CGB3_HUMAN
ID CGB3_HUMAN Reviewed; 165 AA.
AC P0DN86; A1A5E0; B9ZVP5; P01233; Q13991; Q14000; Q3KPI3; Q3SY41; Q8WTT5;
AC Q8WXL1; Q8WXL2; Q8WXL3; Q8WXL4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Choriogonadotropin subunit beta 3;
DE AltName: Full=Choriogonadotropin subunit beta;
DE Short=CG-beta;
DE AltName: Full=Chorionic gonadotropin chain beta;
DE Flags: Precursor;
GN Name=CGB3; Synonyms=CGB;
GN and
GN Name=CGB5;
GN and
GN Name=CGB8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=6774259; DOI=10.1038/286684a0;
RA Fiddes J.C., Goodman H.M.;
RT "The cDNA for the beta-subunit of human chorionic gonadotropin suggests
RT evolution of a gene by readthrough into the 3'-untranslated region.";
RL Nature 286:684-687(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-137.
RX PubMed=6690982; DOI=10.1038/307037a0;
RA Talmadge K., Vamvakopoulos N.C., Fiddes J.C.;
RT "Evolution of the genes for the beta subunits of human chorionic
RT gonadotropin and luteinizing hormone.";
RL Nature 307:37-40(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-24 AND ALA-137.
RX PubMed=6194155; DOI=10.1016/s0021-9258(17)44254-2;
RA Policastro P., Ovitt C.E., Hoshina M., Fukuoka H., Boothby M.R., Boime I.;
RT "The beta subunit of human chorionic gonadotropin is encoded by multiple
RT genes.";
RL J. Biol. Chem. 258:11492-11499(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-4 AND
RP ALA-137.
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 1-20 (PRECURSOR PROTEIN).
RX PubMed=7462224; DOI=10.1016/s0021-9258(19)69881-9;
RA Birken S., Fetherston J., Canfield R.E., Boime I.;
RT "The amino acid sequences of the prepeptides contained in the alpha and
RT beta subunits of human choriogonadotropin.";
RL J. Biol. Chem. 256:1816-1823(1981).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=2422163; DOI=10.1016/s0021-9258(17)38469-7;
RA Policastro P.F., Daniels-Mcqueen S., Carle G., Boime I.;
RT "A map of the hCG beta-LH beta gene cluster.";
RL J. Biol. Chem. 261:5907-5916(1986).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-164, VARIANTS ALA-18; ARG-22;
RP MET-24; TRP-28; HIS-30; ILE-35; ALA-137 AND CYS-147, AND MISCELLANEOUS.
RX PubMed=11861891; DOI=10.1093/oxfordjournals.molbev.a004085;
RA Maston G.A., Ruvolo M.;
RT "Chorionic gonadotropin has a recent origin within primates and an
RT evolutionary history of selection.";
RL Mol. Biol. Evol. 19:320-335(2002).
RN [12]
RP PROTEIN SEQUENCE OF 21-165.
RX PubMed=1150658; DOI=10.1016/s0021-9258(19)41303-3;
RA Morgan F.J., Birken S., Canfield R.E.;
RT "The amino acid sequence of human chorionic gonadotropin. The alpha subunit
RT and beta subunit.";
RL J. Biol. Chem. 250:5247-5258(1975).
RN [13]
RP PRELIMINARY PROTEIN SEQUENCE OF 21-165.
RX PubMed=4795659; DOI=10.1016/s0021-9258(19)43425-x;
RA Carlsen R.B., Bahl O.P., Swaminathan N.;
RT "Human chorionic gonadotropin. Linear amino acid sequence of the beta
RT subunit.";
RL J. Biol. Chem. 248:6810-6827(1973).
RN [14]
RP PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
RX PubMed=7240231; DOI=10.1016/s0021-9258(19)69030-7;
RA Mise T., Bahl O.P.;
RT "Assignment of disulfide bonds in the beta subunit of human chorionic
RT gonadotropin.";
RL J. Biol. Chem. 256:6587-6592(1981).
RN [15]
RP DISULFIDE BONDS.
