INHA_MOUSE
ID INHA_MOUSE Reviewed; 366 AA.
AC Q04997; Q6GTG7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Inhibin alpha chain;
DE Flags: Precursor;
GN Name=Inha;
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 [MRNA].
RX PubMed=8330535; DOI=10.1242/dev.117.2.711;
RA Albano P.M., Groome N., Smith J.C.;
RT "Activins are expressed in preimplantation mouse embryos and in ES and EC
RT cells and are regulated on their differentiation.";
RL Development 117:711-723(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1632772; DOI=10.1016/s0006-291x(05)80806-x;
RA Su J.G.W., Hsueh A.J.W.;
RT "Characterization of mouse inhibin alpha gene and its promoter.";
RL Biochem. Biophys. Res. Commun. 186:293-300(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-366.
RC STRAIN=Swiss Webster;
RX PubMed=2253839; DOI=10.1111/j.1432-0436.1990.tb00537.x;
RA Tone S., Katoh Y., Fujimoto H., Togashi S., Yanazawa M., Kato Y.,
RA Higashinakagawa T.;
RT "Expression of inhibin alpha-subunit gene during mouse gametogenesis.";
RL Differentiation 44:62-68(1990).
RN [6]
RP FUNCTION.
RX PubMed=1448148; DOI=10.1038/360313a0;
RA Matzuk M.M., Finegold M.J., Su J.G.W., Hsueh A.J.W., Bradley A.;
RT "Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in
RT mice.";
RL Nature 360:313-319(1992).
RN [7]
RP FUNCTION.
RX PubMed=8090730; DOI=10.1073/pnas.91.19.8817;
RA Matzuk M.M., Finegold M.J., Mather J.P., Krummen L., Lu H., Bradley A.;
RT "Development of cancer cachexia-like syndrome and adrenal tumors in
RT inhibin-deficient mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8817-8821(1994).
RN [8]
RP FUNCTION, AND REVIEW.
RX PubMed=8701077;
RA Matzuk M.M., Kumar T.R., Shou W., Coerver K.A., Lau A.L., Behringer R.R.,
RA Finegold M.J.;
RT "Transgenic models to study the roles of inhibins and activins in
RT reproduction, oncogenesis, and development.";
RL Recent Prog. Horm. Res. 51:123-154(1996).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Inhibin deficient mice are viable but are acutely sensitive to
CC development of gonadal sex-cord stromal tumors.
CC {ECO:0000269|PubMed:1448148, ECO:0000269|PubMed:8090730,
CC ECO:0000269|PubMed:8701077}.
CC -!- SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A is a
CC dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Proteolytic processing yields a number of bioactive forms,
CC consisting either solely of the mature alpha chain, of the most N-
CC terminal propeptide linked through a disulfide bond to the mature alpha
CC chain, or of the entire proprotein.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; X69618; CAA49324.1; -; mRNA.
DR EMBL; M95525; AAA39314.1; -; Genomic_DNA.
DR EMBL; M95526; AAA39314.1; JOINED; Genomic_DNA.
DR EMBL; CH466548; EDL00422.1; -; Genomic_DNA.
DR EMBL; BC056627; AAH56627.1; -; mRNA.
DR EMBL; X55957; CAA39424.1; -; mRNA.
DR CCDS; CCDS15078.1; -.
DR PIR; JC1106; JC1106.
DR RefSeq; NP_034694.3; NM_010564.5.
DR AlphaFoldDB; Q04997; -.
DR BioGRID; 200761; 1.
DR STRING; 10090.ENSMUSP00000040310; -.
DR GlyGen; Q04997; 2 sites.
DR iPTMnet; Q04997; -.
DR PhosphoSitePlus; Q04997; -.
DR MaxQB; Q04997; -.
DR PaxDb; Q04997; -.
DR PRIDE; Q04997; -.
DR ProteomicsDB; 267138; -.
DR Antibodypedia; 4368; 819 antibodies from 42 providers.
DR DNASU; 16322; -.
DR Ensembl; ENSMUST00000037330; ENSMUSP00000040310; ENSMUSG00000032968.
DR GeneID; 16322; -.
DR KEGG; mmu:16322; -.
DR UCSC; uc007bps.1; mouse.
DR CTD; 3623; -.
DR MGI; MGI:96569; Inha.
DR VEuPathDB; HostDB:ENSMUSG00000032968; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00390000005935; -.
DR HOGENOM; CLU_064515_0_0_1; -.
DR InParanoid; Q04997; -.
DR OMA; TYVFRPS; -.
DR OrthoDB; 1177863at2759; -.
DR PhylomeDB; Q04997; -.
DR TreeFam; TF331531; -.
DR Reactome; R-MMU-209822; Glycoprotein hormones.
DR BioGRID-ORCS; 16322; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Inha; mouse.
DR PRO; PR:Q04997; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q04997; protein.
DR Bgee; ENSMUSG00000032968; Expressed in cumulus cell and 137 other tissues.
DR Genevisible; Q04997; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043512; C:inhibin A complex; ISO:MGI.
DR GO; GO:0043513; C:inhibin B complex; ISO:MGI.
DR GO; GO:0034673; C:inhibin-betaglycan-ActRII complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
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:0034711; F:inhibin binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISO:MGI.
DR GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; ISO:MGI.
DR GO; GO:0001541; P:ovarian follicle development; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
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; IPR017175; Inhibin_asu.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR PANTHER; PTHR11848:SF117; PTHR11848:SF117; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037328; Inhibin_alpha_subunit; 1.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Growth factor; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..63
FT /evidence="ECO:0000250"
FT /id="PRO_0000033688"
FT PROPEP 64..233
FT /note="Inhibin alpha N-terminal region"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033689"
FT CHAIN 234..366
FT /note="Inhibin alpha chain"
FT /id="PRO_0000033690"
FT SITE 63..64
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 233..234
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 263..328
FT /evidence="ECO:0000250"
FT DISULFID 292..363
FT /evidence="ECO:0000250"
FT DISULFID 296..365
FT /evidence="ECO:0000250"
FT DISULFID 327
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 165
FT /note="A -> R (in Ref. 2; AAA39314)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="G -> V (in Ref. 1; CAA49324)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="R -> T (in Ref. 1; CAA49324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 39550 MW; 2CFD44AD9D41B66B CRC64;
MVSQRSLLLL LLLTLRDVDS CQGPELVREL VLAKVKALFL DALGPPAMDG EGGDPGIRRL
PRRHAVGGFM HRTSEPEEED VSQAILFPAT GATCEDQPAA RGLAQEAEEG LFTYVFRPSQ
HIRSHQVTSA QLWFHTGLGR KSTAAANSSA PLLDLLVLSS GGPMAVPVSL GQGPPRWAVL
HLAASAFPLL THPILVLLLR CPLCSCSGRP ETTPFLVAHT RARAPSAGER ARRSTPSVPW
PWSPAALRLL QRPPEEPAAH AFCHRAALNI SFQELGWDRW IVHPPSFIFH YCHGSCGMPT
SDLPLPVPGV PPTPVQPLFL VPGAKPCCAA LPGSMRSLRV RTTSDGGYSF KYEMVPNLIT
QHCACI
