P42276 (TRYDG_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Probable
	Propeptide	23 – 30	8	Activation peptide		PRO_0000028269
	Chain	31 – 253	223	Trypsin delta/gamma		PRO_0000028270
Regions
	Domain	31 – 253	223	Peptidase S1
Sites
	Active site	71	1	Charge relay system By similarity
	Active site	116	1	Charge relay system By similarity
	Active site	210	1	Charge relay system By similarity
	Site	204	1	Required for specificity By similarity
Amino acid modifications
	Disulfide bond	56 ↔ 72		By similarity
	Disulfide bond	180 ↔ 197		By similarity
	Disulfide bond	206 ↔ 230		By similarity
Experimental info
	Sequence conflict	118	1	A → V in AAA17449. Ref.1
	Sequence conflict	118	1	A → V in AAA17450. Ref.1
	Sequence conflict	148	1	A → G in AAA17449. Ref.1
	Sequence conflict	148	1	A → G in AAA17450. Ref.1
	Sequence conflict	240	1	A → S in AAA17449. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42276 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: F77D47E0CCC78F92	FASTA	253	25,680
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
RefSeq	NP_523694.2. NM_078970.4. NP_725034.1. NM_165823.3. NP_725035.1. NM_165824.3.
UniGene	Dm.14041. Dm.21711.
3D structure databases
ProteinModelPortal	P42276.
SMR	P42276. Positions 31-253.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0087224.
Protein family/group databases
MEROPS	S01.A84.
Proteomic databases
PaxDb	P42276.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088123; FBpp0087224; FBgn0050031. FBtr0088124; FBpp0087225; FBgn0010358. FBtr0088159; FBpp0087255; FBgn0010359.
GeneID	246404. 36221. 48343.
KEGG	dme:Dmel_CG12351. dme:Dmel_CG30028. dme:Dmel_CG30031.
UCSC	CG12351-RA. d. melanogaster.
Organism-specific databases
CTD	36221. 48343.
FlyBase	FBgn0050031. CG30031. FBgn0010358. deltaTry. FBgn0010359. gammaTry.
Phylogenomic databases
eggNOG	COG5640.
GeneTree	ENSGT00620000088101.
InParanoid	P42276.
KO	K01312.
OMA	TIGSFPW.
OrthoDB	EOG4M37RJ.
PhylomeDB	P42276.
Gene expression databases
GermOnline	CG12351. Drosophila melanogaster. CG30028. Drosophila melanogaster. CG30031. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	842323.

Entry information

Entry name

TRYDG_DROME

Accession

Primary (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:	April 3, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project