INHBB_MOUSE
ID INHBB_MOUSE Reviewed; 411 AA.
AC Q04999; Q3V1N0; Q61277; Q80VC4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Inhibin beta B chain;
DE AltName: Full=Activin beta-B chain;
DE Flags: Precursor;
GN Name=Inhbb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-411.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 157-390.
RC STRAIN=CBA X NMRI; TISSUE=Testis;
RX PubMed=7619733; DOI=10.1016/0925-4773(94)00342-k;
RA Ritvos O., Tuuri T., Eramaa M., Sainio K., Hilden K., Saxen L., Gilbert S.;
RT "Activin disrupts epithelial branching morphogenesis in developing
RT glandular organs of the mouse.";
RL Mech. Dev. 50:229-245(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 290-411.
RX PubMed=8330535; DOI=10.1242/dev.117.2.711;
RA Albano P.M., Groome N., Smith J.C.;
RT "Activins are expressed in preimplantation mouse embryos and in ES and EC
RT cells and are regulated on their differentiation.";
RL Development 117:711-723(1993).
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: Homo- or heterodimer; disulfide-linked. Inhibin A is a dimer
CC of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin
CC A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin
CC AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Uterus, testis, ovary, lung, kidney, brain, CJ7
CC embryonic stem cells, and possibly in liver.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AK132352; BAE21120.1; -; mRNA.
DR EMBL; BC048845; AAH48845.1; -; mRNA.
DR EMBL; X83376; CAA58290.1; -; mRNA.
DR EMBL; X69620; CAA49326.1; -; mRNA.
DR CCDS; CCDS15224.1; -.
DR PIR; I48235; I48235.
DR RefSeq; NP_032407.1; NM_008381.4.
DR AlphaFoldDB; Q04999; -.
DR SMR; Q04999; -.
DR BioGRID; 200763; 2.
DR STRING; 10090.ENSMUSP00000044918; -.
DR GlyGen; Q04999; 1 site.
DR PhosphoSitePlus; Q04999; -.
DR PaxDb; Q04999; -.
DR PeptideAtlas; Q04999; -.
DR PRIDE; Q04999; -.
DR ProteomicsDB; 269315; -.
DR Antibodypedia; 33396; 427 antibodies from 30 providers.
DR DNASU; 16324; -.
DR Ensembl; ENSMUST00000038765; ENSMUSP00000044918; ENSMUSG00000037035.
DR GeneID; 16324; -.
DR KEGG; mmu:16324; -.
DR UCSC; uc007cir.1; mouse.
DR CTD; 3625; -.
DR MGI; MGI:96571; Inhbb.
DR VEuPathDB; HostDB:ENSMUSG00000037035; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000159862; -.
DR HOGENOM; CLU_020515_5_1_1; -.
DR InParanoid; Q04999; -.
DR OMA; RMDGDFL; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; Q04999; -.
DR TreeFam; TF351791; -.
DR Reactome; R-MMU-1502540; Signaling by Activin.
DR Reactome; R-MMU-209822; Glycoprotein hormones.
DR Reactome; R-MMU-2473224; Antagonism of Activin by Follistatin.
DR BioGRID-ORCS; 16324; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Inhbb; mouse.
DR PRO; PR:Q04999; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q04999; protein.
DR Bgee; ENSMUSG00000037035; Expressed in uterine cervix and 166 other tissues.
DR Genevisible; Q04999; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
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; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IEP: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:0001654; P:eye development; TAS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0032686; P:negative regulation of hepatocyte growth factor production; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR GO; GO:0048599; P:oocyte development; IGI:MGI.
DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP: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; ISS: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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Growth factor; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..296
FT /evidence="ECO:0000255"
FT /id="PRO_0000033724"
FT CHAIN 297..411
FT /note="Inhibin beta B chain"
FT /id="PRO_0000033725"
FT REGION 28..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 300..308
FT /evidence="ECO:0000250"
FT DISULFID 307..376
FT /evidence="ECO:0000250"
FT DISULFID 336..408
FT /evidence="ECO:0000250"
FT DISULFID 340..410
FT /evidence="ECO:0000250"
FT DISULFID 375
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 291
FT /note="H -> D (in Ref. 4; CAA49326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45211 MW; 345F6919F583BC49 CRC64;
MDGLPGRALG AACLLLLVAG WLGPEAWGSP TPPPSPAAPP PPPPPGAPGG SQDTCTSCGG
GGGGFRRPEE LGRVDGDFLE AVKRHILSRL QLRGRPNITH AVPKAAMVTA LRKLHAGKVR
EDGRVEIPHL DGHASPGADG QERVSEIISF AETDGLASSR VRLYFFVSNE GNQNLFVVQA
SLWLYLKLLP YVLEKGSRRK VRVKVYFQEQ GHGDRWNVVE KKVDLKRSGW HTFPITEAIQ
ALFERGERRL NLDVQCDSCQ ELAVVPVFVD PGEESHRPFV VVQARLGDSR HRIRKRGLEC
DGRTSLCCRQ QFFIDFRLIG WNDWIIAPTG YYGNYCEGSC PAYLAGVPGS ASSFHTAVVN
QYRMRGLNPG PVNSCCIPTK LSSMSMLYFD DEYNIVKRDV PNMIVEECGC A
