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P42280 (TRYZ_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. 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
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 zeta
EC=3.4.21.4
Gene names
Name:zetaTry
ORF Names:CG12387
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length280 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

Secreted › extracellular 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

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 Probable
Propeptide23 – 3816Activation peptide
PRO_0000028287
Chain39 – 280242Trypsin zeta
PRO_0000028288

Regions

Domain39 – 278240Peptidase S1

Sites

Active site871Charge relay system By similarity
Active site1341Charge relay system By similarity
Active site2341Charge relay system By similarity
Site2281Required for specificity By similarity

Amino acid modifications

Disulfide bond72 ↔ 88 By similarity
Disulfide bond198 ↔ 218 By similarity
Disulfide bond230 ↔ 254 By similarity

Experimental info

Sequence conflict861A → G in AAA17456. Ref.1
Sequence conflict1451P → A in AAA17456. Ref.1
Sequence conflict1531A → G in AAA17456. Ref.1
Sequence conflict1581L → S in AAA17456. Ref.1
Sequence conflict2221R → P in AAA17456. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42280 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 99A2D76557C308FC

FASTA28029,738
        10         20         30         40         50         60 
MSSSWIVGLL AFLVSLVALT QGLPLLEDLD EKSVPDGRIV GGYATDIAQV PYQISLRYKG 

        70         80         90        100        110        120 
ITTPENPFRH RCGGSIFNET TIVTAAHCVI GTVASQYKVV AGTNFQTGSD GVITNVKEIV 

       130        140        150        160        170        180 
MHEGYYSGAA YNNDIAILFV DPPLPLNNFT IKAIKLALEQ PIEGTVSKVS GWGTTSPGGY 

       190        200        210        220        230        240 
SSNQLLAVDV PIVSNELCDQ DYEDFGDETY RITSAMLCAG KRGVGGADAC QGDSGGPLAV 

       250        260        270        280 
RDELYGVVSW GNSCALPNYP GVYANVAYLR PWIDAVLAGL

« 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.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U04853 Genomic DNA. Translation: AAA17456.1.
AE013599 Genomic DNA. Translation: AAF58663.1.
AY113523 mRNA. Translation: AAM29528.1.
RefSeqNP_523691.1. NM_078967.3.
UniGeneDm.2633.

3D structure databases

ProteinModelPortalP42280.
SMRP42280. Positions 39-276.
ModBaseSearch...

Protein-protein interaction databases

IntActP42280. 2 interactions.
MINTMINT-297272.

Protein family/group databases

MEROPSS01.116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088164; FBpp0087260; FBgn0011556.
GeneID36216.
KEGGdme:Dmel_CG12387.
NMPDRfig|7227.3.peg.4633.
UCSCCG12387-RA. d. melanogaster.

Organism-specific databases

CTD36216.
FlyBaseFBgn0011556. zetaTry.

Phylogenomic databases

eggNOGinNOG07667.
GeneTreeEMGT00050000002488.
InParanoidP42280.
OMAAYNNDIA.
OrthoDBEOG408KR6.
PhylomeDBP42280.

Gene expression databases

BgeeP42280.
GermOnlineCG12387. Drosophila melanogaster.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
KOK01312.
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio797384.

Entry information

Entry nameTRYZ_DROME
AccessionPrimary (citable) accession number: P42280
Secondary accession number(s): Q9V5X8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 16, 2005
Last modified: January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents