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Protein

Trypsin-6

Gene

TRYP6

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Charge relay systemBy similarity
Active sitei132 – 1321Charge relay systemBy similarity
Sitei222 – 2221Required for specificityBy similarity
Active sitei228 – 2281Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. digestion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Protein family/group databases

MEROPSiS01.130.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin-6 (EC:3.4.21.4)
Gene namesi
Name:TRYP6
ORF Names:AGAP008290
OrganismiAnopheles gambiae (African malaria mosquito)
Taxonomic identifieri7165 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
ProteomesiUP000007062: Chromosome 3R

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 4624Activation peptidePRO_0000028253Add
BLAST
Chaini47 – 273227Trypsin-6PRO_0000028254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 88PROSITE-ProRule annotation
Disulfide bondi197 ↔ 213PROSITE-ProRule annotation
Disulfide bondi224 ↔ 248PROSITE-ProRule annotation

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Expressioni

Tissue specificityi

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

Structurei

3D structure databases

ProteinModelPortaliP35040.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 272226Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
InParanoidiP35040.
OrthoDBiEOG75B84T.
PhylomeDBiP35040.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKFTAILL AVHIALFACA LTQAEKRHKL TRPAFHPNAP YLAGKRIVGG
60 70 80 90 100
FVIDISDAPY QISLQYNGKH HCGGSILNSK WILTAAHCID LYSEVKPTVR
110 120 130 140 150
VGSSEHAAGG TVLHLLRIVP HPGHSSGGNN YDIALLELEC ELTFNDNVQP
160 170 180 190 200
VQLPEQDDPI DEGTMGIVSG WGMTMSAADL NAILRATNVP TVNQQECNQA
210 220 230 240 250
YQSYGGVAEQ MFCAGYKQGG TGTCRNDSGG PFVAEGKLIG VVSWSHECAL
260 270
AGYPGVYARV ASVRDWIRET SGV
Length:273
Mass (Da):29,295
Last modified:May 16, 2006 - v2
Checksum:i4A485528B7D679D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131H → L in CAA80513 (PubMed:7498434).Curated
Sequence conflicti45 – 451K → R in CAA80513 (PubMed:7498434).Curated
Sequence conflicti56 – 561S → A in CAA80513 (PubMed:7498434).Curated
Sequence conflicti94 – 941E → Q in CAA80513 (PubMed:7498434).Curated
Sequence conflicti116 – 1161L → V in CAA80513 (PubMed:7498434).Curated
Sequence conflicti127 – 1282GG → SA in CAA80513 (PubMed:7498434).Curated
Sequence conflicti140 – 1423CEL → SEI in CAA80513 (PubMed:7498434).Curated
Sequence conflicti148 – 1481V → L in CAA80513 (PubMed:7498434).Curated
Sequence conflicti152 – 1521Q → S in CAA80513 (PubMed:7498434).Curated
Sequence conflicti161 – 1611D → E in CAA80513 (PubMed:7498434).Curated
Sequence conflicti180 – 1801L → S in CAA80513 (PubMed:7498434).Curated
Sequence conflicti207 – 2082VA → IT in CAA80513 (PubMed:7498434).Curated
Sequence conflicti249 – 2491A → E in CAA80513 (PubMed:7498434).Curated
Sequence conflicti265 – 2651D → E in CAA80513 (PubMed:7498434).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22930 Genomic DNA. Translation: CAA80513.1.
AAAB01008964 Genomic DNA. Translation: EAA12587.2.
PIRiS40003.
RefSeqiXP_317175.2. XM_317175.2.

Genome annotation databases

EnsemblMetazoaiAGAP008290-RA; AGAP008290-PA; AGAP008290.
GeneIDi1277692.
KEGGiaga:AgaP_AGAP008290.
VectorBaseiAGAP008290. Anopheles gambiae.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22930 Genomic DNA. Translation: CAA80513.1.
AAAB01008964 Genomic DNA. Translation: EAA12587.2.
PIRiS40003.
RefSeqiXP_317175.2. XM_317175.2.

3D structure databases

ProteinModelPortaliP35040.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP008290-RA; AGAP008290-PA; AGAP008290.
GeneIDi1277692.
KEGGiaga:AgaP_AGAP008290.
VectorBaseiAGAP008290. Anopheles gambiae.

Organism-specific databases

CTDi1277692.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
InParanoidiP35040.
OrthoDBiEOG75B84T.
PhylomeDBiP35040.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTRY6_ANOGA
AccessioniPrimary (citable) accession number: P35040
Secondary accession number(s): Q7Q492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 16, 2006
Last modified: January 7, 2015
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.