RX PubMed=1688430; DOI=10.1016/s0021-9258(19)40231-7;
RA Saccuzo Beebe J., Mountjoy K., Krzesicki R.F., Perini F., Ruddon R.W.;
RT "Role of disulfide bond formation in the folding of human chorionic
RT gonadotropin beta subunit into an alpha beta dimer assembly-competent
RT form.";
RL J. Biol. Chem. 265:312-317(1990).
RN [16]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=1820200; DOI=10.1093/glycob/1.4.393;
RA Weisshaar G., Hiyama J., Renwick A.G.C.;
RT "Site-specific N-glycosylation of human chorionic gonadotrophin
RT -- structural analysis of glycopeptides by one- and two-dimensional 1H NMR
RT spectroscopy.";
RL Glycobiology 1:393-404(1991).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), GLYCOSYLATION AT ASN-33 AND ASN-50,
RP AND SUBUNIT.
RX PubMed=8202136; DOI=10.1038/369455a0;
RA Lapthorn A.J., Harris D.C., Littlejohn A., Lustbader J.W., Canfield R.E.,
RA Machin K.J., Morgan F.J., Isaacs N.W.;
RT "Crystal structure of human chorionic gonadotropin.";
RL Nature 369:455-461(1994).
RN [18]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16123088; DOI=10.1093/humrep/dei261;
RA Rull K., Laan M.;
RT "Expression of beta-subunit of HCG genes during normal and failed
RT pregnancy.";
RL Hum. Reprod. 20:3360-3368(2005).
CC -!- FUNCTION: Beta subunit of the human chorionic gonadotropin (hCG). hCG
CC is a complex glycoprotein composed of two glycosylated subunits alpha
CC and beta which are non-covalently associated. The alpha subunit is
CC identical to those in the pituitary gonadotropin hormones (LH, FSH and
CC TSH). The beta subunits are distinct in each of the hormones and confer
CC receptor and biological specificity. Has an essential role in pregnancy
CC and maternal adaptation. Stimulates the ovaries to synthesize the
CC steroids that are essential for the maintenance of pregnancy.
CC {ECO:0000305}.
CC -!- SUBUNIT: Heterodimer of a common alpha chain identical in LH, FSH, TSH
CC and HCG and a unique beta chain distinct in each of the hormones.
CC {ECO:0000269|PubMed:8202136, ECO:0000305}.
CC -!- INTERACTION:
CC P0DN86; P01215: CGA; NbExp=2; IntAct=EBI-8626304, EBI-718913;
CC P0DN86; P49901: SMCP; NbExp=3; IntAct=EBI-8626304, EBI-750494;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16123088}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DN86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DN86-2; Sequence=VSP_038396;
CC -!- TISSUE SPECIFICITY: High expression in the placenta throughout
CC pregnancy. {ECO:0000269|PubMed:16123088}.
CC -!- DEVELOPMENTAL STAGE: Expressed continuously during the whole pregnancy
CC with a peak during the first trimester. {ECO:0000269|PubMed:16123088}.
CC -!- PHARMACEUTICAL: Available under the names Novarel (Ferring) and Profasi
CC (Serono). Used as adjunctive therapy in the treatment of obesity. There
CC is no substantial evidence that it increases weight loss beyond that
CC resulting from caloric restriction, that it causes a more attractive or
CC 'normal' distribution of fat, or that it decreases the hunger and
CC discomfort associated with calorie-restricted diets.
CC -!- MISCELLANEOUS: Encoded by a cluster of genes that have evolved by
CC duplication from LHB. HCG-beta is encoded by six non-allelic genes
CC (CGB) clustered on chromosome 19q13.3 and named CGB1, CGB2, CGB3, CGB5,
CC CGB7 and CGB8. Two specific hCGb proteins that differ by three amino
CC acids in positions 2,4 and 117 have been described: type 1 (CGB7) and
CC type 2 (CGB3, CGB5, CGB8). The CGB gene first arose in the common
CC ancestor of the anthropoid primates. {ECO:0000269|PubMed:11861891}.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA25069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Chorionic gonadotropin entry;
CC URL="https://en.wikipedia.org/wiki/Human_chorionic_gonadotropin";
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DR EMBL; J00117; AAA96690.1; -; mRNA.
DR EMBL; X00265; CAA25068.1; ALT_INIT; Genomic_DNA.
