INHB_DROME
ID INHB_DROME Reviewed; 946 AA.
AC O61643; Q8MRB1; Q8WR60; Q9V497;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Inhibin beta chain;
DE AltName: Full=Activin beta chain;
DE Short=dAct;
DE Short=dActivin;
DE Flags: Precursor;
GN Name=Actbeta; Synonyms=activin-beta; ORFNames=CG11062;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-946.
RC TISSUE=Embryo;
RX PubMed=12095682; DOI=10.1016/s0378-1119(02)00463-8;
RA Haerry T.E., O'Connor M.B.;
RT "Isolation of Drosophila activin and follistatin cDNAs using novel MACH
RT amplification protocols.";
RL Gene 291:85-93(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 574-946, AND DEVELOPMENTAL STAGE.
RX PubMed=9618266; DOI=10.1006/bbrc.1998.8678;
RA Kutty G., Kutty R.K., Samuel W., Duncan T., Jaworski C., Wiggert B.;
RT "Identification of a new member of transforming growth factor-beta
RT superfamily in Drosophila: the first invertebrate activin gene.";
RL Biochem. Biophys. Res. Commun. 246:644-649(1998).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12581521; DOI=10.1016/s0092-8674(03)00072-2;
RA Zheng X., Wang J., Haerry T.E., Wu A.Y.-H., Martin J., O'Connor M.B.,
RA Lee C.-H.J., Lee T.;
RT "TGF-beta signaling activates steroid hormone receptor expression during
RT neuronal remodeling in the Drosophila brain.";
RL Cell 112:303-315(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18171686; DOI=10.1242/dev.010876;
RA Zhu C.C., Boone J.Q., Jensen P.A., Hanna S., Podemski L., Locke J.,
RA Doe C.Q., O'Connor M.B.;
RT "Drosophila Activin- and the Activin-like product Dawdle function
RT redundantly to regulate proliferation in the larval brain.";
RL Development 135:513-521(2008).
CC -!- FUNCTION: Controls several aspects of neuronal morphogenesis; essential
CC for optic lobe development, EcR-B1 expression in larval brains,
CC mushroom body remodeling, dorsal neuron morphogenesis and motoneuron
CC axon guidance. Ligands Actbeta and daw act redundantly through the
CC Activin receptor Babo and its transcriptional mediator Smad2 (Smox), to
CC regulate neuroblast numbers and proliferation rates in the developing
CC larval brain. {ECO:0000269|PubMed:12581521,
CC ECO:0000269|PubMed:18171686}.
CC -!- SUBUNIT: Homodimer or heterodimer; disulfide-linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed in larval brains.
CC {ECO:0000269|PubMed:12581521, ECO:0000269|PubMed:18171686}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic, larval and adult stages.
CC {ECO:0000269|PubMed:9618266}.
CC -!- DISRUPTION PHENOTYPE: Development of larvae with small brains and
CC aberrant photoreceptor axon targeting. {ECO:0000269|PubMed:18171686}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AE014135; AAF59386.3; -; Genomic_DNA.
DR EMBL; AY121686; AAM52013.1; -; mRNA.
DR EMBL; AF454392; AAL51005.1; -; mRNA.
DR EMBL; AF054822; AAC39083.1; -; Genomic_DNA.
DR RefSeq; NP_651942.2; NM_143685.3.
DR AlphaFoldDB; O61643; -.
DR SMR; O61643; -.
DR BioGRID; 68652; 8.
DR IntAct; O61643; 2.
DR STRING; 7227.FBpp0088273; -.
DR GlyGen; O61643; 11 sites.
DR PaxDb; O61643; -.
DR EnsemblMetazoa; FBtr0089209; FBpp0088273; FBgn0024913.
DR GeneID; 43826; -.
DR KEGG; dme:Dmel_CG11062; -.
DR CTD; 43826; -.
DR FlyBase; FBgn0024913; Actbeta.
DR VEuPathDB; VectorBase:FBgn0024913; -.
