ID INHBC_HUMAN Reviewed; 352 AA. AC P55103; A1L3Y2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 180. DE RecName: Full=Inhibin beta C chain; DE AltName: Full=Activin beta-C chain; DE Flags: Precursor; GN Name=INHBC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=7826378; DOI=10.1006/bbrc.1995.1086; RA Hoetten G., Neidhardt H., Schneider C., Pohl J.; RT "Cloning of a new member of the TGF-beta family: a putative new activin RT beta C chain."; RL Biochem. Biophys. Res. Commun. 206:608-613(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] RP TISSUE SPECIFICITY. RX PubMed=9428386; RX DOI=10.1002/(sici)1097-0045(19980101)34:1<34::aid-pros5>3.0.co;2-k; RA Thomas T.Z., Chapman S.M., Hong W., Gurusingfhe C., Mellor S.L., RA Fletcher R., Pedersen J., Risbridger G.P.; RT "Inhibins, activins, and follistatins: expression of mRNAs and cellular RT localization in tissues from men with benign prostatic hyperplasia."; RL Prostate 34:34-43(1998). 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 -!- TISSUE SPECIFICITY: Expressed in benign prostatic hyperplasia. CC {ECO:0000269|PubMed:9428386}. CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X82540; CAA57890.1; -; mRNA. DR EMBL; CH471054; EAW97011.1; -; Genomic_DNA. DR EMBL; BC130324; AAI30325.1; -; mRNA. DR EMBL; BC130326; AAI30327.1; -; mRNA. DR CCDS; CCDS8938.1; -. DR PIR; JC2466; JC2466. DR RefSeq; NP_005529.1; NM_005538.4. DR AlphaFoldDB; P55103; -. DR SMR; P55103; -. DR FunCoup; P55103; 418. DR NDEx; IQUERY-CP-INHBC; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000308716; -. DR GlyCosmos; P55103; 3 sites, No reported glycans. DR GlyGen; P55103; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; P55103; -. DR PhosphoSitePlus; P55103; -. DR BioMuta; INHBC; -. DR DMDM; 1708438; -. DR MassIVE; P55103; -. DR PaxDb; 9606-ENSP00000308716; -. DR PeptideAtlas; P55103; -. DR ProteomicsDB; 56791; -. DR Antibodypedia; 28599; 322 antibodies from 30 providers. DR DNASU; 3626; -. DR Ensembl; ENST00000309668.3; ENSP00000308716.2; ENSG00000175189.4. DR GeneID; 3626; -. DR KEGG; hsa:3626; -. DR MANE-Select; ENST00000309668.3; ENSP00000308716.2; NM_005538.4; NP_005529.1. DR UCSC; uc001snv.3; human. DR AGR; HGNC:6068; -. DR ClinPGx; PA29879; -. DR CTD; 3626; -. DR DisGeNET; 3626; -. DR GeneCards; INHBC; -. DR HGNC; HGNC:6068; INHBC. DR HPA; ENSG00000175189; Tissue enriched (liver). DR MIM; 601233; gene. DR OpenTargets; ENSG00000175189; -. DR VEuPathDB; HostDB:ENSG00000175189; -. DR eggNOG; KOG3900; Eukaryota. DR GeneTree; ENSGT00940000160065; -. DR HOGENOM; CLU_020515_5_0_1; -. DR InParanoid; P55103; -. DR OMA; GIDCQGG; -. DR OrthoDB; 6516235at2759; -. DR PAN-GO; P55103; 3 GO annotations based on evolutionary models. DR PhylomeDB; P55103; -. DR PathwayCommons; P55103; -. DR Reactome; R-HSA-209822; Glycoprotein hormones. DR SignaLink; P55103; -. DR Agora; ENSG00000175189; -. DR BioGRID-ORCS; 3626; 20 hits in 1146 CRISPR screens. DR GeneWiki; INHBC; -. DR GenomeRNAi; 3626; -. DR Pharos; P55103; Tbio. DR PRO; PR:P55103; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P55103; protein. DR Bgee; ENSG00000175189; Expressed in right lobe of liver and 34 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; TAS:ProtInc. DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central. DR GO; GO:0008083; F:growth factor activity; IEA:InterPro. DR GO; GO:0005179; F:hormone activity; IEA:InterPro. DR GO; GO:0005160; F:transforming growth factor beta receptor binding; TAS:ProtInc. DR GO; GO:0007178; P:cell surface receptor protein serine/threonine kinase signaling pathway; IBA:GO_Central. DR CDD; cd19406; TGF_beta_INHBC_E; 1. DR FunFam; 2.10.90.10:FF:000005; Inhibin beta A chain; 1. DR FunFam; 2.60.120.970:FF:000022; Inhibin subunit beta C; 1. DR Gene3D; 2.60.120.970; -; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR001318; Inhibin_betaC. DR InterPro; IPR001839; TGF-b_C. DR InterPro; IPR015615; TGF-beta-like. DR InterPro; IPR017948; TGFb_CS. DR PANTHER; PTHR11848:SF130; INHIBIN BETA C CHAIN; 1. DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1. DR Pfam; PF00019; TGF_beta; 1. DR PRINTS; PR00672; INHIBINBC. DR SMART; SM00204; TGFB; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 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; Disulfide bond; Glycoprotein; KW Growth factor; Hormone; Proteomics identification; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT PROPEP 19..236 FT /evidence="ECO:0000255" FT /id="PRO_0000033730" FT CHAIN 237..352 FT /note="Inhibin beta C chain" FT /id="PRO_0000033731" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 240..248 FT /evidence="ECO:0000250" FT DISULFID 247..317 FT /evidence="ECO:0000250" FT DISULFID 276..349 FT /evidence="ECO:0000250" FT DISULFID 280..351 FT /evidence="ECO:0000250" FT DISULFID 316 FT /note="Interchain" FT /evidence="ECO:0000250" FT VARIANT 322 FT /note="R -> Q (in dbSNP:rs2229357)" FT /id="VAR_024230" SQ SEQUENCE 352 AA; 38238 MW; 496476AD82562D3E CRC64; MTSSLLLAFL LLAPTTVATP RAGGQCPACG GPTLELESQR ELLLDLAKRS ILDKLHLTQR PTLNRPVSRA ALRTALQHLH GVPQGALLED NREQECEIIS FAETGLSTIN QTRLDFHFSS DRTAGDREVQ QASLMFFVQL PSNTTWTLKV RVLVLGPHNT NLTLATQYLL EVDASGWHQL PLGPEAQAAC SQGHLTLELV LEGQVAQSSV ILGGAAHRPF VAARVRVGGK HQIHRRGIDC QGGSRMCCRQ EFFVDFREIG WHDWIIQPEG YAMNFCIGQC PLHIAGMPGI AASFHTAVLN LLKANTAAGT TGGGSCCVPT ARRPLSLLYY DRDSNIVKTD IPDMVVEACG CS //