Reviewed, UniProtKB/Swiss-Prot P35036 (TRY2_ANOGA)

Names and origin

Protein names

Recommended name:
    Trypsin-2
    EC=3.4.21.4
Alternative name(s):
    Antryp2

Gene names

Name:	TRYP2
ORF Names:	AGAP008295

Organism

Anopheles gambiae (African malaria mosquito) [Complete proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	277 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)

Function	Major function may be to aid in digestion of the blood meal. Ref.1
Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Subcellular location	Secreted. Ref.1
Tissue specificity	Midgut. Ref.1
Induction	By blood meal. Ref.1
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Digestion
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 50	31	Activation peptide		PRO_0000028245
	Chain	51 – 277	227	Trypsin-2		PRO_0000028246
Regions
	Domain	51 – 276	226	Peptidase S1
Sites
	Active site	91	1	Charge relay system By similarity
	Active site	136	1	Charge relay system By similarity
	Active site	232	1	Charge relay system By similarity
	Site	226	1	Required for specificity By similarity
Amino acid modifications
	Disulfide bond	76 ↔ 92		By similarity
	Disulfide bond	201 ↔ 217		By similarity
	Disulfide bond	228 ↔ 252		By similarity
Experimental info
	Sequence conflict	13	1	V → L in CAA79328. Ref.1
	Sequence conflict	13	1	V → L in CAA80518. Ref.2
	Sequence conflict	26	1	R → G in CAA79328. Ref.1
	Sequence conflict	26	1	R → G in CAA80518. Ref.2
	Sequence conflict	135	1	Y → F in CAA79328. Ref.1
	Sequence conflict	135	1	Y → F in CAA80518. Ref.2
	Sequence conflict	151	1	A → L in CAA79328. Ref.1
	Sequence conflict	151	1	A → L in CAA80518. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P35036-1 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 7C1EAF6FA549B2E7	FASTA	277	29,822
	10 20 30 40 50 60 MSNKIAILLL AVVVAVVACA QAQPSRRHHL VHPLLPRFLP RLHRDSNGHR VVGGFQIDVS 70 80 90 100 110 120 DAPYQVSLQY FNSHRCGGSV LDNKWVLTAA HCTQGLDPSS LAVRLGSSEH ATGGTLVGVL 130 140 150 160 170 180 RTVEHPQYDG NTIDYDFSLM ELETELTFSD AVQPVELPEH EEPVEPGTMA TVSGWGNTQS 190 200 210 220 230 240 AVESSDFLRA ANVPTVSHED CSDAYMWFGE ITDRMLCAGY QQGGKDACQG DSGGPLVADG 250 260 270 KLVGVVSWGY GCAQPGYPGV YGRVASVRDW VRENSGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Members of a trypsin gene family in Anopheles gambiae are induced in the gut by blood meal." Mueller H.-M., Crampton J.M., della Torre A., Sinden R., Crisanti A. EMBO J. 12:2891-2900(1993) [PubMed: 8335004] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION. Strain: Suakoko. Tissue: Midgut.
[2]	"Constitutive and blood meal-induced trypsin genes in Anopheles gambiae." Mueller H.-M., Catteruccia F., Vizioli J., della Torre A., Crisanti A. Exp. Parasitol. 81:371-385(1995) [PubMed: 7498434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Suakoko. Tissue: Midgut.
[3]	"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z18890 mRNA. Translation: CAA79328.1. Z22930 Genomic DNA. Translation: CAA80518.1. AAAB01008964 Genomic DNA. Translation: EAL39600.1.
PIR	S35340.
RefSeq	XP_555167.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBase	Search...
Protein family/group databases
MEROPS	S01.130.
Genome annotation databases
Ensembl	AGAP008295. Anopheles gambiae. [Contig view]
GeneID	3291694.
KEGG	aga:AgaP_AGAP008295.
VectorBase	AGAP008295. Anopheles gambiae.
Phylogenomic databases
HOGENOM	P35036.
OMA	P35036. VELPEHE.
Enzyme and pathway databases
BRENDA	3.4.21.4. 165157.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRY2_ANOGA

Accession

Primary (citable) accession number: P35036
Secondary accession number(s): Q5TQD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)