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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)DescriptionActionsGraphical viewLength
Active sitei74Charge relay systemBy similarity1
Active sitei119Charge relay systemBy similarity1
Sitei206Required for specificityBy similarity1
Active sitei212Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000007062 Componentsi: Chromosome 2L, Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002765418 – 32Activation peptide1 PublicationAdd BLAST15
ChainiPRO_000002765533 – 259Chymotrypsin-1Add BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi59 ↔ 75PROSITE-ProRule annotation
Disulfide bondi182 ↔ 198PROSITE-ProRule annotation
Disulfide bondi208 ↔ 232PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ27289.
PRIDEiQ27289.

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)DescriptionActionsGraphical viewLength
Domaini33 – 255Peptidase S1PROSITE-ProRule annotationAdd BLAST223

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
InParanoidiQ27289.
OMAiWGHTSAN.
OrthoDBiEOG091G0DF7.
PhylomeDBiQ27289.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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 26, 2007 - v3
Checksum:i3EF7D6F19EAAED23
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 11VSV → ASI in CAA79325 (PubMed:11453997).Curated3
Sequence conflicti9 – 11VSV → ASI in CAA83568 (PubMed:11453997).Curated3
Sequence conflicti21T → P in CAA79325 (PubMed:11453997).Curated1
Sequence conflicti21T → P in CAA83568 (PubMed:11453997).Curated1
Sequence conflicti28N → H in CAA79325 (PubMed:11453997).Curated1
Sequence conflicti28N → H in CAA83568 (PubMed:11453997).Curated1
Sequence conflicti130R → Q in CAA79325 (PubMed:11453997).Curated1
Sequence conflicti130R → Q in CAA83568 (PubMed:11453997).Curated1
Sequence conflicti158H → R in CAA79325 (PubMed:11453997).Curated1
Sequence conflicti158H → R in CAA83568 (PubMed:11453997).Curated1

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-RA; AGAP006709-PA; AGAP006709.

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.

Proteomic databases

PaxDbiQ27289.
PRIDEiQ27289.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1270348.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
InParanoidiQ27289.
OMAiWGHTSAN.
OrthoDBiEOG091G0DF7.
PhylomeDBiQ27289.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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...

Entry informationi

Entry nameiCTR1_ANOGA
AccessioniPrimary (citable) accession number: Q27289
Secondary accession number(s): Q7PF17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 26, 2007
Last modified: November 30, 2016
This is version 108 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

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 one 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.