A0E358 (CATL2_PARTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin L 2
EC=3.4.22.15

Gene names

ORF Names:

GSPATT00022898001

Organism

Paramecium tetraurelia [Reference proteome]

Taxonomic identifier

5888 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	May be involved in extracellular digestion By similarity.
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 By similarity.
Sequence similarities	Belongs to the peptidase C1 family.
Sequence caution	The sequence CAK89725.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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 – 24	24	Potential
	Propeptide	25 – 109	85	Activation peptide By similarity		PRO_0000307837
	Chain	110 – 314	205	Cathepsin L 2		PRO_0000307838
Sites
	Active site	135	1	By similarity
	Active site	265	1	By similarity
	Active site	282	1	By similarity
Amino acid modifications
	Disulfide bond	132 ↔ 175		By similarity
	Disulfide bond	166 ↔ 207		By similarity
	Disulfide bond	259 ↔ 302		By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0E358 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: 2D580F2BB700AFD0	FASTA	314	34,935
	10 20 30 40 50 60 MMLLGASLYL NNTQEVSDEI DTANLYANWK MKYNRRYTSQ RDEMYRFKVF SDNLNYIRAF 70 80 90 100 110 120 QDSTESATYT LELNQFADMS QQEFASTYLS LRVPKTAKLN ASNANFQYKG AEVDWTDNKK 130 140 150 160 170 180 VKYPAVKNQG SCGSCWAFSA VGALEINTDI ELNKKYELSE QDLVDCSGPY DNEGCNGGWM 190 200 210 220 230 240 DSAFEYVADN GLAEAKDYPY TAKDGTCKTS VKRPYTHVQG FTDIDSCDEL AQAIQERTVS 250 260 270 280 290 300 VAVDANPWQF YRSGVLSKCT KNLNHGVVLV GVQADGAWKI RNSWGSSWGE AGHIRLAGGD 310 TCGICAAPSF PILG

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Stock d4-2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT868656 Genomic DNA. Translation: CAK89725.1. Different initiation.
UniGene	Pte.76.
3D structure databases
ProteinModelPortal	A0E358.
ModBase	Search...
Protein family/group databases
MEROPS	C01.113.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
ProtClustDB	CLSZ2453112.
Family and domain databases
InterPro	IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view]
PANTHER	PTHR12411. PTHR12411. 1 hit.
Pfam	PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
SMART	SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATL2_PARTE

Accession

Primary (citable) accession number: A0E358

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	October 23, 2007
Last modified:	October 3, 2012
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)