DR EMBL; X00266; CAA25069.1; ALT_INIT; Genomic_DNA.
DR EMBL; K03189; AAA53288.1; -; Genomic_DNA.
DR EMBL; K03187; AAA53288.1; JOINED; Genomic_DNA.
DR EMBL; K03188; AAA53288.1; JOINED; Genomic_DNA.
DR EMBL; K03183; AAA53287.1; -; Genomic_DNA.
DR EMBL; K00092; AAA53287.1; JOINED; Genomic_DNA.
DR EMBL; K03182; AAA53287.1; JOINED; Genomic_DNA.
DR EMBL; BT006890; AAP35536.1; -; mRNA.
DR EMBL; AK291552; BAF84241.1; -; mRNA.
DR EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52434.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52437.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52438.1; -; Genomic_DNA.
DR EMBL; BC006290; AAH06290.1; -; mRNA.
DR EMBL; BC022796; AAH22796.1; -; mRNA.
DR EMBL; BC030994; AAH30994.1; -; mRNA.
DR EMBL; BC041054; AAH41054.1; -; mRNA.
DR EMBL; BC051378; AAH51378.1; -; mRNA.
DR EMBL; BC069526; AAH69526.1; -; mRNA.
DR EMBL; BC103969; AAI03970.1; -; mRNA.
DR EMBL; BC103970; AAI03971.1; -; mRNA.
DR EMBL; BC103971; AAI03972.1; -; mRNA.
DR EMBL; BC106059; AAI06060.1; -; mRNA.
DR EMBL; BC106723; AAI06724.1; -; mRNA.
DR EMBL; BC106724; AAI06725.1; -; mRNA.
DR EMBL; BC128603; AAI28604.1; -; mRNA.
DR EMBL; M13503; AAA52009.1; -; Genomic_DNA.
DR EMBL; M13504; AAA52005.1; -; Genomic_DNA.
DR EMBL; M13505; AAA52008.1; -; Genomic_DNA.
DR EMBL; AF397576; AAL69704.1; -; Genomic_DNA.
DR EMBL; AF397577; AAL69705.1; -; Genomic_DNA.
DR EMBL; AF397578; AAL69706.1; -; Genomic_DNA.
DR EMBL; AF397579; AAL69707.1; -; Genomic_DNA.
DR EMBL; AF397580; AAL69708.1; -; Genomic_DNA.
DR EMBL; AF397581; AAL69709.1; -; Genomic_DNA.
DR CCDS; CCDS12749.1; -. [P0DN86-1]
DR PIR; A93230; KTHUB.
DR PIR; I37231; I37231.
DR RefSeq; NP_000728.1; NM_000737.3. [P0DN86-1]
DR RefSeq; NP_149032.1; NM_033043.1. [P0DN86-1]
DR RefSeq; NP_149439.1; NM_033183.2. [P0DN86-1]
DR PDB; 1HCN; X-ray; 2.60 A; B=21-165.
DR PDB; 1HRP; X-ray; 3.00 A; B=21-165.
DR PDB; 1QFW; X-ray; 3.50 A; B=21-165.
DR PDB; 7FIG; EM; 3.90 A; Y=1-165.
DR PDB; 7FIH; EM; 3.20 A; Y=1-165.
DR PDB; 7FII; EM; 4.30 A; Y=1-165.
DR PDBsum; 1HCN; -.
DR PDBsum; 1HRP; -.
DR PDBsum; 1QFW; -.
DR PDBsum; 7FIG; -.
DR PDBsum; 7FIH; -.
DR PDBsum; 7FII; -.
DR AlphaFoldDB; P0DN86; -.
DR SMR; P0DN86; -.
DR ComplexPortal; CPX-748; Chorionic gonadotropin hormone complex.
DR IntAct; P0DN86; 5.
DR STRING; 9606.ENSP00000301408; -.
DR GlyConnect; 88; 12 N-Linked glycans, 9 O-Linked glycans.
DR GlyConnect; 91; 9 N-Linked glycans (2 sites), 6 O-Linked glycans.
DR GlyGen; P0DN86; 7 sites, 28 N-linked glycans (3 sites), 15 O-linked glycans (5 sites).
DR iPTMnet; P0DN86; -.
