INHBB_CHICK
ID INHBB_CHICK Reviewed; 391 AA.
AC P27093; O73796;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inhibin beta B chain;
DE AltName: Full=Activin beta-B chain;
DE Flags: Precursor;
GN Name=INHBB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Follicular cell;
RA Klinger H., Halaschek-Wiener J., Wohlrab B.K., Kuchler K., Wohlrab F.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Ovary;
RA Hecht D.J., Davis A.J., Ryan I.M., Johnson P.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 311-381.
RX PubMed=2225063; DOI=10.1016/0092-8674(90)90446-l;
RA Mitrani E., Ziv T., Thomsen G., Shimoni Y., Melton D.A., Bril A.;
RT "Activin can induce the formation of axial structures and is expressed in
RT the hypoblast of the chick.";
RL Cell 63:495-501(1990).
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.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; Z71594; CAA96248.1; -; mRNA.
DR EMBL; AF055478; AAC14187.1; -; mRNA.
DR EMBL; M61166; AAA48568.1; -; mRNA.
DR EMBL; M57408; AAA03079.1; -; mRNA.
DR PIR; A36193; A36193.
DR RefSeq; NP_990537.1; NM_205206.1.
DR AlphaFoldDB; P27093; -.
DR SMR; P27093; -.
DR STRING; 9031.ENSGALP00000042014; -.
DR GeneID; 396126; -.
DR KEGG; gga:396126; -.
DR CTD; 3625; -.
DR VEuPathDB; HostDB:geneid_396126; -.
DR eggNOG; KOG3900; Eukaryota.
DR HOGENOM; CLU_020515_5_1_1; -.
DR InParanoid; P27093; -.
DR PhylomeDB; P27093; -.
DR PRO; PR:P27093; -.
DR Proteomes; UP000000539; 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: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:1900164; P:nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; TAS:AgBase.
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 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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..276
FT /evidence="ECO:0000255"
FT /id="PRO_0000033720"
FT CHAIN 277..391
FT /note="Inhibin beta B chain"
FT /id="PRO_0000033721"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..288
FT /evidence="ECO:0000250"
FT DISULFID 287..356
FT /evidence="ECO:0000250"
FT DISULFID 316..388
FT /evidence="ECO:0000250"
FT DISULFID 320..390
FT /evidence="ECO:0000250"
FT DISULFID 355
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 30
FT /note="P -> PG (in Ref. 2; AAC14187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43608 MW; 060017BF33F7AF6C CRC64;
MDGAARRGVL AALLACGLLL LGAAATPTPP PAGSSPQDTC TSCGFRRPEE PGKVDGDFLE
AVKRHILSRL QMRDRPNITH AVPKAAMVTA LRKLHAGKVR EDGRVEIPSL DGQASAGPPA
HDPVSEIISF AETDDLASSR VRLYFFISNE GNQNLFVVQA SLWLYLKLLP YVLEKGSRRK
VRVKVYFQDP DTSNKWNVVE KKVDLKRSGW HTFPMTEAIQ ALFERGERRL NLDVQCEGCE
EYSVLPIYVD PGEESHRPFL VVQARLADNK HRIRKRGLEC DGRTNLCCRQ QFYIDFRLIG
WNDWIIAPSG YYGNYCEGSC PAYLAGVPGS ASSFHTAVVN QYRMRGLNPG TVNSCCIPTK
LSTMSMLYFD DEYNIVKRDV PNMIVEECGC A
