INHBA_BOVIN
ID INHBA_BOVIN Reviewed; 425 AA.
AC P07995; A0JN81;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Inhibin beta A chain;
DE AltName: Full=Activin beta-A chain;
DE Flags: Precursor;
GN Name=INHBA;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 258-425.
RC TISSUE=Ovarian follicular fluid;
RX PubMed=3458167; DOI=10.1073/pnas.83.10.3091;
RA Forage R.G., Ring J.M., Brown R.W., McInerney B.V., Cobon G.S.,
RA Gregson R.P., Robertson D.M., Morgan F.J., Hearn M.T.W., Findlay J.K.,
RA Wettenhall R.E.H., Burger H.G., de Kretser D.M.;
RT "Cloning and sequence analysis of cDNA species coding for the two subunits
RT of inhibin from bovine follicular fluid.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3091-3095(1986).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1733725; DOI=10.1210/endo.130.2.1733725;
RA Sugino K., Nakamura T., Takio K., Miyamoto K., Hasegawa Y., Igarashi M.,
RA Titani K., Sugino H.;
RT "Purification and characterization of high molecular weight forms of
RT inhibin from bovine follicular fluid.";
RL Endocrinology 130:789-796(1992).
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.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; U16239; AAB60627.1; -; Genomic_DNA.
DR EMBL; U16238; AAB60627.1; JOINED; Genomic_DNA.
DR EMBL; BC126556; AAI26557.1; -; mRNA.
DR EMBL; M13274; AAA97415.1; -; mRNA.
DR PIR; S50898; S50898.
DR RefSeq; NP_776788.1; NM_174363.2.
DR RefSeq; XP_005205677.1; XM_005205620.3.
DR AlphaFoldDB; P07995; -.
DR SMR; P07995; -.
DR STRING; 9913.ENSBTAP00000003783; -.
DR PaxDb; P07995; -.
DR PRIDE; P07995; -.
DR Ensembl; ENSBTAT00000066382; ENSBTAP00000056958; ENSBTAG00000048508.
DR GeneID; 281867; -.
DR KEGG; bta:281867; -.
DR CTD; 3624; -.
DR VEuPathDB; HostDB:ENSBTAG00000048508; -.
DR VGNC; VGNC:30200; INHBA.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157116; -.
DR HOGENOM; CLU_020515_5_1_1; -.
DR InParanoid; P07995; -.
DR OMA; LRPHPKH; -.
DR OrthoDB; 1385831at2759; -.
DR TreeFam; TF351791; -.
DR Reactome; R-BTA-1502540; Signaling by Activin.
DR Reactome; R-BTA-209822; Glycoprotein hormones.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000048508; Expressed in granulosa cell and 94 other tissues.
DR GO; GO:0043509; C:activin A complex; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0043512; C:inhibin A complex; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; 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:0042802; F:identical protein binding; ISS:AgBase.
DR GO; GO:0017046; F:peptide hormone binding; ISS:AgBase.
DR GO; GO:0070699; F:type II activin receptor binding; IEA:Ensembl.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0097154; P:GABAergic neuron differentiation; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0051799; P:negative regulation of hair follicle development; IEA:Ensembl.
DR GO; GO:0042476; P:odontogenesis; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042701; P:progesterone secretion; ISS:UniProtKB.
DR GO; GO:0046880; P:regulation of follicle-stimulating hormone secretion; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000491; Inhibin_betaA.
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 Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PRINTS; PR00670; INHIBINBA.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Hormone; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT PROPEP 21..309
FT /evidence="ECO:0000250"
FT /id="PRO_0000033702"
FT CHAIN 310..425
FT /note="Inhibin beta A chain"
FT /id="PRO_0000033703"
FT REGION 259..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..321
FT /evidence="ECO:0000250"
FT DISULFID 320..390
FT /evidence="ECO:0000250"
FT DISULFID 349..422
FT /evidence="ECO:0000250"
FT DISULFID 353..424
FT /evidence="ECO:0000250"
FT DISULFID 389
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 47521 MW; 2D8799D7197CDA37 CRC64;
MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL ATLPKDVPNS QPEMVEAVKK
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT
SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEIWLFLK VPKANRTRSK VTIRLFQQQK
HLQGSLDAGE EAEEVGLKGE KSEMLISEKV VDARKSTWHI FPVSSCIQRL LDQGKSSLDI
RIACEQCQET GASLVLLGKK KKKEEEGEGK KRDGEGGAGG DEEKEQSHRP FLMLQARQSE
DHPHRRRRRG LECDGKVNIC CKKQFFVSFK DIGWNDWIIA PSGYHANYCE GECPSHIAGT
SGSSLSFHST VINHYRMRGH SPFANLKSCC VPTKLRPMSM LYYDDGQNII KKDIQNMIVE
ECGCS
