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P42276 (TRYDG_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trypsin delta/gamma

EC=3.4.21.4
Gene names
Name:deltaTry
ORF Names:CG12351
AND
Name:gammaTry
ORF Names:CG30028
AND
ORF Names:CG30031
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from sequence model PubMed 19546158. Source: FlyBase

   Cellular_componentcytosol

Inferred from direct assay PubMed 23805892. Source: FlyBase

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from sequence model PubMed 19546158. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Probable
Propeptide23 – 308Activation peptide
PRO_0000028269
Chain31 – 253223Trypsin delta/gamma
PRO_0000028270

Regions

Domain31 – 253223Peptidase S1

Sites

Active site711Charge relay system By similarity
Active site1161Charge relay system By similarity
Active site2101Charge relay system By similarity
Site2041Required for specificity By similarity

Amino acid modifications

Disulfide bond56 ↔ 72 By similarity
Disulfide bond180 ↔ 197 By similarity
Disulfide bond206 ↔ 230 By similarity

Experimental info

Sequence conflict1181A → V in AAA17449. Ref.1
Sequence conflict1181A → V in AAA17450. Ref.1
Sequence conflict1481A → G in AAA17449. Ref.1
Sequence conflict1481A → G in AAA17450. Ref.1
Sequence conflict2401A → S in AAA17449. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42276 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: F77D47E0CCC78F92

FASTA25325,680
        10         20         30         40         50         60 
MLKFVILLSA VACALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR SGSHSCGGSI 

        70         80         90        100        110        120 
YSSNVIVTAA HCLQSVSASV LQIRAGSSYW SSGGVTFSVS SFKNHEGYNA NTMVNDIAII 

       130        140        150        160        170        180 
KINGALTFSS TIKAIGLASS NPANGAAASV SGWGTLSYGS SSIPSQLQYV NVNIVSQSQC 

       190        200        210        220        230        240 
ASSTYGYGSQ IRSTMICAAA SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA 

       250 
DVAALRSWVI SNA 

« Hide

References

« Hide 'large scale' references
[1]"Concerted evolution within a trypsin gene cluster in Drosophila."
Wang S., Magoulas C., Hickey D.A.
Mol. Biol. Evol. 16:1117-1124(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DELTATRY AND GAMMATRY).
Strain: Oregon-R.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CG30031; DELTATRY AND GAMMATRY).
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (GAMMATRY).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04853 Genomic DNA. Translation: AAA17449.1.
U04853 Genomic DNA. Translation: AAA17450.1.
AE013599 Genomic DNA. Translation: AAF58657.2.
AE013599 Genomic DNA. Translation: AAM68730.1.
AE013599 Genomic DNA. Translation: AAM68731.1.
AY075487 mRNA. Translation: AAL68297.1.
RefSeqNP_523694.2. NM_078970.4.
NP_725034.1. NM_165823.3.
NP_725035.1. NM_165824.3.
UniGeneDm.14041.
Dm.21711.
Dm.30904.

3D structure databases

ProteinModelPortalP42276.
SMRP42276. Positions 31-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0087224.

Protein family/group databases

MEROPSS01.A84.

Proteomic databases

PaxDbP42276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088123; FBpp0087224; FBgn0050031.
FBtr0088124; FBpp0087225; FBgn0010358.
FBtr0088159; FBpp0087255; FBgn0010359.
GeneID246404.
36221.
48343.
KEGGdme:Dmel_CG12351.
dme:Dmel_CG30028.
dme:Dmel_CG30031.
UCSCCG12351-RA. d. melanogaster.

Organism-specific databases

CTD36221.
48343.
FlyBaseFBgn0050031. CG30031.
FBgn0010358. deltaTry.
FBgn0010359. gammaTry.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00620000088101.
InParanoidP42276.
KOK01312.
OMATIGSFPW.
OrthoDBEOG7MKW6Q.
PhylomeDBP42276.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio842323.

Entry information

Entry nameTRYDG_DROME
AccessionPrimary (citable) accession number: P42276
Secondary accession number(s): P42277, Q8SXZ4, Q9V5Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase