INHBC_HUMAN
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 03-AUG-2022, entry version 162.
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}.
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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_005538.3.
DR AlphaFoldDB; P55103; -.
DR SMR; P55103; -.
DR STRING; 9606.ENSP00000308716; -.
DR GlyGen; P55103; 3 sites.
DR iPTMnet; P55103; -.
DR PhosphoSitePlus; P55103; -.
DR BioMuta; INHBC; -.
DR DMDM; 1708438; -.
DR MassIVE; P55103; -.
DR PaxDb; P55103; -.
DR PeptideAtlas; P55103; -.
DR PRIDE; P55103; -.
DR ProteomicsDB; 56791; -.
DR Antibodypedia; 28599; 319 antibodies from 29 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 CTD; 3626; -.
DR DisGeNET; 3626; -.
DR GeneCards; INHBC; -.
DR HGNC; HGNC:6068; INHBC.
DR HPA; ENSG00000175189; Tissue enriched (liver).
DR MIM; 601233; gene.
DR neXtProt; NX_P55103; -.
DR OpenTargets; ENSG00000175189; -.
DR PharmGKB; PA29879; -.
DR VEuPathDB; HostDB:ENSG00000175189; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000160065; -.
DR HOGENOM; CLU_020515_5_0_1; -.
DR InParanoid; P55103; -.
DR OMA; GLSTINQ; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; P55103; -.
DR TreeFam; TF351791; -.
DR PathwayCommons; P55103; -.
DR Reactome; R-HSA-209822; Glycoprotein hormones.
DR SignaLink; P55103; -.
DR BioGRID-ORCS; 3626; 18 hits in 1068 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 33 other tissues.
DR Genevisible; P55103; HS.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
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:0005160; F:transforming growth factor beta receptor binding; TAS:ProtInc.
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..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
