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Database: UniProt
Entry: B6DT33_SHEEP
LinkDB: B6DT33_SHEEP
Original site: B6DT33_SHEEP 
ID   B6DT33_SHEEP            Unreviewed;       408 AA.
AC   B6DT33;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Inhibin beta B chain {ECO:0000256|ARBA:ARBA00014337};
DE   AltName: Full=Activin beta-B chain {ECO:0000256|ARBA:ARBA00032422};
GN   Name=INHBB {ECO:0000313|EMBL:ACI14288.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|EMBL:ACI14288.1};
RN   [1] {ECO:0000313|EMBL:ACI14288.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2015059;
RA   Rodgers R.J.;
RT   "Cloning of the inhibin/activin beta B subunit gene from the Booroola
RT   merino sheep.";
RL   J. Mol. Endocrinol. 6:87-93(1991).
RN   [2] {ECO:0000313|EMBL:ACI14288.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rodgers R.J., Hatzirodos N.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|ARBA:ARBA00002588}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family.
CC       {ECO:0000256|ARBA:ARBA00006656, ECO:0000256|RuleBase:RU000354}.
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DR   EMBL; FJ167874; ACI14288.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6DT33; -.
DR   SMR; B6DT33; -.
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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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: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: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:0009611; P:response to wounding; ISS:UniProtKB.
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.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW   ECO:0000256|RuleBase:RU000354}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..408
FT                   /note="Inhibin beta B chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002844190"
FT   DOMAIN          287..408
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
FT   REGION          30..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..50
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  44988 MW;  FD2AEC9FB4BBF12E CRC64;
     MDGLPGRALG AACLVMLAVG WLGPGVWGSP TPPPSPAAPQ PPPPPPGAPG GAQDTCTSCG
     GFRRPEELGR VDGDFLEAVK RHILSRLQMR GRPNITHAVP KAAMVTALRK LHAGKVREDG
     RVEIPHLDGH ASPGADGPER VSEIISFAET DGLASSRVRL YFFISNEGNQ NLFVVQASLW
     LYLKLLPYVL EKGGRRKVRV KVYFQEQGPG DRWAAVEKRV DLKRSGWHTF PLTEPIQALF
     SRGERRLSLD VQCDGCRELA VVPVFVDPGE ESHRPFVVVQ ERLGDSRHRI RKRGLECDGR
     TSLCCRQQFF IDFRLIGWND WIIAPTGYYG NYCEGSCPAY LAGVPGSASS FHTAVVNQYR
     MRGLNPGTVN SCCIPTKLST MSMLYFDDEY NIVKRDVPNM IVEECACA
//
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