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Reviewed, UniProtKB/Swiss-Prot P42279 (TRYU_DROME)

Last modified November 3, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trypsin eta
    EC=3.4.21.4
Gene names
Name: etaTry
ORF Names: CG12386
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length262 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
Gene Ontology (GO)
   Biological processproteolysis

Non-traceable author statement. Source: FlyBase

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Non-traceable author statement. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 275Activation peptide
PRO_0000028283
Chain28 – 262235Trypsin eta
PRO_0000028284

Regions

Domain28 – 259232Peptidase S1

Sites

Active site741Charge relay system By similarity
Active site1201Charge relay system By similarity
Active site2151Charge relay system By similarity
Site2091Required for specificity By similarity

Amino acid modifications

Disulfide bond59 ↔ 75 By similarity
Disulfide bond185 ↔ 200 By similarity
Disulfide bond211 ↔ 235 By similarity

Experimental info

Sequence conflict81I → V in AAA17455. Ref.1
Sequence conflict241S → P in AAA17455. Ref.1
Sequence conflict881A → S in AAA17455. Ref.1
Sequence conflict971N → Y in AAA17455. Ref.1
Sequence conflict1051K → Q in AAA17455. Ref.1
Sequence conflict1421E → V in AAA17455. Ref.1
Sequence conflict1491A → P in AAA17455. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42279-1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: BE908F7602A611DC

FASTA26228,088
        10         20         30         40         50         60 
MNKVILRILA VLFLLGIYAV SAQSDGRIVG GADTSSYYTK YVVQLRRRSS SSSSYAQTCG 

        70         80         90        100        110        120 
GCILDAVTIA TAAHCVYNRE AENFLVVAGD DSRGGMNGVV VRVSKLIPHE LYNSSTMDND 

       130        140        150        160        170        180 
IALVVVDPPL PLDSFSTMEA IEIASEQPAV GVQATISGWG YTKENGLSSD QLQQVKVPIV 

       190        200        210        220        230        240 
DSEKCQEAYY WRPISEGMLC AGLSEGGKDA CQGDSGGPLV VANKLAGIVS WGEGCARPNY 

       250        260 
PGVYANVAYY KDWIAKQRTS YV 

« 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: 10486967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-262.
Strain: Berkeley.
Tissue: Larva and Pupae.
+Additional computationally mapped references.

Cross-references

Sequence databases

U04853 Genomic DNA. Translation: AAA17455.1.
AE013599 Genomic DNA. Translation: AAF58662.1.
BT012306 mRNA. Translation: AAS77431.1.
RefSeqNP_523692.1.
UniGeneDm.23664

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBaseSearch...

Protein-protein interaction databases

IntActP42279. 1 interaction.

Protein family/group databases

MEROPSS01.117.

Genome annotation databases

EnsemblFBtr0088163; FBpp0087259; FBgn0011554; Drosophila melanogaster. [Genome view]
GeneID36217.
KEGGdme:Dmel_CG12386.
NMPDRfig|7227.3.peg.4634.
UCSCCG12386-RA. d. melanogaster.

Organism-specific databases

CTD36217.
FlyBaseFBgn0011554. etaTry.

Phylogenomic databases

HOGENOMP42279.
OMAYWRPISE.

Enzyme and pathway databases

BRENDA3.4.21.4. 48.

Gene expression databases

GermOnlineCG12386. Drosophila melanogaster.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. False negative.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio797389.

Entry information

Entry nameTRYU_DROME
AccessionPrimary (citable) accession number: P42279
Secondary accession number(s): Q6NLM5, Q9V5X9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 16, 2005
Last modified: November 3, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents