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Reviewed, UniProtKB/Swiss-Prot P35035 (TRY1_ANOGA)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trypsin-1
    EC=3.4.21.4
Alternative name(s):
    Antryp1
Gene names
Name: TRYP1
ORF Names: AGAP008296
OrganismAnopheles gambiae (African malaria mosquito) [Complete proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Major function may be to aid in digestion of the blood meal. Ref.1 Ref.2

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Subcellular location

Secreted. Ref.1 Ref.2

Tissue specificity

Constitutively expressed at low level in the gut of adult females. Also expressed in the gut of male and female pupae. Ref.1 Ref.2

Induction

By blood meal. Ref.1

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 4729Activation peptide
PRO_0000028243
Chain48 – 274227Trypsin-1
PRO_0000028244

Regions

Domain48 – 273226Peptidase S1

Sites

Active site881Charge relay system By similarity
Active site1331Charge relay system By similarity
Active site2291Charge relay system By similarity
Site2231Required for specificity By similarity

Amino acid modifications

Disulfide bond73 ↔ 89 By similarity
Disulfide bond198 ↔ 214 By similarity
Disulfide bond225 ↔ 249 By similarity

Experimental info

Sequence conflict931A → R in CAA79327. Ref.1
Sequence conflict951P → T in CAA79327. Ref.1
Sequence conflict951P → T in CAA80512. Ref.2
Sequence conflict1011R → P in CAA79327. Ref.1
Sequence conflict1481S → A in CAA80512. Ref.2
Sequence conflict2041E → D in CAA79327. Ref.1
Sequence conflict2041E → D in CAA80512. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35035-1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 7055CA51C6CEF3F8

FASTA27429,057
        10         20         30         40         50         60 
MSNKIAILLA VLVAVVACAE AQANQRHRLV RPSPSFSPRP RYAVGQRIVG GFEIDVSDAP 

        70         80         90        100        110        120 
YQVSLQYNKR HNCGGSVLSS KWVLTAAHCT AGASPSSLTV RLGTSRHASG GTVVRVARVV 

       130        140        150        160        170        180 
QHPKYDSSSI DFDYSLLELE DELTFSDSVQ PVGLPKQDET VKDGTMTTVS GWGNTQSAAE 

       190        200        210        220        230        240 
SNAVLRAANV PTVNQKECNK AYSEFGGVTD RMLCAGYQQG GKDACQGDSG GPLVADGKLV 

       250        260        270 
GVVSWGYGCA QAGYPGVYSR VAVVRDWVRE NSGV 

« Hide

References

« Hide '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], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
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. expand/collapse author list , 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

Z18889 mRNA. Translation: CAA79327.1.
Z22930 Genomic DNA. Translation: CAA80512.1.
AAAB01008964 Genomic DNA. Translation: EAA12590.3.
PIRS35339.
RefSeqXP_317170.2.

3D structure databases

HSSPHSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBaseSearch...

Protein family/group databases

MEROPSS01.130.

Genome annotation databases

EnsemblAGAP008296. Anopheles gambiae. [Contig view]
GeneID1277688.
KEGGaga:AgaP_AGAP008296.
VectorBaseAGAP008296. Anopheles gambiae.

Phylogenomic databases

HOGENOMP35035.
OMAP35035. YDSSSID.

Enzyme and pathway databases

BRENDA3.4.21.4. 165157.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRY1_ANOGA
AccessionPrimary (citable) accession number: P35035
Secondary accession number(s): Q7PN85
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 26, 2008
Last modified: June 16, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents