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Protein

Trypsin-2

Gene

TRYP2

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

Functioni

Major function may be to aid in digestion of the blood meal.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911Charge relay systemBy similarity
Active sitei136 – 1361Charge relay systemBy similarity
Sitei226 – 2261Required for specificityBy similarity
Active sitei232 – 2321Charge 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-2 (EC:3.4.21.4)
Alternative name(s):
Antryp2
Gene namesi
Name:TRYP2
ORF Names:AGAP008295
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 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 5031Activation peptidePRO_0000028245Add
BLAST
Chaini51 – 277227Trypsin-2PRO_0000028246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi76 ↔ 92PROSITE-ProRule annotation
Disulfide bondi201 ↔ 217PROSITE-ProRule annotation
Disulfide bondi228 ↔ 252PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

Midgut.1 Publication

Inductioni

By blood meal.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP35036.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 276226Peptidase 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.
InParanoidiP35036.
OMAiTVSHEDC.
OrthoDBiEOG75B84T.
PhylomeDBiP35036.

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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P35036-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNKIAILLL AVVVAVVACA QAQPSRRHHL VHPLLPRFLP RLHRDSNGHR
60 70 80 90 100
VVGGFQIDVS DAPYQVSLQY FNSHRCGGSV LDNKWVLTAA HCTQGLDPSS
110 120 130 140 150
LAVRLGSSEH ATGGTLVGVL RTVEHPQYDG NTIDYDFSLM ELETELTFSD
160 170 180 190 200
AVQPVELPEH EEPVEPGTMA TVSGWGNTQS AVESSDFLRA ANVPTVSHED
210 220 230 240 250
CSDAYMWFGE ITDRMLCAGY QQGGKDACQG DSGGPLVADG KLVGVVSWGY
260 270
GCAQPGYPGV YGRVASVRDW VRENSGV
Length:277
Mass (Da):29,822
Last modified:May 16, 2006 - v2
Checksum:i7C1EAF6FA549B2E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131V → L in CAA79328. (PubMed:8335004)Curated
Sequence conflicti13 – 131V → L in CAA80518. (PubMed:7498434)Curated
Sequence conflicti26 – 261R → G in CAA79328. (PubMed:8335004)Curated
Sequence conflicti26 – 261R → G in CAA80518. (PubMed:7498434)Curated
Sequence conflicti135 – 1351Y → F in CAA79328. (PubMed:8335004)Curated
Sequence conflicti135 – 1351Y → F in CAA80518. (PubMed:7498434)Curated
Sequence conflicti151 – 1511A → L in CAA79328. (PubMed:8335004)Curated
Sequence conflicti151 – 1511A → L in CAA80518. (PubMed:7498434)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18890 mRNA. Translation: CAA79328.1.
Z22930 Genomic DNA. Translation: CAA80518.1.
AAAB01008964 Genomic DNA. Translation: EAL39600.1.
PIRiS35340.
RefSeqiXP_555167.1. XM_555167.2.

Genome annotation databases

EnsemblMetazoaiAGAP008295-RA; AGAP008295-PA; AGAP008295.
GeneIDi3291694.
KEGGiaga:AgaP_AGAP008295.
VectorBaseiAGAP008295. Anopheles gambiae.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18890 mRNA. Translation: CAA79328.1.
Z22930 Genomic DNA. Translation: CAA80518.1.
AAAB01008964 Genomic DNA. Translation: EAL39600.1.
PIRiS35340.
RefSeqiXP_555167.1. XM_555167.2.

3D structure databases

ProteinModelPortaliP35036.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP008295-RA; AGAP008295-PA; AGAP008295.
GeneIDi3291694.
KEGGiaga:AgaP_AGAP008295.
VectorBaseiAGAP008295. Anopheles gambiae.

Organism-specific databases

CTDi3291694.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
InParanoidiP35036.
OMAiTVSHEDC.
OrthoDBiEOG75B84T.
PhylomeDBiP35036.

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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Members of a trypsin gene family in Anopheles gambiae are induced in the gut by blood meal."
    Mueller H.-M., Crampton J.M., della Torre A., Sinden R., Crisanti A.
    EMBO J. 12:2891-2900(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Strain: Suakoko.
    Tissue: Midgut.
  2. "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].
    Strain: Suakoko.
    Tissue: Midgut.
  3. "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 nameiTRY2_ANOGA
AccessioniPrimary (citable) accession number: P35036
Secondary accession number(s): Q5TQD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 16, 2006
Last modified: January 7, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.