ID INHBB_HUMAN Reviewed; 407 AA. AC P09529; Q53T31; Q8N1D3; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 24-JAN-2024, entry version 200. DE RecName: Full=Inhibin beta B chain; DE AltName: Full=Activin beta-B chain; DE Flags: Precursor; GN Name=INHBB; 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 [GENOMIC DNA]. RX PubMed=2575216; DOI=10.1210/mend-3-9-1352; RA Mason A.J., Berkemeier L.M., Schmelzer C.H., Schwall R.H.; RT "Activin B: precursor sequences, genomic structure and in vitro RT activities."; RL Mol. Endocrinol. 3:1352-1358(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-407. RX PubMed=2739657; DOI=10.1210/mend-3-6-939; RA Feng Z.M., Bardin C.W., Chen C.L.; RT "Characterization and regulation of testicular inhibin beta-subunit mRNA."; RL Mol. Endocrinol. 3:939-948(1989). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-407. RX PubMed=3754442; DOI=10.1016/0006-291x(86)91021-1; RA Mason A.J., Niall H.D., Seeburg P.H.; RT "Structure of two human ovarian inhibins."; RL Biochem. Biophys. Res. Commun. 135:957-964(1986). RN [7] RP PROTEIN SEQUENCE OF 293-307. RX PubMed=2364091; DOI=10.1016/0167-4838(90)90178-i; RA Schmelzer C.H., Burton L.E., Tamony C.M., Schwall R.H., Mason A.J., RA Liegeois N.; RT "Purification and characterization of recombinant human activin B."; RL Biochim. Biophys. Acta 1039:135-141(1990). RN [8] RP INTERACTION WITH FST AND FSTL3. RX PubMed=12697670; DOI=10.1210/en.2002-0203; RA Schneyer A., Schoen A., Quigg A., Sidis Y.; RT "Differential binding and neutralization of activins A and B by follistatin RT and follistatin like-3 (FSTL-3/FSRP/FLRG)."; RL Endocrinology 144:1671-1674(2003). CC -!- FUNCTION: Inhibins and activins inhibit and activate, respectively, the CC secretion of follitropin by the pituitary gland. Inhibins/activins are CC involved in regulating a number of diverse functions such as CC hypothalamic and pituitary hormone secretion, gonadal hormone CC secretion, germ cell development and maturation, erythroid CC differentiation, insulin secretion, nerve cell survival, embryonic CC axial development or bone growth, depending on their subunit CC composition. Inhibins appear to oppose the functions of activins. CC -!- SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A is a CC dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. CC Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. CC Activin AB is a dimer of beta-A and beta-B. Interacts with FST and CC FSTL3. {ECO:0000269|PubMed:12697670}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Inhibin entry; CC URL="https://en.wikipedia.org/wiki/Inhibin"; 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; M31669; AAA59451.1; -; Genomic_DNA. DR EMBL; M31668; AAA59451.1; JOINED; Genomic_DNA. DR EMBL; AC012363; AAY14801.1; -; Genomic_DNA. DR EMBL; CH471103; EAW95243.1; -; Genomic_DNA. DR EMBL; BC030029; AAH30029.1; -; mRNA. DR EMBL; M31682; AAA59170.1; -; mRNA. DR EMBL; M13437; AAA59169.1; -; mRNA. DR CCDS; CCDS2132.1; -. DR PIR; A40150; A40150. DR RefSeq; NP_002184.2; NM_002193.3. DR PDB; 7U5O; X-ray; 3.45 A; A/B/C=293-407. DR PDBsum; 7U5O; -. DR AlphaFoldDB; P09529; -. DR SMR; P09529; -. DR BioGRID; 109837; 12. DR IntAct; P09529; 2. DR STRING; 9606.ENSP00000295228; -. DR GlyCosmos; P09529; 3 sites, 1 glycan. DR GlyGen; P09529; 4 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P09529; -. DR PhosphoSitePlus; P09529; -. DR BioMuta; INHBB; -. DR DMDM; 1708437; -. DR MassIVE; P09529; -. DR MaxQB; P09529; -. DR PaxDb; 9606-ENSP00000295228; -. DR PeptideAtlas; P09529; -. DR ProteomicsDB; 52243; -. DR TopDownProteomics; P09529; -. DR Antibodypedia; 33396; 483 antibodies from 31 providers. DR DNASU; 3625; -. DR Ensembl; ENST00000295228.4; ENSP00000295228.3; ENSG00000163083.6. DR GeneID; 3625; -. DR KEGG; hsa:3625; -. DR MANE-Select; ENST00000295228.4; ENSP00000295228.3; NM_002193.4; NP_002184.2. DR UCSC; uc002tmn.3; human. DR AGR; HGNC:6067; -. DR CTD; 3625; -. DR DisGeNET; 3625; -. DR GeneCards; INHBB; -. DR HGNC; HGNC:6067; INHBB. DR HPA; ENSG00000163083; Tissue enhanced (adipose tissue, breast). DR MIM; 147390; gene. DR neXtProt; NX_P09529; -. DR OpenTargets; ENSG00000163083; -. DR PharmGKB; PA29878; -. DR VEuPathDB; HostDB:ENSG00000163083; -. DR eggNOG; KOG3900; Eukaryota. DR GeneTree; ENSGT00940000159862; -. DR HOGENOM; CLU_020515_5_1_1; -. DR InParanoid; P09529; -. DR OMA; DIQCEGC; -. DR OrthoDB; 3015718at2759; -. DR PhylomeDB; P09529; -. DR TreeFam; TF351791; -. DR PathwayCommons; P09529; -. DR Reactome; R-HSA-1502540; Signaling by Activin. DR Reactome; R-HSA-209822; Glycoprotein hormones. DR Reactome; R-HSA-2473224; Antagonism of Activin by Follistatin. DR