Reviewed, UniProtKB/Swiss-Prot Q94715 (CATL3_PARTE)

Names and origin

Protein names

Recommended name:
    Putative cathepsin L 3
    EC=3.4.22.15

Gene names

ORF Names:

GSPATT00022199001

Organism

Paramecium tetraurelia

Taxonomic identifier

5888 [NCBI]

Taxonomic lineage

Eukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Peniculida › Parameciidae › Paramecium

Protein attributes

Sequence length	308 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	May be involved in extracellular digestion.
Catalytic activity	Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase C1 family.
Caution	This protein may be non-functional as it lacks the cysteine active site residue which is replaced by Gly-132.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 110	89	Activation peptide Potential		PRO_0000026275
	Chain	111 – 308	198	Putative cathepsin L 3		PRO_0000026276
Sites
	Active site	261	1	By similarity
	Active site	278	1	By similarity
	Site	132	1	Ancestral active site Cys
Amino acid modifications
	Disulfide bond	129 ↔ 170		By similarity
	Disulfide bond	254 ↔ 298		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q94715-1 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: 5615E8B6308FC4A5	FASTA	308	35,189
	10 20 30 40 50 60 MKQFLTAAIV TLLMTAGYYH LQEDDTNDFE RWALKNNKFY TESEKLYRME IYNSNKRMIE 70 80 90 100 110 120 EHNQREDVTY QMGENQFMTL SHEEFVDLYL QKSDSSVNIM GASLPEVQLE GLGAVDWRNY 130 140 150 160 170 180 TTVKEQGQCA SGWAFSVSNS LEAWYAIRGF QKINASTQQI VDCDYNNTGC SGGYNAYAME 190 200 210 220 230 240 YVLRVGLVSS TNYPYVAKNQ TCKQSRNGTY FINGYSFVGG SQSNLQYYLN NYPISVGVEA 250 260 270 280 290 300 SNWQFYRSGL FSNCSSNGTN HYALAVGFDS ANNWIVQNSW GTQWGESGNI RLYPQNTCGI LNYPYQVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia." Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R. , Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., Cohen J., Wincker P. Nature 444:171-178(2006) [PubMed: 17086204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Stock d4-2.
[2]	"Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia: purification, cloning, sequencing and specific inhibition by its expressed propeptide." Voelkel H., Kurz U., Linder J., Klumpp S., Gnau V., Jung G., Schultz J.E. Eur. J. Biochem. 238:198-206(1996) [PubMed: 8665938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-308. Strain: Stock 51.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT868652 Genomic DNA. Translation: CAK89030.1. X91756 mRNA. Translation: CAA62871.1.
PIR	S68784.
RefSeq	XP_001456427.1.
UniGene	Pte.895
3D structure databases
SMR	Q94715. Positions 26-304.
ModBase	Search...
Genome annotation databases
GeneID	5042212.
KEGG	ptm:GSPATT00022199001.
Enzyme and pathway databases
BRENDA	3.4.22.15. 21526.
Family and domain databases
InterPro	IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view]
PANTHER	PTHR12411. Peptidase_C1A. 1 hit.
Pfam	PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
SMART	SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. False negative. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATL3_PARTE

Accession

Primary (citable) accession number: Q94715
Secondary accession number(s): A0E163

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	October 23, 2007
Last modified:	January 19, 2010
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)