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P35039 (TRY5_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. 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-5

EC=3.4.21.4
Gene names
Name:TRYP5
ORF Names:AGAP008291
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

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

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.

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

proteolysis

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 – 2121 Potential
Propeptide22 – 4726Activation peptide
PRO_0000028251
Chain48 – 274227Trypsin-5
PRO_0000028252

Regions

Domain48 – 273226Peptidase S1

Sites

Active site881Charge relay system By similarity
Active site1321Charge relay system By similarity
Active site2291Charge relay system By similarity
Site2231Required for specificity By similarity

Amino acid modifications

Disulfide bond73 ↔ 89 By similarity
Disulfide bond197 ↔ 214 By similarity
Disulfide bond225 ↔ 249 By similarity

Experimental info

Sequence conflict131F → I in CAA80514. Ref.1
Sequence conflict181Y → C in CAA80514. Ref.1
Sequence conflict551N → D in CAA80514. Ref.1
Sequence conflict1061K → E in CAA80514. Ref.1
Sequence conflict1141I → V in CAA80514. Ref.1
Sequence conflict1801S → T in CAA80514. Ref.1
Sequence conflict2111Q → E in CAA80514. Ref.1
Sequence conflict2361K → E in CAA80514. Ref.1
Sequence conflict2591A → P in CAA80514. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35039 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 468AB656797AED8E

FASTA27429,815
        10         20         30         40         50         60 
MSIKFTTLLA VLFALLAYAR AQAERRHKLT RPVHRFAPNR PYLAGKRIVG GFVINISDAP 

        70         80         90        100        110        120 
YQISLQYDDD HNCGGSILSS KWILTAAHCI NDNAPSKPTV RVGSSKHASG GTVIRVARIV 

       130        140        150        160        170        180 
PHPMHGSKNN YDIALLELKN ELTFSEKVQP IALPEQDEPI EEGTMGIVSG WGLTLSEADS 

       190        200        210        220        230        240 
NDVLRATNVP TVNQQECNKA YQSRYGGITD QMFCAGYKQG GQDTCRQDSG GPFVAKGKLI 

       250        260        270 
GVISWGHECA LAGYPGVYAR VASVRDWIRT TSGV 

« 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: CAA80514.1.
AAAB01008964 Genomic DNA. Translation: EAA12584.2.
PIRS40004.

3D structure databases

ProteinModelPortalP35039.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP008291-RA; AGAP008291-PA; AGAP008291.
KEGGaga:AgaP_AGAP008291.
VectorBaseAGAP008291. Anopheles gambiae.

Organism-specific databases

CTD1277691.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidP35039.
OMACINDNAP.
OrthoDBEOG75B84T.
PhylomeDBP35039.

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 nameTRY5_ANOGA
AccessionPrimary (citable) accession number: P35039
Secondary accession number(s): Q7Q493
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 103 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