GD_DROME
ID GD_DROME Reviewed; 531 AA.
AC O62589; D9PTR2; M9PEE0; M9PGY7; M9PJK1; Q1EC38;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Serine protease gd;
DE EC=3.4.21.-;
DE AltName: Full=Protein gastrulation defective;
DE Flags: Precursor;
GN Name=gd; ORFNames=CG1505;
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 / MRNA] (ISOFORM C), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9618496; DOI=10.1073/pnas.95.12.6819;
RA Konrad K.D., Goralski T.J., Mahowald A.P., Marsh J.L.;
RT "The gastrulation defective gene of Drosophila melanogaster is a member of
RT the serine protease superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6819-6824(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley;
RA Stapleton M., Booth B., Carlson J., Chavez C., Frise E., George R.,
RA Pacleb J., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CLEAVAGE OF EASTER, AND SUBCELLULAR LOCATION.
RX PubMed=9477324; DOI=10.1242/dev.125.7.1261;
RA Misra S., Hecht P., Maeda R., Anderson K.V.;
RT "Positive and negative regulation of Easter, a member of the serine
RT protease family that controls dorsal-ventral patterning in the Drosophila
RT embryo.";
RL Development 125:1261-1267(1998).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF TYR-513.
RX PubMed=12493753; DOI=10.1074/jbc.m211820200;
RA Rose T., LeMosy E.K., Cantwell A.M., Banerjee-Roy D., Skeath J.B.,
RA Di Cera E.;
RT "Three-dimensional models of proteases involved in patterning of the
RT Drosophila Embryo. Crucial role of predicted cation binding sites.";
RL J. Biol. Chem. 278:11320-11330(2003).
CC -!- FUNCTION: Component of the extracellular signaling pathway that
CC establishes the dorsal-ventral pathway of the embryo (PubMed:9618496,
CC PubMed:9477324, PubMed:12493753). Three proteases; ndl, gd and snk
CC process easter to create active easter (PubMed:9477324). Active easter
CC defines cell identities along the dorsal-ventral continuum by
CC activating the spz ligand for the Tl receptor in the ventral region of
CC the embryo (PubMed:9477324). {ECO:0000269|PubMed:12493753,
CC ECO:0000269|PubMed:9477324, ECO:0000269|PubMed:9618496}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9477324}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=D {ECO:0000312|FlyBase:FBgn0000808};
CC IsoId=O62589-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0000808}; Synonyms=F
CC {ECO:0000312|FlyBase:FBgn0000808};
CC IsoId=O62589-2; Sequence=VSP_054451;
CC Name=E {ECO:0000312|FlyBase:FBgn0000808};
CC IsoId=O62589-3; Sequence=VSP_054451, VSP_054452, VSP_054453;
CC -!- TISSUE SPECIFICITY: Expression begins in previtellogenic stages and is
CC seen in germline-derived nurse cells of the germarium. Expression
CC continues throughout oogenesis with transcripts from the nurse cells
CC accumulating in the oocytes. Most abundant in the ovaries, the level of
CC protein decreases from the moment of egg laying and is essentially gone
CC by 4 hours. {ECO:0000269|PubMed:9618496}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9618496}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG02140.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABG02140.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=ADK93997.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF056311; AAC13558.1; -; mRNA.
DR EMBL; U09808; AAC24235.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48122.3; -; Genomic_DNA.
DR EMBL; AE014298; AGB95321.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95322.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95323.1; -; Genomic_DNA.
DR EMBL; BT025896; ABG02140.1; ALT_SEQ; mRNA.
DR EMBL; BT125069; ADK93997.1; ALT_INIT; mRNA.
DR RefSeq; NP_001259478.1; NM_001272549.1. [O62589-2]
DR RefSeq; NP_001259479.1; NM_001272550.1. [O62589-1]
DR RefSeq; NP_001259480.1; NM_001272551.1. [O62589-3]
DR RefSeq; NP_001303552.1; NM_001316623.1. [O62589-2]
DR AlphaFoldDB; O62589; -.
