[1]	PROTEIN SEQUENCE, DISULFIDE BONDS, AND ACTIVE SITE. PubMed=5649671 [NCBI, ExPASy, EBI, Israel, Japan] Smillie L.B., Furka A., Nagabhushan N., Stevenson K.J., Parkes C.O.; "Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen."; Nature 218:343-346(1968).

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].
WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/CHY/";.

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

A00953; KYBOB.

UniGene

Bt.62239

3D structure databases

PDB

1AFQ; X-ray; 1.80 A; A=1-13.	[ExPASy / RCSB / EBI]
1CBW; X-ray; 2.60 A; A/F=1-13.	[ExPASy / RCSB / EBI]
1GMH; X-ray; 2.10 A; E=1-13.	[ExPASy / RCSB / EBI]
1HJA; X-ray; 2.30 A; A=1-13.	[ExPASy / RCSB / EBI]
2GCH; X-ray; 1.90 A; E=1-13.	[ExPASy / RCSB / EBI]
5GCH; X-ray; 2.70 A; E=1-13.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AFQ; -.
1CBW; -.
1GMH; -.
1HJA; -.
2GCH; -.
5GCH; -.

SMR

P00767; 1-245.

ModBase

P00767.

Protein family/group databases

MEROPS

S01.152; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0007586;	Biological process: digestion (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).

Genome annotation databases

Ensembl

ENSBTAG00000008500; Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P00767; -.

Other

LinkHub

P00767; -.

UniRef

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

Keywords

3D-structure; Digestion; Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 13`	`13`	`Chymotrypsin B chain A.`	`PRO_0000027629`
`PROPEP`	`14 15`	`2`		`PRO_0000027630`
`CHAIN`	`16 146`	`131`	`Chymotrypsin B chain B.`	`PRO_0000027631`
`PROPEP`	`147 148`	`2`		`PRO_0000027632`
`CHAIN`	`149 245`	`97`	`Chymotrypsin B chain C.`	`PRO_0000027633`
`DOMAIN`	`16 243`	`228`	`Peptidase S1.`
`ACT_SITE`	`57 57`		`Charge relay system.`
`ACT_SITE`	`102 102`		`Charge relay system.`
`ACT_SITE`	`195 195`		`Charge relay system.`
`DISULFID`	`1 122`
`DISULFID`	`42 58`
`DISULFID`	`136 201`
`DISULFID`	`168 182`
`DISULFID`	`191 220`

Sequence information

Length: 245 AA [This is the length of the unprocessed precursor]

Molecular weight: 25755 Da [This is the MW of the unprocessed precursor]

CRC64: 678016446FF5FEB5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
CGVPAIQPVL SGLARIVNGE DAVPGSWPWQ VSLQDSTGFH FCGGSLISED WVVTAAHCGV 

        70         80         90        100        110        120 
TTSDVVVAGE FDQGLETEDT QVLKIGKVFK NPKFSILTVR NDITLLKLAT PAQFSETVSA 

       130        140        150        160        170        180 
VCLPSADEDF PAGMLCATTG WGKTKYNALK TPDKLQQATL PIVSNTDCRK YWGSRVTDVM 

       190        200        210        220        230        240 
ICAGASGVSS CMGDSGGPLV CQKNGAWTLA GIVSWGSSTC STSTPAVYAR VTALMPWVQE 


TLAAN

P00767 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