P42279 (TRYU_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trypsin eta
EC=3.4.21.4

Gene names

Name:	etaTry
ORF Names:	CG12386

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	262 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 Non-traceable author statement PubMed 12568721. Source: FlyBase
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from sequence or structural similarity PubMed 9305763. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 27	5	Activation peptide		PRO_0000028283
	Chain	28 – 262	235	Trypsin eta		PRO_0000028284
Regions
	Domain	28 – 259	232	Peptidase S1
Sites
	Active site	74	1	Charge relay system By similarity
	Active site	120	1	Charge relay system By similarity
	Active site	215	1	Charge relay system By similarity
	Site	209	1	Required for specificity By similarity
Amino acid modifications
	Disulfide bond	59 ↔ 75		By similarity
	Disulfide bond	185 ↔ 200		By similarity
	Disulfide bond	211 ↔ 235		By similarity
Experimental info
	Sequence conflict	8	1	I → V in AAA17455. Ref.1
	Sequence conflict	24	1	S → P in AAA17455. Ref.1
	Sequence conflict	88	1	A → S in AAA17455. Ref.1
	Sequence conflict	97	1	N → Y in AAA17455. Ref.1
	Sequence conflict	105	1	K → Q in AAA17455. Ref.1
	Sequence conflict	142	1	E → V in AAA17455. Ref.1
	Sequence conflict	149	1	A → P in AAA17455. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42279 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: BE908F7602A611DC	FASTA	262	28,088
	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

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]. 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]. 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., 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.
RefSeq	NP_523692.1. NM_078968.2.
UniGene	Dm.23664.
3D structure databases
ProteinModelPortal	P42279.
SMR	P42279. Positions 28-260.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-317423.
Protein family/group databases
MEROPS	S01.117.
Proteomic databases
PaxDb	P42279.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088163; FBpp0087259; FBgn0011554.
GeneID	36217.
KEGG	dme:Dmel_CG12386.
UCSC	CG12386-RA. d. melanogaster.
Organism-specific databases
CTD	36217.
FlyBase	FBgn0011554. etaTry.
Phylogenomic databases
eggNOG	COG5640.
GeneTree	ENSGT00560000077440.
InParanoid	P42279.
KO	K01312.
OMA	YWRPISE.
OrthoDB	EOG46DJJN.
PhylomeDB	P42279.
Gene expression databases
Bgee	P42279.
GermOnline	CG12386. 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. False negative. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	36217.
NextBio	797389.

Entry information

Entry name

TRYU_DROME

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project