DR SMR; O62589; -.
DR BioGRID; 58564; 4.
DR IntAct; O62589; 1.
DR STRING; 7227.FBpp0304588; -.
DR MEROPS; S01.202; -.
DR GlyGen; O62589; 3 sites.
DR PaxDb; O62589; -.
DR DNASU; 32159; -.
DR EnsemblMetazoa; FBtr0332308; FBpp0304587; FBgn0000808. [O62589-2]
DR EnsemblMetazoa; FBtr0332309; FBpp0304588; FBgn0000808. [O62589-1]
DR EnsemblMetazoa; FBtr0332310; FBpp0304589; FBgn0000808. [O62589-3]
DR EnsemblMetazoa; FBtr0347416; FBpp0312566; FBgn0000808. [O62589-2]
DR GeneID; 32159; -.
DR KEGG; dme:Dmel_CG1505; -.
DR CTD; 619206; -.
DR FlyBase; FBgn0000808; gd.
DR VEuPathDB; VectorBase:FBgn0000808; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000171626; -.
DR InParanoid; O62589; -.
DR OMA; FIDWIMA; -.
DR Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
DR BioGRID-ORCS; 32159; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32159; -.
DR PRO; PR:O62589; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000808; Expressed in egg cell and 3 other tissues.
DR ExpressionAtlas; O62589; baseline and differential.
DR Genevisible; O62589; DM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0098595; C:perivitelline space; IDA:FlyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:UniProtKB.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IDA:FlyBase.
DR GO; GO:0006508; P:proteolysis; IDA:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IMP:FlyBase.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR031986; GD_N.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF16030; GD_N; 1.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..531
FT /note="Serine protease gd"
FT /id="PRO_0000028135"
FT DOMAIN 246..531
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 295
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 350
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 471
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 432..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 72..74
FT /note="Missing (in isoform C and isoform E)"
FT /evidence="ECO:0000303|PubMed:9618496, ECO:0000303|Ref.4"
FT /id="VSP_054451"
FT VAR_SEQ 178..182
FT /note="KPFAQ -> YASGF (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_054452"
FT VAR_SEQ 183..531
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_054453"
FT MUTAGEN 513
FT /note="Y->A,P: Results in a defective gastrulation with
FT excessive ventralization showing very prominent ventral
FT furrow, no anterior displacement of posterior cells and
FT only a small headfold on the dorsal side of the embryo."
FT /evidence="ECO:0000269|PubMed:12493753"
SQ SEQUENCE 531 AA; 59477 MW; D420F2879DB92C97 CRC64;
MRLHLAAILI LCIEHVTKAV AQGMPISPCP KVFQYRFDGS EWFGLMAVRS PDGHQPLHIR
VTLSMRGKPT TYTQNYLGEI ELLTRGKFTH NAPVLYKIRF PKHHFPPKLL LMSANNHVIC
FGSGEHSIFM TQIQLEHIRK LSFIPDKKSS LLLDPEEEEV RKTDDKPPST PHIQFKKKPF
AQAPKEICGR IDRDLDFHLS QRTESLHVAI GEPKSSDGIT SPVFVDDDED DVLEHQFVDE
SEAEAIESDS ADSLPSITRG SWPWLAAIYV NNLTSLDFQC GGSLVSARVV ISSAHCFKLF
NKRYTSNEVL VFLGRHNLKN WNEEGSLAAP VDGIYIHPDF NSQLSSYDAD IAVIILKDEV
RFNTFIRPAC LWSGSSKTEY IVGERGIVIG WSFDRTNRTR DQKLSSELPG KKSTDASAPK
VVKAPIVGNA ECFRANAHFR SLSSNRTFCA GIQAEERDTH QSGASIYTGI SGAGLFIRRN
NRWMLRGTVS AALPAVETPD AESSHKLCCK NQYIIYADVA KFLDWITAFV I
