[1]	PROTEIN SEQUENCE, AND DISULFIDE BONDS. DOI=10.1016/0006-291X(83)91251-2; PubMed=6340663 [NCBI, ExPASy, EBI, Israel, Japan] Jany K.-D., Bekelar K., Pfleiderer G., Ishay J.; "Amino acid sequence of an insect chymotrypsin from the larvae of the hornet, Vespa orientalis."; Biochem. Biophys. Res. Commun. 110:1-7(1983).
[2]	ACTIVE SITE. DOI=10.1016/0005-2795(81)90164-1; PubMed=6786354 [NCBI, ExPASy, EBI, Israel, Japan] Jany K.-D., Bekelar K., Ishay J.; "The amino acid sequences around the reactive serine and histidine residues of the chymotrypsin-like protease from the hornet, Vespa orientalis."; Biochim. Biophys. Acta 668:197-200(1981).

Comments

CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
SUBCELLULAR LOCATION: Secreted, extracellular space.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A00954; KYVH2O.

3D structure databases

HSSP

P00760; 1EZX. [HSSP ENTRY / PDB]

ModBase

P00768.

Protein family/group databases

MEROPS

S01.438; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 216`	`216`	`Chymotrypsin-2.`	`PRO_0000088677`
`DOMAIN`	`1 216`	`216`	`Peptidase S1.`
`ACT_SITE`	`39 39`		`Charge relay system.`
`ACT_SITE`	`82 82`		`Charge relay system.`
`ACT_SITE`	`173 173`		`Charge relay system.`
`DISULFID`	`25 40`
`DISULFID`	`146 159`
`DISULFID`	`169 193`

Sequence information

Length: 216 AA [This is the length of the unprocessed precursor]

Molecular weight: 23471 Da [This is the MW of the unprocessed precursor]

CRC64: F235BF992AEFEDE1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
IVGGTNAPRG KYPYQVSLRA PKHFCGGSIS KRYVLTAAHC LVGKSEHQVT VGSVLLNKEE 

        70         80         90        100        110        120 
AVYNAKELIV NKNYNSIRLI NDIGLIRVSK DISFTQLVQP VKLPVSNTIK AGDPVVLTGW 

       130        140        150        160        170        180 
GRIYVNGPIP NNLQQITLSI VNQQTCKSKH WGLTDSQICT FTKRGEGACH GDSGGPLVAN 

       190        200        210 
GVQIGIVSYG HPCAIGSPNV FTRVYSFLDW IQKNQL

P00768 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools