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Protein

Serine protease easter

Gene

ea

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo (PubMed:9477324, PubMed:2107028, PubMed:12493753). Three proteases; ndl, gd and snk process easter to create active easter (PubMed:9477324). Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo (PubMed:9477324).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei173Charge relay systemPROSITE-ProRule annotation1
Metal bindingi193CalciumBy similarity1
Metal bindingi195Calcium; via carbonyl oxygenBy similarity1
Metal bindingi198Calcium; via carbonyl oxygenBy similarity1
Metal bindingi201CalciumBy similarity1
Active sitei240Charge relay systemPROSITE-ProRule annotation1
Active sitei338Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

  • endopeptidase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: FlyBase

GO - Biological processi

  • dorsal/ventral axis specification Source: FlyBase
  • dorsal/ventral pattern formation Source: UniProtKB
  • maternal specification of dorsal/ventral axis, oocyte, germ-line encoded Source: FlyBase
  • proteolysis Source: FlyBase
  • Toll signaling pathway Source: FlyBase
  • ventral furrow formation Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Hydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-209442 Formation of the trans-membrane 'signalling complex'

Protein family/group databases

MEROPSiS01.201

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease easter (EC:3.4.21.-)
Gene namesi
Name:ea
ORF Names:CG4920
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000533 ea

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi131G → E in EA 20N; results in extreme lateralized embryonic pattern where the most dorsal pattern elements (e.g. dorsal cuticles) and the most ventral pattern element (mesoderm) are absent. 1 Publication1
Mutagenesisi172S → L in EA 111; results in temperature-sensitive defects in dorsoventral patterning. 1 Publication1
Mutagenesisi193E → A or K: Probable loss of calcium binding which might affect catalytic activity. Results in defective dorsoventral patterning showing a complete dorsalization in which there is no ventral furrow or headfold, cells at the posterior do not migrate, and multiple symmetric folds appear along the anterior-posterior axis of the embryo. 1 Publication1
Mutagenesisi283G → S in EA 84B; results in weakly ventralized embryos with ventral denticle bands that are approximately normal in width and the filzkorper have the normal tubular morphology. 1 Publication1
Mutagenesisi324C → Y in EA 818; results in temperature-sensitive defects in dorsoventral patterning. 1 Publication1
Mutagenesisi325A → V in EA 83I and EA 4102; results in ventralized embryos. 1 Publication1
Mutagenesisi335R → C in EA 125.3; results in ventralized embryos. 1 Publication1
Mutagenesisi335R → Q in EA QGDS; results in lateralised embryos. 1 Publication1
Mutagenesisi336G → S in EA 12A; results in weakly ventralized embryos with ventral denticle bands that are approximately normal in width and the filzkorper have the normal tubular morphology. 1 Publication1
Mutagenesisi338S → A: Loss of catalytic activity results in defective dorsoventral patterning characterized by a complete dorsalization in which there is no ventral furrow or headfold, cells at the posterior do not migrate, and multiple symmetric folds appear along the anterior-posterior axis of the embryo. 2 Publications1
Mutagenesisi339G → R in EA 1; results in completely dorsalized embryos. 1 Publication1
Mutagenesisi360V → M in EA 5.13; results in extreme lateralized embryonic pattern where the most dorsal pattern elements (e.g. dorsal cuticle) and the most ventral pattern element (mesoderm) are absent. 1 Publication1
Mutagenesisi363G → E in EA 8; results in completely dorsalized embryos. 1 Publication1
Mutagenesisi371G → R in EA 161.13; results in weakly ventralized embryos with ventral denticle bands that are approximately normal in width and the filzkorper have the normal tubular morphology. 1 Publication1
Mutagenesisi373P → I or Y: Probable loss of catalytic activity results in partially defective dorsoventral patterning; during gastrulation, shows defective ventralization; in late embryogenesis results in moderately dorsalized embryos presenting defective lateral filzkorper, head skeleton and ventral denticles. 1 Publication1
Mutagenesisi373P → S in EA 5022; probable loss of catalytic activity results in partially defective dorsoventral patterning; in gastrulation, shows an intermediate ventralization with the headfold prominent on the dorsal side and some anteriorward displacement of posterior cells along the dorsal site; in late embryogenesis, shows partial filzkorper and head skeleton, as well as ventral denticles erroneously in dorsal position. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19CuratedAdd BLAST19
PropeptideiPRO_000002813320 – 127Activation peptideSequence analysisAdd BLAST108
ChainiPRO_0000028134128 – 392Serine protease easterAdd BLAST265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi37 ↔ 88By similarity
Disulfide bondi47 ↔ 78By similarity
Disulfide bondi53 ↔ 89By similarity
Disulfide bondi120 ↔ 260By similarity
Disulfide bondi158 ↔ 174PROSITE-ProRule annotation
Disulfide bondi202 ↔ 212By similarity
Disulfide bondi307 ↔ 324PROSITE-ProRule annotation
Disulfide bondi334 ↔ 367PROSITE-ProRule annotation

