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P35004 (TRYB_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 107. 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 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

Non-traceable author statement PubMed 12568721. Source: FlyBase

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Non-traceable author statement PubMed 12568721. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Probable
Propeptide23 – 308Activation peptide
PRO_0000028265
Chain31 – 253223Trypsin beta
PRO_0000028266

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 conflict531S → R in AAA28980. Ref.1
Sequence conflict531S → R in AAA17451. Ref.2
Sequence conflict851A → G in AAA28980. Ref.1
Sequence conflict851A → G in AAA17451. Ref.2
Sequence conflict114 – 1152VN → TS in AAA28980. Ref.1
Sequence conflict114 – 1152VN → TS in AAA17451. Ref.2
Sequence conflict1211H → N in AAA28980. Ref.1
Sequence conflict1211H → N in AAA17451. Ref.2
Sequence conflict1421P → T in AAA28980. Ref.1
Sequence conflict1421P → T in AAA17451. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35004 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 3F5D35D235B8D8CD

FASTA25325,693
        10         20         30         40         50         60 
MLKFLILLSA VACALGGTIP EGLLPQLDGR IVGGTATTIS SFPWQISLQR SGSHSCGGSI 

        70         80         90        100        110        120 
YSARVIVTAA HCLQSVSASS LQIRAGSSYW SSGGVVAKVS SFKNHEGYNA NTMVNDIAVL 

       130        140        150        160        170        180 
HLSSSLSFSS TIKAIGLASS NPANGAAASV SGWGTESSGS SSIPSQLRYV NVNIVSQSRC 

       190        200        210        220        230        240 
SSSSYGYGNQ IKSSMICAFA SGKDSCQGDS GGPLVSGGVL VGVVSWGYGC AAANYPGVYA 

       250 
DVAALRSWVI NNA 

« 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]Wang S., Magoulas C., Hickey D.A.
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Oregon-R.
[3]"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.
[4]"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.
[5]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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Larva and Pupae.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96372 Genomic DNA. Translation: AAA28980.1.
U04853 Genomic DNA. Translation: AAA17451.1.
AE013599 Genomic DNA. Translation: AAF58658.2.
BT016077 mRNA. Translation: AAV36962.1.
RefSeqNP_524904.1. NM_080165.2.
UniGeneDm.11279.

3D structure databases

ProteinModelPortalP35004.
SMRP35004. Positions 31-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0087223.

Protein family/group databases

MEROPSS01.A83.

Proteomic databases

PaxDbP35004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088122; FBpp0087223; FBgn0010357.
GeneID47901.
KEGGdme:Dmel_CG18211.
UCSCCG18211-RA. d. melanogaster.

Organism-specific databases

CTD47901.
FlyBaseFBgn0010357. betaTry.

Phylogenomic databases

eggNOGNOG245986.
GeneTreeENSGT00620000088101.
InParanoidP35004.
KOK01312.
OMAMICAFAS.
OrthoDBEOG7MKW6Q.
PhylomeDBP35004.

Gene expression databases

BgeeP35004.

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

GenomeRNAi47901.
NextBio839220.

Entry information

Entry nameTRYB_DROME
AccessionPrimary (citable) accession number: P35004
Secondary accession number(s): Q9V5Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 16, 2005
Last modified: November 13, 2013
This is version 107 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