NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Larval gut;
DOI=10.1016/S0965-1748(99)00104-6; PubMed=10612046 [NCBI, ExPASy, EBI, Israel, Japan]
Girard C., Jouanin L.;
"Molecular cloning of cDNAs encoding a range of digestive enzymes from a phytophagous beetle, Phaedon cochleariae.";
Insect Biochem. Mol. Biol. 29:1129-1142(1999).

Comments

FUNCTION: Serine protease with chymotryptic and collagenolytic activities (By similarity).
CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
SUBCELLULAR LOCATION: Secreted, extracellular space (By similarity).
TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult gut.
DEVELOPMENTAL STAGE: Ovarial and mature eggs, larvae and adult.
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

EMBL

Y17904; CAA76928.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P23946; 1NN6. [HSSP ENTRY / PDB]

ModBase

O97398.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0030574;	Biological process: collagen catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0007586;	Biological process: digestion (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
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

ProtoNet

O97398.

UniRef

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

Keywords

Collagen degradation; Digestion; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`PROPEP`	`17 45`	`29`	`Activation peptide (By similarity).`	`PRO_0000314680`
`CHAIN`	`46 276`	`231`	`Chymotrypsin.`	`PRO_5000147324`
`DOMAIN`	`46 272`	`227`	`Peptidase S1.`
`ACT_SITE`	`89 89`		`Charge relay system (By similarity).`
`ACT_SITE`	`135 135`		`Charge relay system (By similarity).`
`ACT_SITE`	`229 229`		`Charge relay system (By similarity).`
`CARBOHYD`	`144 144`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`193 193`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`74 90`		`By similarity.`
`DISULFID`	`202 215`		`By similarity.`
`DISULFID`	`225 250`		`By similarity.`

Sequence information

Length: 276 AA [This is the length of the unprocessed precursor]

Molecular weight: 29868 Da [This is the MW of the unprocessed precursor]

CRC64: FC5FD05DB882A1DE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVALVVLAL FGVSLAASID NIEIPPSKNI YVEPINQPEV DPSLEIVNGQ EVVPHSIPYQ 

        70         80         90        100        110        120 
IFLVASAGET SWTCGGSLIT KRYVLTAAHC IQGAKSVHVT LGAHNLAKHE ASKVTVNGRS 

       130        140        150        160        170        180 
WVIHEKYDST NIDNDIGVIQ LERNLTLTRS IQLARLPSLR DVGINLEGRT ATVSGWGLTN 

       190        200        210        220        230        240 
GIFQTTTDVL RANNTIISNK ECNDVFKIVQ PTEVCLSIAG GRSACSGDSG GPLVIDNVQH 

       250        260        270 
GIVSYGSSYC RSTPSVFTRV SSYLNWLQTH SEWRAQ

O97398 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