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Protein

Chymotrypsin-1

Gene

CHYM1

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741Charge relay systemBy similarity
Active sitei119 – 1191Charge relay systemBy similarity
Sitei206 – 2061Required for specificityBy similarity
Active sitei212 – 2121Charge 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

MEROPSiS01.166.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-1 (EC:3.4.21.1)
Alternative name(s):
AnChym1
Gene namesi
Name:CHYM1
ORF Names:AGAP006709
OrganismiAnopheles gambiae (African malaria mosquito)
Taxonomic identifieri7165 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
ProteomesiUP000007062 Componenti: Chromosome 2L

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 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 3215Activation peptide1 PublicationPRO_0000027654Add
BLAST
Chaini33 – 259227Chymotrypsin-1PRO_0000027655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 75PROSITE-ProRule annotation
Disulfide bondi182 ↔ 198PROSITE-ProRule annotation
Disulfide bondi208 ↔ 232PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

After blood feeding, expression is induced in the midgut epithelium, followed by secretion into the midgut lumen.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ27289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 255223Peptidase 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.
InParanoidiQ27289.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ27289.

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.

Q27289-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRKVFAVVS VLLVVSAAKV TKLVLDDNYV NRVVGGEVAK NGSAPYQVSL
60 70 80 90 100
QVPGWGHNCG GSLLNDRWVL TAAHCLVGHA PGDLMVLVGT NSLKEGGELL
110 120 130 140 150
KVDKLLYHSR YNLPRFHNDI GLVRLEQPVR FSELVQSVEY SEKAVPANAT
160 170 180 190 200
VRLTGWGHTS ANGPSPTLLQ SLNVVTLSNE DCNKKGGDPG YTDVGHLCTL
210 220 230 240 250
TKTGEGACNG DSGGPLVYEG KLVGVVNFGV PCALGYPDGF ARVSYYHDWV

RTTMANNSK
Length:259
Mass (Da):27,722
Last modified:June 25, 2007 - v3
Checksum:i3EF7D6F19EAAED23
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 113VSV → ASI in CAA79325 (PubMed:11453997).Curated
Sequence conflicti9 – 113VSV → ASI in CAA83568 (PubMed:11453997).Curated
Sequence conflicti21 – 211T → P in CAA79325 (PubMed:11453997).Curated
Sequence conflicti21 – 211T → P in CAA83568 (PubMed:11453997).Curated
Sequence conflicti28 – 281N → H in CAA79325 (PubMed:11453997).Curated
Sequence conflicti28 – 281N → H in CAA83568 (PubMed:11453997).Curated
Sequence conflicti130 – 1301R → Q in CAA79325 (PubMed:11453997).Curated
Sequence conflicti130 – 1301R → Q in CAA83568 (PubMed:11453997).Curated
Sequence conflicti158 – 1581H → R in CAA79325 (PubMed:11453997).Curated
Sequence conflicti158 – 1581H → R in CAA83568 (PubMed:11453997).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18887 mRNA. Translation: CAA79325.1.
Z32645 Genomic DNA. Translation: CAA83568.1.
AAAB01008807 Genomic DNA. Translation: EAA45497.2.
PIRiS49129.
RefSeqiXP_309033.2. XM_309033.4.

Genome annotation databases

EnsemblMetazoaiAGAP006709-RA; AGAP006709-PA; AGAP006709.
GeneIDi1270348.
KEGGiaga:AgaP_AGAP006709.
VectorBaseiAGAP006709. Anopheles gambiae.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18887 mRNA. Translation: CAA79325.1.
Z32645 Genomic DNA. Translation: CAA83568.1.
AAAB01008807 Genomic DNA. Translation: EAA45497.2.
PIRiS49129.
RefSeqiXP_309033.2. XM_309033.4.

3D structure databases

ProteinModelPortaliQ27289.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP006709-RA; AGAP006709-PA; AGAP006709.
GeneIDi1270348.
KEGGiaga:AgaP_AGAP006709.
VectorBaseiAGAP006709. Anopheles gambiae.

Organism-specific databases

CTDi1270348.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
InParanoidiQ27289.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ27289.

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. "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(2000) [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.
    , 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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PEST.

Entry informationi

Entry nameiCTR1_ANOGA
AccessioniPrimary (citable) accession number: Q27289
Secondary accession number(s): Q7PF17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: June 25, 2007
Last modified: January 6, 2015
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.