ID   INHBE_RAT               Reviewed;         350 AA.
AC   O88959; Q9R285;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Inhibin beta E chain;
DE   AltName: Full=Activin beta-E chain;
DE   Flags: Precursor;
GN   Name=Inhbe;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver, and Lung;
RX   PubMed=10828834; DOI=10.1677/jme.0.0240409;
RA   O'Bryan M.K., Sebire K.L., Gerdprasert O., Hedger M.P., Hearn M.T.W.,
RA   de Kretser D.M.;
RT   "Cloning and regulation of the rat activin betaE subunit.";
RL   J. Mol. Endocrinol. 24:409-418(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RA   Rossmanith W., Peter B., Schulte-Hermann R.;
RT   "Rat activin beta C and beta E: sequence and expression.";
RL   Submitted (APR-1999) 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   -!- SUBUNIT: Homodimeric or heterodimeric through association with alpha
CC       and beta subunits, linked by one or more disulfide bonds. Inhibins are
CC       heterodimers of one alpha and one beta subunit. Activins are homo- or
CC       heterodimers of beta subunits only (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; AF089825; AAC36741.1; -; mRNA.
DR   EMBL; AF140032; AAD30133.1; -; mRNA.
DR   RefSeq; NP_114003.2; NM_031815.2.
DR   AlphaFoldDB; O88959; -.
DR   SMR; O88959; -.
DR   STRING; 10116.ENSRNOP00000010106; -.
DR   GlyGen; O88959; 1 site.
DR   PaxDb; O88959; -.
DR   PRIDE; O88959; -.
DR   GeneID; 83711; -.
DR   KEGG; rno:83711; -.
DR   UCSC; RGD:621196; rat.
DR   CTD; 83729; -.
DR   RGD; 621196; Inhbe.
DR   eggNOG; KOG3900; Eukaryota.
DR   InParanoid; O88959; -.
DR   OrthoDB; 1385831at2759; -.
DR   PhylomeDB; O88959; -.
DR   TreeFam; TF318514; -.
DR   Reactome; R-RNO-209822; Glycoprotein hormones.
DR   PRO; PR:O88959; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001318; Inhibin_betaC.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   PRINTS; PR00672; INHIBINBC.
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..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..236
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033740"
FT   CHAIN           237..350
FT                   /note="Inhibin beta E chain"
FT                   /id="PRO_0000033741"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        240..248
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..315
FT                   /evidence="ECO:0000250"
FT   DISULFID        276..347
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..349
FT                   /evidence="ECO:0000250"
FT   DISULFID        314
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        160..161
FT                   /note="EH -> DY (in Ref. 2; AAD30133)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  38899 MW;  0CEBF6E108E926E3 CRC64;
     MGLSNVQLWT ILLWALAWVQ STRSACPSCG APTLTPQGER ALVLELAKQQ ILEGLHLTSR
     PRITRPLPQA ALTRALRRLQ PRSMVPGNRE KVISFATSID KSTSTYRSVL TFQLSPLWSH
     HLYHARLWLH VPPSFPATLY LRIFGCGTTR CRGSRTFLAE HQTTSSGWHA LTLPSSGLRS
     EESGVTKLQL EFRPLDLNST TARLPRLLLD TAGQQRPFLE LKIRANEPGA GRARRRTPTC
     ESETPLCCRR DHYVDFQELG WRDWILQPEG YQLNYCSGQC PPHLAGSPGI AASFHSAVFS
     LLKANNPWPA GSSCCVPTAR RPLSLLYLDH NGNVVKTDVP DMVVEACGCS