DR eggNOG; KOG3900; Eukaryota.
DR HOGENOM; CLU_013135_0_0_1; -.
DR InParanoid; O61643; -.
DR OMA; KQFIWET; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; O61643; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-1502540; Signaling by Activin.
DR Reactome; R-DME-2129379; Molecules associated with elastic fibres.
DR Reactome; R-DME-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-DME-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-8941855; RUNX3 regulates CDKN1A transcription.
DR Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
DR BioGRID-ORCS; 43826; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43826; -.
DR PRO; PR:O61643; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0024913; Expressed in brain and 28 other tissues.
DR Genevisible; O61643; DM.
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:0032924; P:activin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:FlyBase.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:FlyBase.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0044719; P:regulation of imaginal disc-derived wing size; IMP:FlyBase.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:FlyBase.
DR GO; GO:0009749; P:response to glucose; IEP:FlyBase.
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; 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 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; Developmental protein; Disulfide bond;
KW Glycoprotein; Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..830
FT /evidence="ECO:0000255"
FT /id="PRO_0000033742"
FT CHAIN 834..946
FT /note="Inhibin beta chain"
FT /id="PRO_0000033743"
FT REGION 115..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 837..846
FT /evidence="ECO:0000250"
FT DISULFID 845..912
FT /evidence="ECO:0000250"
FT DISULFID 874..943
FT /evidence="ECO:0000250"
FT DISULFID 878..945
FT /evidence="ECO:0000250"
FT DISULFID 911
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 275
FT /note="I -> V (in Ref. 4; AAL51005)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="I -> T (in Ref. 4; AAL51005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 108792 MW; 7CECD6E73EAA306B CRC64;
MRFAFDSNHS QSGAPFKGSR CFFNCQCICC RQGCCVVVVK CCCCFNLNCC NSLGSRKSFP
QPAAMRKKVA DLEVLRVSRF VAVILVLARW VTAVATLLTS CILLDIFSVP GQSGVADRSQ
ASSRTVHVSV PTTPNETPSS TSETKLKLLY GYTSYDINND QQVKSNNLCR VLCKSRNRKR
QRRRRRRRNH RRRRHRYTKR LHHLMQDNMS GFEQRLNFSD AKCQSLETNY GTNYDLVQGG
KLFSQSERSL LVSPLREIEA PWPAIHGSMR NCSKIKRNRA NLIWLLIGLV WFEVKLINCN
GISSSNYYAS NLESHKGCTL CHESGKPNIY TDKDNPHTDY NIYNKYHSNN NFNKKTNQPH
NNIAPSDEVR LESIKRQILT KLGLSHKPNV SHPLPKQFIW ETIYRVDGGR MIPNNAFGSS
GKNLDQKTIK LRAFASPGSH LFNGRGGRTD QRSERDPSHH KYRSPFDFTF NISKNNVYGK
VLRNRSLERI DKKNSFLNGW TENRQLKINS QIASMPIELK SHHNSSPKEL KSGAVRKVNG
INGTQMNENA LKKSTYPIDI NHSIDNKTHT GKNGEMSHND YEYFNDYSVQ THDKNRYHEG
RSSIGYQPAI HNIEYENQKG HHESFADDHE NIDHEDFFGN TQEIITFAEE GTQYRQYRIL
EFSAQNRRVP SQKLSIRSAQ IHIRIDKPHS LWIEKAKSLP EKHLLNTKRK WGANKPHHRI
KIWVFQLSTS INITEKGIDK AIIFRASFQV DPKNLGWQKF DLTDTIREWY GHTSHEKLRL
LIDCTGCGGR YSLHLFQTSK LRGNSSDYLS TNPNRPFLVL HTESSRTRRV RRRAVDCGGA
LNGQCCKESF YVSFKALGWD DWIIAPRGYF ANYCRGDCTG SFRTPDTFQT FHAHFIEEYR
KMGLMNGMRP CCAPIKFSSM SLIYYGDDGI IKRDLPKMVV DECGCP
