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 02-SEP-2026, entry version 61. 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"; 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; 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_000737.5. [P0DN86-1] DR RefSeq; NP_149032.1; NM_033043.2. [P0DN86-1] DR RefSeq; NP_149439.1; NM_033183.3. [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 PDB; 9RHU; EM; 2.65 A; G2=21-93, G2=96-151. DR AlphaFoldDB; P0DN86; -. DR EMDB; EMD-31596; -. DR EMDB; EMD-31597; -. DR EMDB; EMD-31598; -. DR SMR; P0DN86; -. DR ComplexPortal; CPX-748; Chorionic gonadotropin hormone complex. DR FunCoup; P0DN86; 49. DR IntAct; P0DN86; 12. DR MINT; P0DN86; -. DR STRING; 9606.ENSP00000301408; -. DR GlyConnect; P0DN86; 55 N-Linked glycans (2 sites), 6 O-Linked glycans. DR GlyCosmos; P0DN86; 6 sites, 43 glycans. DR GlyGen; P0DN86; 9 sites, 28 N-linked glycans (3 sites), 16 O-linked glycans (5 sites). DR iPTMnet; P0DN86; -. DR PhosphoSitePlus; P0DN86; -. DR BioMuta; CGB5; -. DR jPOST; P0DN86; -. DR MassIVE; P0DN86; -. DR PaxDb; 9606-ENSP00000301408; -. DR PeptideAtlas; P0DN86; -. DR ABCD; P0DN86; 6 sequenced antibodies. DR Antibodypedia; 4392; 2202 antibodies from 39 providers. DR Antibodypedia; 74544; 112 antibodies from 11 providers. DR Antibodypedia; 76402; 30 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; ENSG00000213030.7. [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 AGR; HGNC:16452; -. DR AGR; HGNC:16453; -. DR AGR; HGNC:1886; -. 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 enhanced (pancreas, pituitary gland, placenta). DR HPA; ENSG00000189052; Group enriched (pituitary gland, placenta). DR HPA; ENSG00000213030; Group enriched (pituitary gland, placenta). DR MIM; 118860; gene. DR MIM; 608825; gene. DR MIM; 608827; gene. DR OpenTargets; ENSG00000189052; -. DR OpenTargets; ENSG00000213030; -. DR VEuPathDB; HostDB:ENSG00000104827; -. DR VEuPathDB; HostDB:ENSG00000189052; -. DR VEuPathDB; HostDB:ENSG00000213030; -. DR GeneTree; ENSGT00940000163162; -. DR InParanoid; P0DN86; -. DR OMA; MGRTWAS; -. DR OrthoDB; 9525526at2759; -. DR PAN-GO; P0DN86; 3 GO annotations based on evolutionary models. 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 Agora; ENSG00000104827; -. DR Agora; ENSG00000189052; -. DR BioGRID-ORCS; 1082; 25 hits in 222 CRISPR screens. DR BioGRID-ORCS; 93659; 29 hits in 598 CRISPR screens. DR BioGRID-ORCS; 94115; 21 hits in 244 CRISPR screens. DR ChiTaRS; CGB8; human. DR EvolutionaryTrace; P0DN86; -. DR Pharos; P0DN86; Tbio. DR PRO; PR:P0DN86; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P0DN86; protein. DR Bgee; ENSG00000104827; Expressed in placenta and 48 other cell types or tissues. DR ExpressionAtlas; P0DN86; baseline and differential. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0061696; C:pituitary gonadotropin complex; IPI:ComplexPortal. DR GO; GO:0005179; F:hormone activity; IBA:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-ARBA. 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; NAS:ComplexPortal. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00069; GHB_like; 1. DR DisProt; DP00013; -. DR FunFam; 2.10.90.10:FF:000007; Luteinizing hormone beta subunit; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 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:SF25; CHORIOGONADOTROPIN SUBUNIT BETA 3-RELATED; 1. DR PANTHER; PTHR11515; GLYCOPROTEIN HORMONE BETA CHAIN; 1. DR Pfam; PF00007; Cys_knot; 1. DR SMART; SM00068; GHB; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 1. DR PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1. DR PROSITE; PS00689; GLYCO_HORMONE_BETA_2; 1. DR PDBsum; 1HCN; -. DR PDBsum; 1HRP; -. DR PDBsum; 1QFW; -. DR PDBsum; 7FIG; -. DR PDBsum; 7FIH; -. DR PDBsum; 7FII; -. DR PDBsum; 9RHU; -. 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 143..154 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 HELIX 70..73 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 //