P35004 (TRYB_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trypsin beta
EC=3.4.21.4

Gene names

Name:	betaTry
ORF Names:	CG18211

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 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 Non-traceable author statement PubMed 12568721. 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	Probable
	Propeptide	23 – 30	8	Activation peptide		PRO_0000028265
	Chain	31 – 253	223	Trypsin beta		PRO_0000028266
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	53	1	S → R in AAA28980. Ref.1
	Sequence conflict	53	1	S → R in AAA17451. Ref.2
	Sequence conflict	85	1	A → G in AAA28980. Ref.1
	Sequence conflict	85	1	A → G in AAA17451. Ref.2
	Sequence conflict	114 – 115	2	VN → TS in AAA28980. Ref.1
	Sequence conflict	114 – 115	2	VN → TS in AAA17451. Ref.2
	Sequence conflict	121	1	H → N in AAA28980. Ref.1
	Sequence conflict	121	1	H → N in AAA17451. Ref.2
	Sequence conflict	142	1	P → T in AAA28980. Ref.1
	Sequence conflict	142	1	P → T in AAA17451. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P35004 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 3F5D35D235B8D8CD	FASTA	253	25,693
	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

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]	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. , 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. , 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.
RefSeq	NP_524904.1. NM_080165.2.
UniGene	Dm.11279.
3D structure databases
ProteinModelPortal	P35004.
SMR	P35004. Positions 31-249.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0087223.
Protein family/group databases
MEROPS	S01.A83.
Proteomic databases
PaxDb	P35004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088122; FBpp0087223; FBgn0010357.
GeneID	47901.
KEGG	dme:Dmel_CG18211.
UCSC	CG18211-RA. d. melanogaster.
Organism-specific databases
CTD	47901.
FlyBase	FBgn0010357. betaTry.
Phylogenomic databases
eggNOG	NOG245986.
GeneTree	ENSGT00620000088101.
InParanoid	P35004.
KO	K01312.
OMA	MICAFAS.
PhylomeDB	P35004.
Gene expression databases
Bgee	P35004.
GermOnline	CG18211. 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
GenomeRNAi	47901.
NextBio	839220.

Entry information

Entry name

TRYB_DROME

Accession

Primary (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:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project