INHBB_RAT
ID INHBB_RAT Reviewed; 411 AA.
AC P17491; Q8K471;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Inhibin beta B chain;
DE AltName: Full=Activin beta-B chain;
DE Flags: Precursor;
GN Name=Inhbb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 1-174.
RC TISSUE=Liver;
RX PubMed=2628729; DOI=10.1210/mend-3-12-1914;
RA Feng Z.-M., Li Y.-P., Chen C.-L.C.;
RT "Analysis of the 5'-flanking regions of rat inhibin alpha- and beta-B-
RT subunit genes suggests two different regulatory mechanisms.";
RL Mol. Endocrinol. 3:1914-1925(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-7.
RC TISSUE=Granulocyte;
RX PubMed=8033818; DOI=10.1210/endo.135.2.8033818;
RA Dykema J.C., Mayo K.E.;
RT "Two messenger ribonucleic acids encoding the common beta B-chain of
RT inhibin and activin have distinct 5'-initiation sites and are
RT differentially regulated in rat granulosa cells.";
RL Endocrinology 135:702-711(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 133-411, AND VARIANT BETA-B20 HIS-270.
RC TISSUE=Ovary;
RX PubMed=2484214; DOI=10.1210/mend-1-5-388;
RA Esch F.S., Shimasaki S., Cooksey K., Mercado M., Mason A.J., Ying S.-Y.,
RA Ueno N., Ling N.;
RT "Complementary deoxyribonucleic acid (cDNA) cloning and DNA sequence
RT analysis of rat ovarian inhibins.";
RL Mol. Endocrinol. 1:388-396(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 158-266.
RC STRAIN=Wistar; TISSUE=Thyroid;
RX PubMed=12729472; DOI=10.1089/105072503321582033;
RA Matsuo S.E., Ebina K.N., Kulcsar M.A., Friguglietti C.U., Kimura E.T.;
RT "Activin betaB expression in rat experimental goiter and human thyroid
RT tumors.";
RL Thyroid 13:239-247(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: Homodimer or heterodimer; disulfide-linked. 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Alpha- and beta-B subunits are the predominant
CC forms found in rat testis. Also expressed in ovary.
CC -!- INDUCTION: Increased expression in methimazole-induced goiter.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; M32757; AAA41438.1; -; Genomic_DNA.
DR EMBL; M32756; AAA41438.1; JOINED; Genomic_DNA.
DR EMBL; AF478684; AAM46787.1; -; mRNA.
DR PIR; B41398; B41398.
DR RefSeq; NP_542949.1; NM_080771.1.
DR AlphaFoldDB; P17491; -.
DR SMR; P17491; -.
DR STRING; 10116.ENSRNOP00000065153; -.
DR GlyGen; P17491; 1 site.
DR PaxDb; P17491; -.
DR Ensembl; ENSRNOT00000086350; ENSRNOP00000071390; ENSRNOG00000060237.
DR GeneID; 25196; -.
DR KEGG; rno:25196; -.
DR CTD; 3625; -.
DR RGD; 2913; Inhbb.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000159862; -.
DR InParanoid; P17491; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; P17491; -.
DR TreeFam; TF351791; -.
DR Reactome; R-RNO-1502540; Signaling by Activin.
DR Reactome; R-RNO-209822; Glycoprotein hormones.
DR Reactome; R-RNO-2473224; Antagonism of Activin by Follistatin.
DR PRO; PR:P17491; -.
DR Proteomes; UP000002494; Chromosome 13.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS: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; 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; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071397; P:cellular response to cholesterol; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0044320; P:cellular response to leptin stimulus; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEP:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0010259; P:multicellular organism aging; IEP:RGD.
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; ISS:UniProtKB.
DR GO; GO:0048599; P:oocyte development; ISO:RGD.
DR GO; GO:0021983; P:pituitary gland development; IEP:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; ISS: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; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IEP:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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_0000033728"
FT CHAIN 297..411
FT /note="Inhibin beta B chain"
FT /id="PRO_0000033729"
FT REGION 27..69
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 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 VARIANT 270
FT /note="D -> H (in beta-B20)"
FT /evidence="ECO:0000269|PubMed:2484214"
SQ SEQUENCE 411 AA; 45183 MW; 85D4D4CAD9D74620 CRC64;
MDGLPGRALG AACLLLLAAG 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
