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P42279 (TRYU_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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 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
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Non-traceable author statement PubMed 12568721. Source: FlyBase

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from sequence or structural similarity PubMed 9305763. 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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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

EMBL
GenBank
DDBJ
U04853 Genomic DNA. Translation: AAA17455.1.
AE013599 Genomic DNA. Translation: AAF58662.1.
BT012306 mRNA. Translation: AAS77431.1.
RefSeqNP_523692.1. NM_078968.2.
UniGeneDm.23664.

3D structure databases

ProteinModelPortalP42279.
SMRP42279. Positions 28-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62010. 1 interaction.
MINTMINT-317423.

Protein family/group databases

MEROPSS01.117.

Proteomic databases

PaxDbP42279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088163; FBpp0087259; FBgn0011554.
GeneID36217.
KEGGdme:Dmel_CG12386.
UCSCCG12386-RA. d. melanogaster.

Organism-specific databases

CTD36217.
FlyBaseFBgn0011554. etaTry.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00620000088101.
InParanoidP42279.
KOK01312.
OMAYWRPISE.
OrthoDBEOG75B84T.
PhylomeDBP42279.

Gene expression databases

BgeeP42279.

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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi36217.
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: April 16, 2014
This is version 104 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