Reviewed, UniProtKB/Swiss-Prot Q94714 (CATL1_PARTE)

Names and origin

Protein names

Recommended name:
    Cathepsin L 1
    EC=3.4.22.15

Gene names

ORF Names:

GSPATT00020990001

Organism

Paramecium tetraurelia

Taxonomic identifier

5888 [NCBI]

Taxonomic lineage

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	Evidence at protein 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Zymogen
Technical term	Direct protein sequencing
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 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 – 24	24	Potential
	Propeptide	25 – 109	85	Activation peptide Ref.1		PRO_0000026273
	Chain	110 – 314	205	Cathepsin L 1		PRO_0000026274
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)
	Q94714-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 56B4489D118FF097	FASTA	314	35,159
	10 20 30 40 50 60 MMLLGASLYL NNTQEVSDEI DTANLYANWK MKYNRRYTNQ RDEMYRYKVF TDNLNYIRAF 70 80 90 100 110 120 YESPEEATFT LELNQFADMS QQEFAQTYLS LKVPRTAKLN AANSNFQYKG AEVDWTDNKK 130 140 150 160 170 180 VKYPAVKNQG SCGSCWAFSA VGALEINTDI ELNRKYELSE QDLVDCSGPY DNDGCNGGWM 190 200 210 220 230 240 DSAFEYVADN GLAEAKDYPY TAKDGTCKTS VKRPYTHVQG FKDIDSCDEL AQTIQERTVA 250 260 270 280 290 300 VAVDANPWQF YRSGVLSKCT KNLNHGVVLV GVQADGAWKI RNSWGSSWGE AGHIRLAGGD 310 TCGICAAPSF PILG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], PROTEIN SEQUENCE OF 110-129 AND 181-204. Strain: Stock 51.
[2]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X91754 mRNA. Translation: CAA62869.1. CT868618 Genomic DNA. Translation: CAK87348.1. Different initiation.
PIR	S68783.
UniGene	Pte.76
3D structure databases
HSSP	HSSP built from PDB template 1K3B based on UniProtKB P53634.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.4.22.15. 21526.
Family and domain databases
InterPro	IPR000169. Pept_cys_AS. 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]
PRINTS	PR00705. PAPAIN.
ProDom	PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	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

CATL1_PARTE

Accession

Primary (citable) accession number: Q94714
Secondary accession number(s): A0DWD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)