Q52V24 (Q52V24_PONLE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Hepatopancreas trypsin EMBL AAX98287.1
Organism	Pontastacus leptodactylus (Narrow-fingered crayfish) (Astacus leptodactylus) EMBL AAX98287.1
Taxonomic identifier	6717 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Astacoidea › Astacidae › Pontastacus

Protein attributes

Sequence length	237 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the peptidase S1 family. RuleBase RU000360

Ontologies

Keywords
Molecular function	Hydrolase Protease Serine protease RuleBase RU004260
Technical term	3D-structure PDB 2F91
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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
Experimental info
	Non-terminal residue	1	1	EMBL AAX98287.1

Sequences

	Sequence		Length	Mass (Da)
	Q52V24 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: E9C74D1EA3847025	FASTA	237	25,033
	10 20 30 40 50 60 IVGGTDATLG EFPYQLSFQE TFIGFSFHFC GASIYNENYA ITAGHCAYGD DYENPSGLQI 70 80 90 100 110 120 VAGELDMSVN EGSEQIITVS KIILHENFDY NLLDNDISLL KLSGSLTFND NVAPIALPEQ 130 140 150 160 170 180 GHTATGDVIV TGWGTTSEGG NTPDVLQKVT VPLVSDEDCR ADYGADEILD SMICAGVPEG 190 200 210 220 230 GKDSCQGDSG GPLAASDTGS TYLAGIVSWG YGCARPGYPG VYTEVSYHVD WIKANAV

References

[1]	"Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition." Fodor K., Harmat V., Hetenyi C., Kardos J., Antal J., Perczel A., Patthy A., Katona G., Graf L. J. Mol. Biol. 350:156-169(2005) [PubMed: 15922357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis." Fodor K., Harmat V., Neutze R., Szilagyi L., Graf L., Katona G. Biochemistry 45:2114-2121(2006) [PubMed: 16475800] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY906961 mRNA. Translation: AAX98287.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F91	X-ray	1.20	A	1-237	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.035.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR009003. Pept_cys/ser_Trypsin-like.
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]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q52V24_PONLE

Accession

Primary (citable) accession number: Q52V24

Entry history

Integrated into UniProtKB/TrEMBL:	May 24, 2005
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)