INHBA_MOUSE
ID INHBA_MOUSE Reviewed; 424 AA.
AC Q04998;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Inhibin beta A chain;
DE AltName: Full=Activin beta-A chain;
DE Flags: Precursor;
GN Name=Inhba;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8330535; DOI=10.1242/dev.117.2.711;
RA Albano P.M., Groome N., Smith J.C.;
RT "Activins are expressed in preimplantation mouse embryos and in ES and EC
RT cells and are regulated on their differentiation.";
RL Development 117:711-723(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 309-325.
RX PubMed=2133547; DOI=10.1242/dev.110.2.435;
RA Albano R.M., Godsave S.F., Huylebroeck D., Van Nimmen K., Isaacs H.V.,
RA Slack J.M., Smith J.C.;
RT "A mesoderm-inducing factor produced by WEHI-3 murine myelomonocytic
RT leukemia cells is activin A.";
RL Development 110:435-443(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. Interacts with FST and
CC FSTL3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Uterus, ovary and liver.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; X69619; CAA49325.1; -; mRNA.
DR EMBL; BC053527; AAH53527.1; -; mRNA.
DR CCDS; CCDS26251.1; -.
DR PIR; A60087; S31440.
DR RefSeq; NP_032406.1; NM_008380.2.
DR RefSeq; XP_006516621.1; XM_006516558.2.
DR RefSeq; XP_006516622.1; XM_006516559.2.
DR RefSeq; XP_011242587.1; XM_011244285.2.
DR RefSeq; XP_011242588.1; XM_011244286.1.
DR AlphaFoldDB; Q04998; -.
DR SMR; Q04998; -.
DR BioGRID; 200762; 5.
DR STRING; 10090.ENSMUSP00000047894; -.
DR BindingDB; Q04998; -.
DR ChEMBL; CHEMBL3588734; -.
DR GlyGen; Q04998; 1 site.
DR PhosphoSitePlus; Q04998; -.
DR PaxDb; Q04998; -.
DR PeptideAtlas; Q04998; -.
DR PRIDE; Q04998; -.
DR ProteomicsDB; 301652; -.
DR Antibodypedia; 13122; 568 antibodies from 35 providers.
DR DNASU; 16323; -.
DR Ensembl; ENSMUST00000042603; ENSMUSP00000047894; ENSMUSG00000041324.
DR Ensembl; ENSMUST00000164993; ENSMUSP00000132085; ENSMUSG00000041324.
DR GeneID; 16323; -.
DR KEGG; mmu:16323; -.
DR UCSC; uc007pnw.1; mouse.
DR CTD; 3624; -.
DR MGI; MGI:96570; Inhba.
DR VEuPathDB; HostDB:ENSMUSG00000041324; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157116; -.
DR HOGENOM; CLU_020515_5_1_1; -.
DR InParanoid; Q04998; -.
DR OMA; LALCWIR; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; Q04998; -.
DR TreeFam; TF351791; -.
DR Reactome; R-MMU-1502540; Signaling by Activin.
DR Reactome; R-MMU-209822; Glycoprotein hormones.
DR Reactome; R-MMU-2473224; Antagonism of Activin by Follistatin.
DR BioGRID-ORCS; 16323; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q04998; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q04998; protein.
DR Bgee; ENSMUSG00000041324; Expressed in cumulus cell and 178 other tissues.
DR ExpressionAtlas; Q04998; baseline and differential.
DR Genevisible; Q04998; MM.
DR GO; GO:0043509; C:activin A complex; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0043512; C:inhibin A complex; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0070699; F:type II activin receptor binding; ISO:MGI.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; ISO:MGI.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISO:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IGI:UniProtKB.
DR GO; GO:0097154; P:GABAergic neuron differentiation; ISO:MGI.
DR GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:MGI.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IDA:MGI.
DR GO; GO:0048333; P:mesodermal cell differentiation; IDA:MGI.
DR GO; GO:0010259; P:multicellular organism aging; 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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI: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:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
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 /evidence="ECO:0000250"
FT PROPEP 21..308
FT /evidence="ECO:0000269|PubMed:2133547"
FT /id="PRO_0000033710"
FT CHAIN 309..424
FT /note="Inhibin beta A chain"
FT /id="PRO_0000033711"
FT REGION 264..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 312..320
FT /evidence="ECO:0000250"
FT DISULFID 319..389
FT /evidence="ECO:0000250"
FT DISULFID 348..421
FT /evidence="ECO:0000250"
FT DISULFID 352..423
FT /evidence="ECO:0000250"
FT DISULFID 388
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 47392 MW; 80C251B8754A7213 CRC64;
MPLLWLRGFL LASCWIIVRS SPTPGSEGHG SAPDCPSCAL ATLPKDGPNS QPEMVEAVKK
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT
SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEVWLFLK VPKANRTRTK VTIRLFQQQK
HPQGSLDTGD EAEEMGLKGE RSELLLSEKV VDARKSTWHI FPVSSSIQRL LDQGKSSLDV
RIACEQCQES GASLVLLGKK KKKEVDGDGK KKDGSDGGLE EEKEQSHRPF LMLQARQSED
HPHRRRRRGL ECDGKVNICC KKQFFVSFKD IGWNDWIIAP SGYHANYCEG ECPSHIAGTS
GSSLSFHSTV INHYRMRGHS PFANLKSCCV PTKLRPMSML YYDDGQNIIK KDIQNMIVEE
CGCS