DR PhosphoSitePlus; P0DN86; -.
DR BioMuta; CGB5; -.
DR MassIVE; P0DN86; -.
DR MaxQB; P0DN86; -.
DR PeptideAtlas; P0DN86; -.
DR PRIDE; P0DN86; -.
DR ABCD; P0DN86; 6 sequenced antibodies.
DR Antibodypedia; 4392; 2118 antibodies from 40 providers.
DR Antibodypedia; 74544; 114 antibodies from 13 providers.
DR Antibodypedia; 76402; 28 antibodies from 4 providers.
DR CPTC; P0DN86; 10 antibodies.
DR DNASU; 1082; -.
DR Ensembl; ENST00000301408.7; ENSP00000301408.5; ENSG00000189052.7. [P0DN86-1]
DR Ensembl; ENST00000357383.4; ENSP00000349954.2; ENSG00000104827.12. [P0DN86-1]
DR Ensembl; ENST00000448456.4; ENSP00000403649.2; ENSG00000213030.6. [P0DN86-1]
DR GeneID; 1082; -.
DR GeneID; 93659; -.
DR GeneID; 94115; -.
DR KEGG; hsa:1082; -.
DR KEGG; hsa:93659; -.
DR KEGG; hsa:94115; -.
DR MANE-Select; ENST00000301408.7; ENSP00000301408.5; NM_033043.2; NP_149032.1.
DR MANE-Select; ENST00000357383.4; ENSP00000349954.2; NM_000737.5; NP_000728.1.
DR MANE-Select; ENST00000448456.4; ENSP00000403649.2; NM_033183.3; NP_149439.1.
DR CTD; 1082; -.
DR CTD; 93659; -.
DR CTD; 94115; -.
DR DisGeNET; 1082; -.
DR DisGeNET; 93659; -.
DR DisGeNET; 94115; -.
DR GeneCards; CGB3; -.
DR GeneCards; CGB5; -.
DR GeneCards; CGB8; -.
DR HGNC; HGNC:1886; CGB3.
DR HGNC; HGNC:16452; CGB5.
DR HGNC; HGNC:16453; CGB8.
DR HPA; ENSG00000104827; Tissue enriched (placenta).
DR HPA; ENSG00000189052; Group enriched (pituitary gland, placenta).
DR HPA; ENSG00000213030; Tissue enriched (placenta).
DR MIM; 118860; gene.
DR MIM; 608825; gene.
DR MIM; 608827; gene.
DR neXtProt; NX_P0DN86; -.
DR OpenTargets; ENSG00000189052; -.
DR OpenTargets; ENSG00000213030; -.
DR VEuPathDB; HostDB:ENSG00000104827; -.
DR VEuPathDB; HostDB:ENSG00000189052; -.
DR VEuPathDB; HostDB:ENSG00000213030; -.
DR GeneTree; ENSGT00940000163162; -.
DR OMA; GPCRLSN; -.
DR PhylomeDB; P0DN86; -.
DR PathwayCommons; P0DN86; -.
DR Reactome; R-HSA-209822; Glycoprotein hormones.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR SignaLink; P0DN86; -.
DR BioGRID-ORCS; 1082; 21 hits in 186 CRISPR screens.
DR BioGRID-ORCS; 93659; 23 hits in 560 CRISPR screens.
DR BioGRID-ORCS; 94115; 14 hits in 208 CRISPR screens.
DR ChiTaRS; CGB8; human.
DR Pharos; P0DN86; Tdark.
DR PRO; PR:P0DN86; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0DN86; protein.
DR Bgee; ENSG00000104827; Expressed in placenta and 46 other tissues.
DR ExpressionAtlas; P0DN86; baseline and differential.
DR Genevisible; P01233; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0061696; C:pituitary gonadotropin complex; IPI:ComplexPortal.
DR GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00069; GHB_like; 1.
