Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P35037 (TRY3_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trypsin-3

EC=3.4.21.4
Gene names
Name:TRYP3
ORF Names:AGAP008294
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Constitutive trypsin that is expressed 2 days after emergence, coinciding with host seeking behavior of the female. Ref.1

Catalytic activity

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

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed in the midgut. Expression levels drop a few hours after blood feeding and pick up again 28 hours later. Ref.1

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Sequence caution

The sequence EAA12261.3 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 2222 Potential
Propeptide23 – 4826Activation peptide
PRO_0000028247
Chain49 – 275227Trypsin-3
PRO_0000028248

Regions

Domain49 – 274226Peptidase S1

Sites

Active site891Charge relay system By similarity
Active site1341Charge relay system By similarity
Active site2301Charge relay system By similarity
Site2241Required for specificity By similarity

Amino acid modifications

Disulfide bond74 ↔ 90 By similarity
Disulfide bond199 ↔ 215 By similarity
Disulfide bond226 ↔ 250 By similarity

Experimental info

Sequence conflict421K → Q in CAA80517. Ref.1
Sequence conflict1421S → T in CAA80517. Ref.1
Sequence conflict1571D → E in CAA80517. Ref.1
Sequence conflict1691I → T in CAA80517. Ref.1
Sequence conflict1911V → I in CAA80517. Ref.1
Sequence conflict2671D → N in CAA80517. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35037 [UniParc].

Last modified July 1, 2008. Version 5.
Checksum: 93D27A26AF4C5458

FASTA27529,374
        10         20         30         40         50         60 
MISNKIAILL AVLVVAVACA QARVALKHRS VQALPRFLPR PKYDVGHRIV GGFEIDVSET 

        70         80         90        100        110        120 
PYQVSLQYFN SHRCGGSVLN SKWILTAAHC TVNLQPSSLA VRLGSSRHAS GGTVVRVARV 

       130        140        150        160        170        180 
LEHPNYDDST IDYDFSLMEL ESELTFSDVV QPVSLPDQDE AVEDGTMTIV SGWGNTQSAA 

       190        200        210        220        230        240 
ESNAILRAAN VPTVNQKECT IAYSSSGGIT DRMLCAGYKR GGKDACQGDS GGPLVVDGKL 

       250        260        270 
VGVVSWGFGC AMPGYPGVYA RVAVVRDWVR ENSGA 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: Suakoko.
Tissue: Midgut.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22930 Genomic DNA. Translation: CAA80517.1.
AAAB01008964 Genomic DNA. Translation: EAA12261.3. Sequence problems.
PIRS40007.
RefSeqXP_317171.2. XM_317171.3.

3D structure databases

ProteinModelPortalP35037.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3291693.
KEGGaga:AgaP_AGAP008294.
VectorBaseAGAP008294. Anopheles gambiae.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidP35037.
OrthoDBEOG75B84T.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRY3_ANOGA
AccessionPrimary (citable) accession number: P35037
Secondary accession number(s): Q7PNF7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 1, 2008
Last modified: July 9, 2014
This is version 100 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries