ID   INHBC_RAT               Reviewed;         351 AA.
AC   Q9WUK5; Q5FVS9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Inhibin beta C chain;
DE   AltName: Full=Activin beta-C chain;
DE   Flags: Precursor;
GN   Name=Inhbc;
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=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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
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; AF140031; AAD30132.1; -; mRNA.
DR   EMBL; BC089799; AAH89799.1; -; mRNA.
DR   RefSeq; NP_072136.1; NM_022614.2.
DR   AlphaFoldDB; Q9WUK5; -.
DR   SMR; Q9WUK5; -.
DR   STRING; 10116.ENSRNOP00000010240; -.
DR   GlyGen; Q9WUK5; 3 sites.
DR   PaxDb; Q9WUK5; -.
DR   PRIDE; Q9WUK5; -.
DR   Ensembl; ENSRNOT00000010240; ENSRNOP00000010240; ENSRNOG00000007700.
DR   GeneID; 64549; -.
DR   KEGG; rno:64549; -.
DR   UCSC; RGD:621194; rat.
DR   CTD; 3626; -.
DR   RGD; 621194; Inhbc.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000160065; -.
DR   HOGENOM; CLU_020515_5_1_1; -.
DR   InParanoid; Q9WUK5; -.
DR   OMA; GLSTINQ; -.
DR   OrthoDB; 1385831at2759; -.
DR   PhylomeDB; Q9WUK5; -.
DR   TreeFam; TF351791; -.
DR   Reactome; R-RNO-209822; Glycoprotein hormones.
DR   PRO; PR:Q9WUK5; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000007700; Expressed in liver and 2 other tissues.
DR   Genevisible; Q9WUK5; RN.
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   Disulfide bond; Glycoprotein; Growth factor; Hormone; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..236
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033734"
FT   CHAIN           237..351
FT                   /note="Inhibin beta C chain"
FT                   /id="PRO_0000033735"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        239..247
FT                   /evidence="ECO:0000250"
FT   DISULFID        246..316
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..348
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        315
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  39335 MW;  6B219BF6C3E180A1 CRC64;
     MASSLLLALL FLTLATVVNL KTDGPCPACW GATFDLESHR ELLLDLAKKS ILDKLHLSQR
     PILSRPVSRE ALKTALRRLR GTRAETLLEH DQRQEYEIIS FADTGLSNIN QTRLEFHFSD
     RTTGGVEVLQ TRFMFFMQLP PNTTQTMNIR VLVLRPYDTN LTLTSQYMLQ VDASGWYQLL
     LGPEAQAACS QGHLTLELVP ESQLAHSSLI LDGVSHRPFV AAQVRVEGKH RVRRRGINCQ
     GLSRMCCRQE FFVDFREIGW HDWIIQPEGY AMNFCTGQCP LHVAGMPGIS ASFHTAVLNL
     LKANTDAGTA RRGSCCVPTS RRPLSLLYYD RDSNIVKTDI PDMVVEACGC S