DR DisProt; DP00013; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hormone; Pharmaceutical; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1150658,
FT ECO:0000269|PubMed:6774259"
FT CHAIN 21..165
FT /note="Choriogonadotropin subunit beta 3"
FT /id="PRO_0000011676"
FT REGION 131..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:1HRP"
FT /id="CAR_000042"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:1HRP"
FT /id="CAR_000043"
FT CARBOHYD 141
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1150658"
FT CARBOHYD 147
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1150658"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1150658"
FT CARBOHYD 158
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1150658"
FT DISULFID 29..77
FT /evidence="ECO:0000269|PubMed:1688430,
FT ECO:0000269|PubMed:8202136"
FT DISULFID 43..92
FT /evidence="ECO:0000269|PubMed:1688430,
FT ECO:0000269|PubMed:8202136"
FT DISULFID 46..130
FT /evidence="ECO:0000269|PubMed:1688430,
FT ECO:0000269|PubMed:8202136"
FT DISULFID 54..108
FT /evidence="ECO:0000269|PubMed:1688430,
FT ECO:0000269|PubMed:8202136"
FT DISULFID 58..110
FT /evidence="ECO:0000269|PubMed:1688430,
FT ECO:0000269|PubMed:8202136"
FT DISULFID 113..120
FT /evidence="ECO:0000269|PubMed:1688430,
FT ECO:0000269|PubMed:8202136"
FT VAR_SEQ 1..4
FT /note="MEMF -> MGRPGLGAAVSDPGEAVSLS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038396"
FT VARIANT 4
FT /note="F -> L (in dbSNP:rs767100833 and dbSNP:rs371475564)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_014585"
FT VARIANT 18
FT /note="T -> A (in dbSNP:rs201240617)"
FT /evidence="ECO:0000269|PubMed:11861891"
FT /id="VAR_015231"
FT VARIANT 22
FT /note="K -> R (in dbSNP:rs201575305 and dbSNP:rs199720009)"
FT /evidence="ECO:0000269|PubMed:11861891"
FT /id="VAR_014586"
FT VARIANT 24
FT /note="P -> M (requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11861891,
FT ECO:0000269|PubMed:6194155"
FT /id="VAR_015232"
FT VARIANT 28
FT /note="R -> W (in dbSNP:rs1261895475)"
FT /evidence="ECO:0000269|PubMed:11861891"
FT /id="VAR_015233"
FT VARIANT 30
FT /note="R -> H (in dbSNP:rs201373221)"
FT /evidence="ECO:0000269|PubMed:11861891"
FT /id="VAR_015234"
FT VARIANT 35
FT /note="T -> I (in dbSNP:rs201780746 and dbSNP:rs199824672)"
FT /evidence="ECO:0000269|PubMed:11861891"
FT /id="VAR_014587"
FT VARIANT 137
FT /note="D -> A (in dbSNP:rs200199557 and dbSNP:rs199614255)"
FT /evidence="ECO:0000269|PubMed:11861891,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:6194155,
FT ECO:0000269|PubMed:6690982"
FT /id="VAR_003188"
FT VARIANT 147
FT /note="S -> C"
FT /evidence="ECO:0000269|PubMed:11861891"
FT /id="VAR_015235"
FT CONFLICT 123
FT /note="P -> T (in Ref. 11; AAL69709)"
FT /evidence="ECO:0000305"
FT STRAND 25..38
FT /evidence="ECO:0007829|PDB:1HCN"
FT STRAND 47..60
FT /evidence="ECO:0007829|PDB:1HCN"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 75..88
FT /evidence="ECO:0007829|PDB:1HCN"
FT STRAND 99..112
FT /evidence="ECO:0007829|PDB:1HCN"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1HCN"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1HCN"
FT CONFLICT P0DN86-2:7
FT /note="G -> R (in Ref. 2; CAA25069)"
FT /evidence="ECO:0000305"
FT CONFLICT P0DN86-2:9
FT /note="A -> V (in Ref. 2; CAA25069)"
FT /evidence="ECO:0000305"
FT CONFLICT P0DN86-2:12
FT /note="D -> G (in Ref. 2; CAA25069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 17739 MW; 5598FB9E51A05748 CRC64;
MEMFQGLLLL LLLSMGGTWA SKEPLRPRCR PINATLAVEK EGCPVCITVN TTICAGYCPT
MTRVLQGVLP ALPQVVCNYR DVRFESIRLP GCPRGVNPVV SYAVALSCQC ALCRRSTTDC
GGPKDHPLTC DDPRFQDSSS SKAPPPSLPS PSRLPGPSDT PILPQ
