INHBB_BOVIN
ID INHBB_BOVIN Reviewed; 408 AA.
AC P42917;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Inhibin beta B chain;
DE AltName: Full=Activin beta-B chain;
DE Flags: Precursor;
GN Name=INHBB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7813465; DOI=10.1111/j.1432-1033.1994.00751.x;
RA Thompson D.A., Cronin C.N., Martin F.;
RT "Genomic cloning and sequence analyses of the bovine alpha-, beta A- and
RT beta B-inhibin/activin genes. Identification of transcription factor AP-2-
RT binding sites in the 5'-flanking regions by DNase I footprinting.";
RL Eur. J. Biochem. 226:751-764(1994).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; U16241; AAB60628.1; -; Genomic_DNA.
DR EMBL; U16240; AAB60628.1; JOINED; Genomic_DNA.
DR PIR; S50899; S50899.
DR AlphaFoldDB; P42917; -.
DR SMR; P42917; -.
DR STRING; 9913.ENSBTAP00000042801; -.
DR PaxDb; P42917; -.
DR PRIDE; P42917; -.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; P42917; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
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:AgBase.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; ISS:AgBase.
DR GO; GO:0032686; P:negative regulation of hepatocyte growth factor production; ISS:AgBase.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; ISS:AgBase.
DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
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 3: Inferred from homology;
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..293
FT /evidence="ECO:0000255"
FT /id="PRO_0000033718"
FT CHAIN 294..408
FT /note="Inhibin beta B chain"
FT /id="PRO_0000033719"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 297..305
FT /evidence="ECO:0000250"
FT DISULFID 304..373
FT /evidence="ECO:0000250"
FT DISULFID 333..405
FT /evidence="ECO:0000250"
FT DISULFID 337..407
FT /evidence="ECO:0000250"
FT DISULFID 372
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 44897 MW; EF497DB30D2897DF CRC64;
MDGLPGRALG AACLLMLAVG SLGPGVWGSP TPPPLPAAPQ PPPPPPGAPG GSQDTCTSCG
GFRRPEELGR VDGDFLEAVK RHILNRLQMR GRPNITHAVP KAAMVTALRK LHAGKVREDG
RVEIPHLDGH ASPGADGQER VSEIISFAET DGLASSRVRL YFFISNEGNQ NLFVVQASLW
LYLKLLPYVL EKGGRRKVRV KVYGQEQGPG DRWAAVEKRV DLKRSGWHTF PLTEPIQALF
SRGERRLSLD VQCDSCRELA VVPVFVDPGE ESHRPFVVVQ ARLGDSRHRI RKRGLECDGR
TNLCCRQQFF IDFRLIGWND WIIAPTGYYG NYCEGSCPAY LAGVPGSASS FHTAVVNQYR
MRGLNPGTVN SCCIPTKLST MSMLYFDDEY NIVKRDVPNM IVEECGCA
