CGHB_SAIBB
ID CGHB_SAIBB Reviewed; 163 AA.
AC Q3S2X5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Choriogonadotropin subunit beta;
DE Short=CG-beta;
DE AltName: Full=Chorionic gonadotrophin chain beta;
DE Flags: Precursor;
GN Name=CGB;
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17897645; DOI=10.1016/j.ygcen.2007.08.004;
RA Scammell J.G., Funkhouser J.D., Moyer F.S., Gibson S.V., Willis D.L.;
RT "Molecular cloning of pituitary glycoprotein alpha-subunit and follicle
RT stimulating hormone and chorionic gonadotropin beta-subunits from New World
RT squirrel monkey and owl monkey.";
RL Gen. Comp. Endocrinol. 155:534-541(2008).
CC -!- FUNCTION: Stimulates the ovaries to synthesize the steroids that are
CC essential for the maintenance of pregnancy. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
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DR EMBL; DQ174773; ABA00515.1; -; mRNA.
DR AlphaFoldDB; Q3S2X5; -.
DR SMR; Q3S2X5; -.
DR STRING; 39432.ENSSBOP00000040430; -.
DR Ensembl; ENSSBOT00000057397; ENSSBOP00000040431; ENSSBOG00000036196.
DR GeneTree; ENSGT00940000163162; -.
DR OMA; GPCRLSN; -.
DR Proteomes; UP000233220; Unplaced.
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.
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..163
FT /note="Choriogonadotropin subunit beta"
FT /id="PRO_0000253469"
FT REGION 135..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
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 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 29..76
FT /evidence="ECO:0000250"
FT DISULFID 43..91
FT /evidence="ECO:0000250"
FT DISULFID 46..129
FT /evidence="ECO:0000250"
FT DISULFID 54..107
FT /evidence="ECO:0000250"
FT DISULFID 58..109
FT /evidence="ECO:0000250"
FT DISULFID 112..119
FT /evidence="ECO:0000250"
SQ SEQUENCE 163 AA; 17704 MW; D213E57E9616B27C CRC64;
MEMLQGLLLC LLLSTGGAWA SKEPLRPPCR PTNVILAVEK EGCPVCVPFN TTICAGYCSS
MVRVMQTLPP LPQTVCNYHE LRFTSVRLPG CRRGVDPVVY MPMAVSCRCA LCRRSYSDCG
SFRNESLGCD YATSQDSSSN VPPSNLTSPS QLLEPAVTPL VPQ
