDPPRNLTSP SQLLEPADPP LVPQ
