60A_DROME
ID 60A_DROME Reviewed; 455 AA.
AC P27091; Q9W1I4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein 60A;
DE AltName: Full=Protein glass bottom boat;
DE Flags: Precursor;
GN Name=gbb; Synonyms=60A, gbb-60A, TGFb-60A; ORFNames=CG5562;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=1924384; DOI=10.1073/pnas.88.20.9214;
RA Wharton K.A., Thomsen G.H., Gelbart W.M.;
RT "Drosophila 60A gene, another transforming growth factor beta family
RT member, is closely related to human bone morphogenetic proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9214-9218(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1601181; DOI=10.1016/0012-1606(92)90188-m;
RA Doctor J.S., Jackson P.D., Rashka K.E., Visalli M., Hoffmann F.M.;
RT "Sequence, biochemical characterization, and developmental expression of a
RT new member of the TGF-beta superfamily in Drosophila melanogaster.";
RL Dev. Biol. 151:491-505(1992).
RN [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9636086; DOI=10.1242/dev.125.14.2723;
RA Khalsa O., Yoon J.-W., Torres-Schumann S., Wharton K.A.;
RT "TGF-beta/BMP superfamily members, Gbb-60A and Dpp, cooperate to provide
RT pattern information and establish cell identity in the Drosophila wing.";
RL Development 125:2723-2734(1998).
CC -!- FUNCTION: Required for the growth of imaginal tissues and for
CC patterning of the adult wing. {ECO:0000269|PubMed:9636086}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:1601181}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1601181}.
CC -!- TISSUE SPECIFICITY: Expressed in cells of the developing foregut and
CC hindgut during germ band retraction and later embryonic stages.
CC Expressed in the wing disk, mainly in the posterior compartment in the
CC pteropleural and medial regions extending into the progenitors of the
CC scutellum. High levels are found within the posterior and anterior
CC compartments of the wing pouch and low levels in the hinge region. In
CC the eye/antennal disk, expression is highest anterior to the
CC morphogenetic furrow and in the medial regions with lower levels of
CC expression posterior to the morphogenetic furrow. Expressed throughout
CC the posterior compartment of the leg imaginal disks and within the
CC ventral anterior compartment. {ECO:0000269|PubMed:1601181,
CC ECO:0000269|PubMed:9636086}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development with peaks of
CC transcription during early embryogenesis, in pupae, and in adult males.
CC {ECO:0000269|PubMed:1601181, ECO:0000269|PubMed:1924384}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit transparent larvae, and a reduction
CC of the adult wing size. {ECO:0000269|PubMed:9636086}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; M77012; AAA28306.1; -; Genomic_DNA.
DR EMBL; M84795; AAA28307.1; -; mRNA.
DR EMBL; AE013599; AAF47075.1; -; Genomic_DNA.
DR PIR; A43918; A43918.
DR RefSeq; NP_001286786.1; NM_001299857.1.
DR RefSeq; NP_477340.1; NM_057992.3.
DR AlphaFoldDB; P27091; -.
DR SMR; P27091; -.
DR BioGRID; 63372; 36.
DR DIP; DIP-19466N; -.
DR IntAct; P27091; 3.
DR STRING; 7227.FBpp0072036; -.
DR GlyGen; P27091; 3 sites.
DR PaxDb; P27091; -.
DR PRIDE; P27091; -.
DR EnsemblMetazoa; FBtr0072127; FBpp0072036; FBgn0024234.
DR EnsemblMetazoa; FBtr0343274; FBpp0309939; FBgn0024234.
DR GeneID; 37778; -.
DR KEGG; dme:Dmel_CG5562; -.
DR CTD; 37778; -.
DR FlyBase; FBgn0024234; gbb.
DR VEuPathDB; VectorBase:FBgn0024234; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000167023; -.
DR HOGENOM; CLU_020515_4_1_1; -.
DR InParanoid; P27091; -.
DR OMA; KVPNDNY; -.
DR OrthoDB; 1063560at2759; -.
DR PhylomeDB; P27091; -.
DR BioGRID-ORCS; 37778; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Gbeta13F; fly.
DR GenomeRNAi; 37778; -.
DR PRO; PR:P27091; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0024234; Expressed in seminal fluid secreting gland and 40 other tissues.
DR ExpressionAtlas; P27091; baseline and differential.
DR Genevisible; P27091; DM.
DR GO; GO:0031045; C:dense core granule; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:FlyBase.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0007504; P:larval fat body development; IMP:FlyBase.
DR GO; GO:0099558; P:maintenance of synapse structure; IGI:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0048636; P:positive regulation of muscle organ development; IGI:FlyBase.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:FlyBase.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IDA:FlyBase.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IGI:FlyBase.
DR GO; GO:0098917; P:retrograde trans-synaptic signaling; IGI:FlyBase.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 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; Cytokine; Developmental protein;
KW Disulfide bond; Glycoprotein; Growth factor; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT PROPEP 37..335
FT /evidence="ECO:0000255"
FT /id="PRO_0000033660"
FT CHAIN 336..455
FT /note="Protein 60A"
FT /id="PRO_0000033661"
FT REGION 108..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 354..420
FT /evidence="ECO:0000250"
FT DISULFID 383..452
FT /evidence="ECO:0000250"
FT DISULFID 387..454
FT /evidence="ECO:0000250"
FT DISULFID 419
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 51687 MW; C8FA795556341F94 CRC64;
MSGLRNTSEA VAVLASLGLG MVLLMFVATT PPAVEATQSG IYIDNGKDQT IMHRVLSEDD
KLDVSYEILE FLGIAERPTH LSSHQLSLRK SAPKFLLDVY HRITAEEGLS DQDEDDDYER
GHRSRRSADL EEDEGEQQKN FITDLDKRAI DESDIIMTFL NKRHHNVDEL RHEHGRRLWF
DVSNVPNDNY LVMAELRIYQ NANEGKWLTA NREFTITVYA IGTGTLGQHT MEPLSSVNTT
GDYVGWLELN VTEGLHEWLV KSKDNHGIYI GAHAVNRPDR EVKLDDIGLI HRKVDDEFQP
FMIGFFRGPE LIKATAHSSH HRSKRSASHP RKRKKSVSPN NVPLLEPMES TRSCQMQTLY
IDFKDLGWHD WIIAPEGYGA FYCSGECNFP LNAHMNATNH AIVQTLVHLL EPKKVPKPCC
APTRLGALPV LYHLNDENVN LKKYRNMIVK SCGCH