Post-translational modificationi

Activation peptide and active catalytic domain are associated by a disulfide bond. Processed easter is present in extremely low amounts in the early embryo as it is rapidly converted into a high molecular mass complex, which may contain a protease inhibitor. Zymogen activation is also controlled by a negative feedback loop from Dorsal.

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP13582
PRIDEiP13582

Miscellaneous databases

PMAP-CutDBiP13582

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiFBgn0000533
ExpressionAtlasiP13582 baseline and differential
GenevisibleiP13582 DM

Interactioni

Protein-protein interaction databases

BioGridi66921, 14 interactors
DIPiDIP-18843N
IntActiP13582, 1 interactor
STRINGi7227.FBpp0082539

Structurei

3D structure databases

ProteinModelPortaliP13582
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 89CLIPSequence analysisAdd BLAST53
Domaini128 – 391Peptidase S1PROSITE-ProRule annotationAdd BLAST264

Domaini

The CLIP domain consists of 37-55 residues which are "knitted" together usually by 3 conserved disulfide bonds forming a clip-like compact structure.Curated

Sequence similaritiesi

Belongs to the peptidase S1 family. CLIP subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
InParanoidiP13582
OrthoDBiEOG091G0DF7
PhylomeDBiP13582

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di2.20.20.90, 1 hit
InterProiView protein in InterPro
IPR022700 CLIP
IPR038565 CLIP_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF12032 CLIP, 1 hit
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00680 CLIP, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKPSIICLF LGILAKSSAG QFYFPNEAAQ VPNYGRCITP NRERALCIHL
60 70 80 90 100
EDCKYLYGLL TTTPLRDTDR LYLSRSQCGY TNGKVLICCP DRYRESSSET
110 120 130 140 150
TPPPKPNVTS NSLLPLPGQC GNILSNRIYG GMKTKIDEFP WMALIEYTKS
160 170 180 190 200
QGKKGHHCGG SLISTRYVIT ASHCVNGKAL PTDWRLSGVR LGEWDTNTNP
210 220 230 240 250
DCEVDVRGMK DCAPPHLDVP VERTIPHPDY IPASKNQVND IALLRLAQQV
260 270 280 290 300
EYTDFVRPIC LPLDVNLRSA TFDGITMDVA GWGKTEQLSA SNLKLKAAVE
310 320 330 340 350
GSRMDECQNV YSSQDILLED TQMCAGGKEG VDSCRGDSGG PLIGLDTNKV
360 370 380 390
NTYYFLAGVV SFGPTPCGLA GWPGVYTLVG KYVDWIQNTI ES
Length:392
Mass (Da):43,065
Last modified:November 7, 2003 - v3
Checksum:i1309C41E6FC176B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti302S → F in AAF55170 (PubMed:10731132).Curated1
Sequence conflicti302S → F in AAQ22447 (PubMed:10731132).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03154 mRNA Translation: AAA28496.1
AE014297 Genomic DNA Translation: AAF55170.1
BT009978 mRNA Translation: AAQ22447.1
PIRiA30100
RefSeqiNP_524362.2, NM_079638.3
UniGeneiDm.2421

Genome annotation databases

GeneIDi41858
KEGGidme:Dmel_CG4920
UCSCiCG4920-RA d. melanogaster

Similar proteinsi

Entry informationi

Entry nameiEAST_DROME
AccessioniPrimary (citable) accession number: P13582
Secondary accession number(s): Q9VF90
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 7, 2003
Last modified: May 23, 2018
This is version 155 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health