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P35040 (TRY6_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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-6

EC=3.4.21.4
Gene names
Name:TRYP6
ORF Names:AGAP008290
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length273 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.

Caution

As this protein has Gly-222 in the position that determines the specificity of the enzyme instead of the Asp found in trypsins, it could have a chymotrypsin-like activity.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide 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 – 4624Activation peptide
PRO_0000028253
Chain47 – 273227Trypsin-6
PRO_0000028254

Regions

Domain47 – 272226Peptidase S1

Sites

Active site871Charge relay system By similarity
Active site1321Charge relay system By similarity
Active site2281Charge relay system By similarity
Site2221Required for specificity By similarity

Amino acid modifications

Disulfide bond72 ↔ 88 By similarity
Disulfide bond197 ↔ 213 By similarity
Disulfide bond224 ↔ 248 By similarity

Experimental info

Sequence conflict131H → L in CAA80513. Ref.1
Sequence conflict451K → R in CAA80513. Ref.1
Sequence conflict561S → A in CAA80513. Ref.1
Sequence conflict941E → Q in CAA80513. Ref.1
Sequence conflict1161L → V in CAA80513. Ref.1
Sequence conflict127 – 1282GG → SA in CAA80513. Ref.1
Sequence conflict140 – 1423CEL → SEI in CAA80513. Ref.1
Sequence conflict1481V → L in CAA80513. Ref.1
Sequence conflict1521Q → S in CAA80513. Ref.1
Sequence conflict1611D → E in CAA80513. Ref.1
Sequence conflict1801L → S in CAA80513. Ref.1
Sequence conflict207 – 2082VA → IT in CAA80513. Ref.1
Sequence conflict2491A → E in CAA80513. Ref.1
Sequence conflict2651D → E in CAA80513. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35040 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 4A485528B7D679D1

FASTA27329,295
        10         20         30         40         50         60 
MLSKFTAILL AVHIALFACA LTQAEKRHKL TRPAFHPNAP YLAGKRIVGG FVIDISDAPY 

        70         80         90        100        110        120 
QISLQYNGKH HCGGSILNSK WILTAAHCID LYSEVKPTVR VGSSEHAAGG TVLHLLRIVP 

       130        140        150        160        170        180 
HPGHSSGGNN YDIALLELEC ELTFNDNVQP VQLPEQDDPI DEGTMGIVSG WGMTMSAADL 

       190        200        210        220        230        240 
NAILRATNVP TVNQQECNQA YQSYGGVAEQ MFCAGYKQGG TGTCRNDSGG PFVAEGKLIG 

       250        260        270 
VVSWSHECAL AGYPGVYARV ASVRDWIRET SGV 

« 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: CAA80513.1.
AAAB01008964 Genomic DNA. Translation: EAA12587.2.
PIRS40003.
RefSeqXP_317175.2. XM_317175.2.

3D structure databases

ProteinModelPortalP35040.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP008290-RA; AGAP008290-PA; AGAP008290.
GeneID1277692.
KEGGaga:AgaP_AGAP008290.
VectorBaseAGAP008290. Anopheles gambiae.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidP35040.
OrthoDBEOG75B84T.
PhylomeDBP35040.

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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRY6_ANOGA
AccessionPrimary (citable) accession number: P35040
Secondary accession number(s): Q7Q492
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 16, 2006
Last modified: July 9, 2014
This is version 104 of the entry and version 2 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