INHBA_RAT
ID INHBA_RAT Reviewed; 424 AA.
AC P18331;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Inhibin beta A chain;
DE AltName: Full=Activin beta-A chain;
DE Flags: Precursor;
GN Name=Inhba;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3153478; DOI=10.1210/mend-1-8-561;
RA Woodruff T.K., Meunier H., Jones P.B.C., Hsueh A.J.W., Mayo K.E.;
RT "Rat inhibin: molecular cloning of alpha- and beta-subunit complementary
RT deoxyribonucleic acids and expression in the ovary.";
RL Mol. Endocrinol. 1:561-568(1987).
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; M37482; AAA41436.1; -; mRNA.
DR PIR; B40905; B40905.
DR RefSeq; NP_058824.1; NM_017128.2.
DR RefSeq; XP_006254063.1; XM_006254001.3.
DR RefSeq; XP_008769934.1; XM_008771712.2.
DR RefSeq; XP_008769935.1; XM_008771713.2.
DR RefSeq; XP_008769936.1; XM_008771714.2.
DR RefSeq; XP_008769937.1; XM_008771715.2.
DR RefSeq; XP_008769938.1; XM_008771716.2.
DR AlphaFoldDB; P18331; -.
DR SMR; P18331; -.
DR STRING; 10116.ENSRNOP00000019272; -.
DR GlyGen; P18331; 1 site.
DR iPTMnet; P18331; -.
DR PhosphoSitePlus; P18331; -.
DR PaxDb; P18331; -.
DR Ensembl; ENSRNOT00000019272; ENSRNOP00000019272; ENSRNOG00000014320.
DR GeneID; 29200; -.
DR KEGG; rno:29200; -.
DR UCSC; RGD:62074; rat.
DR CTD; 3624; -.
DR RGD; 62074; Inhba.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157116; -.
DR HOGENOM; CLU_020515_5_1_1; -.
DR InParanoid; P18331; -.
DR OMA; LALCWIR; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; P18331; -.
DR TreeFam; TF351791; -.
DR Reactome; R-RNO-1502540; Signaling by Activin.
DR Reactome; R-RNO-209822; Glycoprotein hormones.
DR Reactome; R-RNO-2473224; Antagonism of Activin by Follistatin.
DR PRO; PR:P18331; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000014320; Expressed in ovary and 13 other tissues.
DR Genevisible; P18331; RN.
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; IDA:RGD.
DR GO; GO:0043512; C:inhibin A complex; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
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:RGD.
DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0070699; F:type II activin receptor binding; ISO:RGD.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; IDA:UniProtKB.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0097154; P:GABAergic neuron differentiation; ISO:RGD.
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:0001707; P:mesoderm formation; ISO:RGD.
DR GO; GO:0048333; P:mesodermal cell differentiation; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; IEP:RGD.
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:RGD.
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:RGD.
DR GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD.
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:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; ISO:RGD.
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 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..20
FT /evidence="ECO:0000250"
FT PROPEP 21..308
FT /id="PRO_0000033714"
FT CHAIN 309..424
FT /note="Inhibin beta A chain"
FT /id="PRO_0000033715"
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; 47406 MW; B2DAF7917FA50984 CRC64;
MPLLWLRGFL LASCWIIVRS SPTPGSEGHG AAPDCPSCAL ATLPKDGPNS QPEMVEAVKK
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT
SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEVWLFLK VPKANRTRTK VTIRLFQQQK
HPQGSLDMGD EAEEMGLKGE RSELLLSEKV VDARKSTWHI FPVSSSIQRL LDQGKSSLDV
RIACEQCQES GASLVLLGKK KKKEVDGDGK KKDGSDGGLE EEKEQSHRPF LMLQARQSED
HPHRRRRRGL ECDGKVNICC KKQFFVSFKD IGWNDWIIAP SGYHANYCEG ECPSHIAGTS
GSSLSFHSTV INHYRMRGHS PFANLKSCCV PTKLRPMSML YYDDGQNIIK KDIQNMIVEE
CGCS
