INHBB_HUMAN
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 03-AUG-2022, entry version 192.
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";
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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 AlphaFoldDB; P09529; -.
DR SMR; P09529; -.
DR BioGRID; 109837; 12.
DR IntAct; P09529; 2.
DR STRING; 9606.ENSP00000295228; -.
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; P09529; -.
DR PeptideAtlas; P09529; -.
DR PRIDE; P09529; -.
DR ProteomicsDB; 52243; -.
DR TopDownProteomics; P09529; -.
DR Antibodypedia; 33396; 427 antibodies from 30 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 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; RMDGDFL; -.
DR OrthoDB; 1385831at2759; -.
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 1070 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 129 other tissues.
DR Genevisible; P09529; HS.
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:0010259; P:multicellular organism aging; IEA:Ensembl.
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:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
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:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000381; Inhibin_betaB.
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; PTHR11848; 1.
DR PANTHER; PTHR11848:SF29; PTHR11848:SF29; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Hormone; Reference proteome;
KW 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"
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
