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Q27289 (CTR1_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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:
Chymotrypsin-1

EC=3.4.21.1
Alternative name(s):
AnChym1
Gene names
Name:CHYM1
ORF Names:AGAP006709
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

Subcellular location

Secreted Ref.1.

Tissue specificity

After blood feeding, expression is induced in the midgut epithelium, followed by secretion into the midgut lumen. 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
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Direct protein sequencing
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 – 1717 Potential
Propeptide18 – 3215Activation peptide
PRO_0000027654
Chain33 – 259227Chymotrypsin-1
PRO_0000027655

Regions

Domain33 – 255223Peptidase S1

Sites

Active site741Charge relay system By similarity
Active site1191Charge relay system By similarity
Active site2121Charge relay system By similarity
Site2061Required for specificity By similarity

Amino acid modifications

Disulfide bond59 ↔ 75 By similarity
Disulfide bond182 ↔ 198 By similarity
Disulfide bond208 ↔ 232 By similarity

Experimental info

Sequence conflict9 – 113VSV → ASI in CAA79325. Ref.1
Sequence conflict9 – 113VSV → ASI in CAA83568. Ref.1
Sequence conflict211T → P in CAA79325. Ref.1
Sequence conflict211T → P in CAA83568. Ref.1
Sequence conflict281N → H in CAA79325. Ref.1
Sequence conflict281N → H in CAA83568. Ref.1
Sequence conflict1301R → Q in CAA79325. Ref.1
Sequence conflict1301R → Q in CAA83568. Ref.1
Sequence conflict1581H → R in CAA79325. Ref.1
Sequence conflict1581H → R in CAA83568. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q27289 [UniParc].

Last modified June 26, 2007. Version 3.
Checksum: 3EF7D6F19EAAED23

FASTA25927,722
        10         20         30         40         50         60 
MLRKVFAVVS VLLVVSAAKV TKLVLDDNYV NRVVGGEVAK NGSAPYQVSL QVPGWGHNCG 

        70         80         90        100        110        120 
GSLLNDRWVL TAAHCLVGHA PGDLMVLVGT NSLKEGGELL KVDKLLYHSR YNLPRFHNDI 

       130        140        150        160        170        180 
GLVRLEQPVR FSELVQSVEY SEKAVPANAT VRLTGWGHTS ANGPSPTLLQ SLNVVTLSNE 

       190        200        210        220        230        240 
DCNKKGGDPG YTDVGHLCTL TKTGEGACNG DSGGPLVYEG KLVGVVNFGV PCALGYPDGF 

       250 
ARVSYYHDWV RTTMANNSK 

« Hide

References

« Hide 'large scale' references
[1]"Blood digestion in the malaria mosquito Anopheles gambiae: molecular cloning and biochemical characterization of two inducible chymotrypsins."
Vizioli J., Catteruccia F., della Torre A., Reckmann I., Mueller H.M.
Eur. J. Biochem. 268:4027-4035(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 33-42, 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
Z18887 mRNA. Translation: CAA79325.1.
Z32645 Genomic DNA. Translation: CAA83568.1.
AAAB01008807 Genomic DNA. Translation: EAA45497.2.
PIRS49129.

3D structure databases

ProteinModelPortalQ27289.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP006709-RA; AGAP006709-PA; AGAP006709.
KEGGaga:AgaP_AGAP006709.
VectorBaseAGAP006709. Anopheles gambiae.

Organism-specific databases

CTD1270348.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
InParanoidQ27289.
OrthoDBEOG7MKW6Q.
PhylomeDBQ27289.

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

Entry information

Entry nameCTR1_ANOGA
AccessionPrimary (citable) accession number: Q27289
Secondary accession number(s): Q7PF17
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 96 of the entry and version 3 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