[1]	PROTEIN SEQUENCE. Jany K.-D., Haug H.; "Amino acid sequence of the chymotryptic protease II from the larvae of the nornet, Vespa crabro."; FEBS Lett. 158:98-102(1983).

Comments

CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
SUBCELLULAR LOCATION: Secreted, extracellular space.
MISCELLANEOUS: An additional Arg at the carboxyl end was found in some of the molecules.
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

A00955; KYVH2C.

3D structure databases

HSSP

P00734; 1GHW. [HSSP ENTRY / PDB]

ModBase

P00769.

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`	`1 218`	`218`	`Chymotrypsin-2.`	`PRO_0000088676`
`DOMAIN`	`1 218`	`218`	`Peptidase S1.`
`ACT_SITE`	`39 39`		`Charge relay system.`
`ACT_SITE`	`84 84`		`Charge relay system.`
`ACT_SITE`	`175 175`		`Charge relay system.`
`DISULFID`	`25 40`
`DISULFID`	`148 161`
`DISULFID`	`171 195`

Sequence information

Length: 218 AA [This is the length of the unprocessed precursor]

Molecular weight: 23677 Da [This is the MW of the unprocessed precursor]

CRC64: 509AB50DE190EB39 [This is a checksum on the sequence]

        10         20         30         40         50         60 
IVGGTDAPRG KYPYQVSLRA PKHFCGGSIS KRYVLTAAHC LVGKSKHQVT VHAGSVLLNK 

        70         80         90        100        110        120 
EEAVYNAEEL IVNKNYNSIR LINDIGLIRV SKDISYTQLV QPVKLPVSNT IKAGDPVVLT 

       130        140        150        160        170        180 
GWGRIYVNGP IPNNLQQITL SIVNQQTCKF KHWGLTDSQI CTFTKLGEGA CDGDSGGPLV 

       190        200        210 
ANGVQIGIVS YGHPCAVGSP NVFTRVYSFL DWIQKNQL

P00769 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