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INHBC_MOUSE
ID   INHBC_MOUSE             Reviewed;         352 AA.
AC   P55104; Q61452;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Inhibin beta C chain;
DE   AltName: Full=Activin beta-C chain;
DE   Flags: Precursor;
GN   Name=Inhbc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129; TISSUE=Liver;
RX   PubMed=8838799; DOI=10.1006/geno.1996.0130;
RA   Schmitt J., Hoetten G., Jenkins N.A., Gilbert D.J., Copeland N.G., Pohl J.,
RA   Schrewe H.;
RT   "Structure, chromosomal localization, and expression analysis of the mouse
RT   inhibin/activin beta C (Inhbc) gene.";
RL   Genomics 32:358-366(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8679697; DOI=10.1016/0167-4781(96)00061-9;
RA   Lau A.L., Nishimori K., Matzuk M.M.;
RT   "Structural analysis of the mouse activin beta C gene.";
RL   Biochim. Biophys. Acta 1307:145-148(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9070865; DOI=10.1006/bbrc.1997.6162;
RA   Fang J., Wang S.Q., Smiley E., Bonadio J.;
RT   "Genes coding for mouse activin beta C and beta E are closely linked and
RT   exhibit a liver-specific expression pattern in adult tissues.";
RL   Biochem. Biophys. Res. Commun. 231:655-661(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; 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   -!- TISSUE SPECIFICITY: Mainly expressed in the adult liver.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; X90841; CAA62347.1; -; Genomic_DNA.
DR   EMBL; X90842; CAA62347.1; JOINED; Genomic_DNA.
DR   EMBL; X90819; CAA62333.1; -; mRNA.
DR   EMBL; U40773; AAC52723.1; -; Genomic_DNA.
DR   EMBL; U40772; AAC52723.1; JOINED; Genomic_DNA.
DR   EMBL; U95962; AAC53164.1; -; mRNA.
DR   EMBL; BC026140; AAH26140.1; -; mRNA.
DR   CCDS; CCDS24240.1; -.
DR   PIR; JC5366; JC5366.
DR   PIR; S70580; S70580.
DR   RefSeq; NP_034695.1; NM_010565.4.
DR   AlphaFoldDB; P55104; -.
DR   SMR; P55104; -.
DR   STRING; 10090.ENSMUSP00000026472; -.
DR   GlyGen; P55104; 4 sites.
DR   iPTMnet; P55104; -.
DR   PhosphoSitePlus; P55104; -.
DR   MaxQB; P55104; -.
DR   PaxDb; P55104; -.
DR   PeptideAtlas; P55104; -.
DR   PRIDE; P55104; -.
DR   ProteomicsDB; 269485; -.
DR   Antibodypedia; 28599; 319 antibodies from 29 providers.
DR   DNASU; 16325; -.
DR   Ensembl; ENSMUST00000026472; ENSMUSP00000026472; ENSMUSG00000025405.
DR   GeneID; 16325; -.
DR   KEGG; mmu:16325; -.
DR   UCSC; uc007hjj.2; mouse.
DR   CTD; 3626; -.
DR   MGI; MGI:105932; Inhbc.
DR   VEuPathDB; HostDB:ENSMUSG00000025405; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000160065; -.
DR   HOGENOM; CLU_020515_5_1_1; -.
DR   InParanoid; P55104; -.
DR   OMA; GLSTINQ; -.
DR   OrthoDB; 1385831at2759; -.
DR   PhylomeDB; P55104; -.
DR   TreeFam; TF351791; -.
DR   Reactome; R-MMU-209822; Glycoprotein hormones.
DR   BioGRID-ORCS; 16325; 2 hits in 73 CRISPR screens.
DR   PRO; PR:P55104; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P55104; protein.
DR   Bgee; ENSMUSG00000025405; Expressed in liver and 4 other tissues.
DR   Genevisible; P55104; MM.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..236
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033732"
FT   CHAIN           237..352
FT                   /note="Inhibin beta C chain"
FT                   /id="PRO_0000033733"
FT   CARBOHYD        111
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   CARBOHYD        173
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   CONFLICT        243
FT                   /note="A -> G (in Ref. 1; CAA62347/CAA62333)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  39401 MW;  220812FD73717185 CRC64;
     MASSLLLALL FLTPTTVVNP KTEGPCPACW GAIFDLESQR ELLLDLAKKS ILDKLHLSQR
     PILSRPVSRG ALKTALQRLR GPRRETLLEH DQRQEEYEII SFADTDLSSI NQTRLEFHFS
     GRMASGMEVR QTRFMFFVQF PHNATQTMNI RVLVLRPYDT NLTLTSQYVV QVNASGWYQL
     LLGPEAQAAC SQGHLTLELV PESQVAHSSL ILGWFSHRPF VAAQVRVEGK HRVRRRGIDC
     QGASRMCCRQ EFFVDFREIG WNDWIIQPEG YAMNFCTGQC PLHVAGMPGI SASFHTAVLN
     LLKANAAAGT TGRGSCCVPT SRRPLSLLYY DRDSNIVKTD IPDMVVEACG CS
 
 
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