SignaLink; P09529; -. DR BioGRID-ORCS; 3625; 16 hits in 1148 CRISPR screens. DR GeneWiki; INHBB; -. DR GenomeRNAi; 3625; -. DR Pharos; P09529; Tbio. DR PRO; PR:P09529; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P09529; Protein. DR Bgee; ENSG00000163083; Expressed in endometrium epithelium and 131 other cell types or tissues. DR GO; GO:0071944; C:cell periphery; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0005179; F:hormone activity; TAS:UniProtKB. DR GO; GO:0046789; F:host cell surface receptor binding; TAS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0032924; P:activin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB. DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB. DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl. DR GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl. DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB. DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl. DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl. DR GO; GO:0006952; P:defense response; TAS:UniProtKB. DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB. DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; IPI:UniProtKB. DR GO; GO:0032686; P:negative regulation of hepatocyte growth factor production; IDA:UniProtKB. DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB. DR GO; GO:0048599; P:oocyte development; IEA:Ensembl. DR GO; GO:0001541; P:ovarian follicle development; NAS:UniProtKB. DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IPI:UniProtKB. DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB. DR GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl. DR GO; GO:0017085; P:response to insecticide; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB. DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd19405; TGF_beta_INHBB; 1. DR Gene3D; 2.60.120.970; -; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR000381; INHBB_C. DR InterPro; IPR001839; TGF-b_C. DR InterPro; IPR001111; TGF-b_propeptide. DR InterPro; IPR015615; TGF-beta-rel. DR InterPro; IPR017948; TGFb_CS. DR PANTHER; PTHR11848:SF29; INHIBIN BETA B CHAIN; 1. DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1. DR Pfam; PF00019; TGF_beta; 1. DR Pfam; PF00688; TGFb_propeptide; 1. DR PRINTS; PR00671; INHIBINBB. DR SMART; SM00204; TGFB; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 1. DR PROSITE; PS00250; TGF_BETA_1; 1. DR PROSITE; PS51362; TGF_BETA_2; 1. DR Genevisible; P09529; HS. PE 1: Evidence at protein level; KW 3D-structure; Cleavage on pair of basic residues; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor; KW Hormone; Reference proteome; Secreted; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT PROPEP 29..292 FT /evidence="ECO:0000255" FT /id="PRO_0000033722" FT CHAIN 293..407 FT /note="Inhibin beta B chain" FT /id="PRO_0000033723" FT REGION 26..62 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 27..49 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 93 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 296..304 FT /evidence="ECO:0000250" FT DISULFID 303..372 FT /evidence="ECO:0000250" FT DISULFID 332..404 FT /evidence="ECO:0000250" FT DISULFID 336..406 FT /evidence="ECO:0000250" FT DISULFID 371 FT /note="Interchain" FT /evidence="ECO:0000250" FT CONFLICT 39 FT /note="P -> Q (in Ref. 4; AAH30029)" FT /evidence="ECO:0000305" FT CONFLICT 47 FT /note="S -> A (in Ref. 5; AAA59170)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="E -> G (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="G -> S (in Ref. 4; AAH30029)" FT /evidence="ECO:0000305" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:7U5O" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:7U5O" FT TURN 312..316 FT /evidence="ECO:0007829|PDB:7U5O" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:7U5O" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:7U5O" FT STRAND 325..328 FT /evidence="ECO:0007829|PDB:7U5O" FT STRAND 331..335 FT /evidence="ECO:0007829|PDB:7U5O" FT HELIX 347..360 FT /evidence="ECO:0007829|PDB:7U5O" FT STRAND 372..385 FT /evidence="ECO:0007829|PDB:7U5O" FT STRAND 391..406 FT /evidence="ECO:0007829|PDB:7U5O" SQ SEQUENCE 407 AA; 45122 MW; 90316C83597BA6B4 CRC64; MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPTPAAPP PPPPPGSPGG SQDTCTSCGG FRRPEELGRV DGDFLEAVKR HILSRLQMRG RPNITHAVPK AAMVTALRKL HAGKVREDGR VEIPHLDGHA SPGADGQERV SEIISFAETD GLASSRVRLY FFISNEGNQN LFVVQASLWL YLKLLPYVLE KGSRRKVRVK VYFQEQGHGD RWNMVEKRVD LKRSGWHTFP LTEAIQALFE RGERRLNLDV QCDSCQELAV VPVFVDPGEE SHRPFVVVQA RLGDSRHRIR KRGLECDGRT NLCCRQQFFI DFRLIGWNDW IIAPTGYYGN YCEGSCPAYL AGVPGSASSF HTAVVNQYRM RGLNPGTVNS CCIPTKLSTM SMLYFDDEYN IVKRDVPNMI VEECGCA //