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Reviewed, UniProtKB/Swiss-Prot P35039 (TRY5_ANOGA)

Last modified July 28, 2009. Version 75. 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-5
    EC=3.4.21.4
Gene names
Name: TRYP5
ORF Names: AGAP008291
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

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
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 – 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
P35039-1 [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: 7498434] [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: 12364791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

Z22930 Genomic DNA. Translation: CAA80514.1.
AAAB01008964 Genomic DNA. Translation: EAA12584.2.
PIRS40004.
RefSeqXP_317174.2.

3D structure databases

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

Protein family/group databases

MEROPSS01.130.

Genome annotation databases

EnsemblAGAP008291-RA; AGAP008291-PA; AGAP008291; Anopheles gambiae. [Genome view]
GeneID1277691.
KEGGaga:AgaP_AGAP008291.
VectorBaseAGAP008291. Anopheles gambiae.

Phylogenomic databases

HOGENOMP35039.

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. False negative.
[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: July 28, 2009
This is version 75 of the entry and version 2 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