Reviewed, UniProtKB/Swiss-Prot P36178 (CTRB2_LITVA)

Names and origin

Protein names	Recommended name:     Chymotrypsin BII     EC=3.4.21.1
Organism	Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei)
Taxonomic identifier	6689 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Dendrobranchiata › Penaeoidea › Penaeidae › Litopenaeus

Protein attributes

Sequence length	271 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)

Function	Serine protease with chymotryptic and collagenolytic activities.
Catalytic activity	Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Subcellular location	Secreted › extracellular space.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space 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 – 15	15	Potential
	Propeptide	16 – 45	30	Activation peptide Ref.2		PRO_0000027652
	Chain	46 – 271	226	Chymotrypsin BII		PRO_0000027653
Regions
	Domain	46 – 268	223	Peptidase S1
Sites
	Active site	86	1	Charge relay system By similarity
	Active site	132	1	Charge relay system By similarity
	Active site	223	1	Charge relay system By similarity
Amino acid modifications
	Disulfide bond	71 ↔ 87		By similarity
	Disulfide bond	196 ↔ 209		By similarity
	Disulfide bond	219 ↔ 245		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P36178-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 2254D7C7E63FA2E1	FASTA	271	28,723
	10 20 30 40 50 60 MIGKLSLLLV CVAVASGNPA AGKPWHWKSP KPLVDPRIHV NATPRIVGGV EATPHSWPHQ 70 80 90 100 110 120 AALFIDDMYF CGGSLISSEW VLTAAHCMDG AGFVEVVLGA HNIRQNEASQ VSITSTDFFT 130 140 150 160 170 180 HENWNSWLLT NDIALIKLPS PVSLNSNIKT VKLPSSDVAV GTTVTPTGWG RPLDSAGGIS 190 200 210 220 230 240 DVLRQVDVPI MTNDDCDAVY GIVGNGVVCI DSEGGKGTCN GDSGGPLNLN GMTYGITSFG 250 260 270 SSAGCEVGYP DAFTRVYYYL DWIEQKTGVT P

References

[1]	"Molecular cloning of a cDNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vanameii (Crustacea, Decapoda)." Sellos D., van Wormhoudt A. FEBS Lett. 309:219-224(1992) [PubMed: 1516690] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Hepatopancreas.
[2]	"Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda)." van Wormhoudt A., le Chevalier P., Sellos D. Comp. Biochem. Physiol. 103B:675-680(1992) [PubMed: 1458841] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-65, CHARACTERIZATION. Tissue: Hepatopancreas.

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1AZZ based on UniProtKB P00771.
SMR	P36178. Positions 46-271.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.4.21.1. 39338.
Family and domain databases
InterPro	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]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CTRB2_LITVA

Accession

Primary (citable) accession number: P36178

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)