Q27289 (CTR1_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chymotrypsin-1
EC=3.4.21.1

Alternative name(s):
AnChym1

Gene names

Name:	CHYM1
ORF Names:	AGAP006709

Organism

Anopheles gambiae (African malaria mosquito)

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Digestion
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – 32	15	Activation peptide		PRO_0000027654
	Chain	33 – 259	227	Chymotrypsin-1		PRO_0000027655
Regions
	Domain	33 – 255	223	Peptidase S1
Sites
	Active site	74	1	Charge relay system By similarity
	Active site	119	1	Charge relay system By similarity
	Active site	212	1	Charge relay system By similarity
	Site	206	1	Required for specificity By similarity
Amino acid modifications
	Disulfide bond	59 ↔ 75		By similarity
	Disulfide bond	182 ↔ 198		By similarity
	Disulfide bond	208 ↔ 232		By similarity
Experimental info
	Sequence conflict	9 – 11	3	VSV → ASI in CAA79325. Ref.1
	Sequence conflict	9 – 11	3	VSV → ASI in CAA83568. Ref.1
	Sequence conflict	21	1	T → P in CAA79325. Ref.1
	Sequence conflict	21	1	T → P in CAA83568. Ref.1
	Sequence conflict	28	1	N → H in CAA79325. Ref.1
	Sequence conflict	28	1	N → H in CAA83568. Ref.1
	Sequence conflict	130	1	R → Q in CAA79325. Ref.1
	Sequence conflict	130	1	R → Q in CAA83568. Ref.1
	Sequence conflict	158	1	H → R in CAA79325. Ref.1
	Sequence conflict	158	1	H → R in CAA83568. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q27289 [UniParc]. Last modified June 26, 2007. Version 3. Checksum: 3EF7D6F19EAAED23	FASTA	259	27,722
	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

References

	« Hide 'large scale' referencesShow '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: 11453997] [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(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z18887 mRNA. Translation: CAA79325.1. Z32645 Genomic DNA. Translation: CAA83568.1. AAAB01008807 Genomic DNA. Translation: EAA45497.2.
PIR	S49129.
RefSeq	XP_309033.2. XM_309033.4.
3D structure databases
ProteinModelPortal	Q27289.
ModBase	Search...
Protein family/group databases
MEROPS	S01.166.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	AGAP006709-RA; AGAP006709-PA; AGAP006709.
GeneID	1270348.
KEGG	aga:AgaP_AGAP006709.
VectorBase	AGAP006709. Anopheles gambiae.
Organism-specific databases
CTD	1270348.
Phylogenomic databases
eggNOG	KOG3627.
GeneTree	EMGT00050000002508.
HOGENOM	HBG755338.
InParanoid	Q27289.
OMA	ISNDECK.
OrthoDB	EOG43TXB9.
PhylomeDB	Q27289.
Family and domain databases
InterPro	IPR009003. Pept_cys/ser_Trypsin-like. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CTR1_ANOGA

Accession

Primary (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:	December 14, 2011
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)