O60911 (CATL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin L2
EC=3.4.22.43

Alternative name(s):
Cathepsin U
Cathepsin V

Gene names

Name:	CTSL2
Synonyms:	CATL2, CTSU, CTSV
ORF Names:	UNQ268/PRO305

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	334 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	Cysteine protease. May have an important role in corneal physiology. Ref.2 Ref.3
Catalytic activity	The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec). Ref.3
Subcellular location	Lysosome Potential.
Tissue specificity	Predominantly expressed in the thymus and testis. Also expressed in corneal epithelium, and to a lesser extent in conjunctival epithelium and skin. Ref.1 Ref.2 Ref.3
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Sertoli cell differentiation Inferred from electronic annotation. Source: Compara antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome autophagic cell death Inferred from electronic annotation. Source: Compara cellular response to starvation Inferred from electronic annotation. Source: Compara decidualization Inferred from electronic annotation. Source: Compara multicellular organismal aging Inferred from electronic annotation. Source: Compara nerve development Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara response to gonadotropin stimulus Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara lysosomal lumen Traceable author statement. Source: Reactome microvillus Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara perikaryon Inferred from electronic annotation. Source: Compara
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: Compara cysteine-type endopeptidase activity Traceable author statement Ref.1. Source: ProtInc peptide binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 113

96

Activation peptide

PRO_0000026277

Chain

114 – 334

221

Cathepsin L2

PRO_0000026278

Sites

Active site

138

1

Ref.8

Active site

277

1

Ref.8

Active site

301

1

Ref.8

Amino acid modifications

Glycosylation

221

1

N-linked (GlcNAc...) Potential

Glycosylation

292

1

N-linked (GlcNAc...) Potential

Disulfide bond

135 ↔ 178

Disulfide bond

169 ↔ 211

Disulfide bond

270 ↔ 323

Experimental info

Sequence conflict

81

1

G → P in CAA75029. Ref.1

Secondary structure

1

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334

Helix Strand Turn

Details...

Helix

120 – 123

4

Helix

138 – 155

18

Helix

163 – 169

7

Helix

171 – 173

3

Helix

177 – 179

3

Helix

183 – 193

11

Beta strand

196 – 198

3

Turn

199 – 201

3

Helix

215 – 217

3

Beta strand

218 – 220

3

Beta strand

225 – 227

3

Helix

233 – 242

10

Beta strand

246 – 250

5

Helix

255 – 258

4

Beta strand

262 – 265

4

Beta strand

272 – 274

3

Beta strand

277 – 289

13

Beta strand

293 – 300

8

Beta strand

312 – 316

5

Beta strand

318 – 321

4

Helix

322 – 324

3

Turn

325 – 327

3

Beta strand

330 – 332

3

Sequences

	Sequence		Length	Mass (Da)
	O60911 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: CD2DE51AC5F242C8	FASTA	334	37,329
	10 20 30 40 50 60 MNLSLVLAAF CLGIASAVPK FDQNLDTKWY QWKATHRRLY GANEEGWRRA VWEKNMKMIE 70 80 90 100 110 120 LHNGEYSQGK HGFTMAMNAF GDMTNEEFRQ MMGCFRNQKF RKGKVFREPL FLDLPKSVDW 130 140 150 160 170 180 RKKGYVTPVK NQKQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS RPQGNQGCNG 190 200 210 220 230 240 GFMARAFQYV KENGGLDSEE SYPYVAVDEI CKYRPENSVA NDTGFTVVAP GKEKALMKAV 250 260 270 280 290 300 ATVGPISVAM DAGHSSFQFY KSGIYFEPDC SSKNLDHGVL VVGYGFEGAN SNNSKYWLVK 310 320 330 NSWGPEWGSN GYVKIAKDKN NHCGIATAAS YPNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas." Santamaria I., Velasco G., Cazorla M., Fueyo A., Campo E., Lopez-Otin C. Cancer Res. 58:1624-1630(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Brain.
[2]	"Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium." Adachi W., Kawamoto S., Ohno I., Nishida K., Kinoshita S., Matsubara K., Okubo K. Invest. Ophthalmol. Vis. Sci. 39:1789-1796(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Corneal epithelium.
[3]	"Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization." Broemme D., Li Z., Barnes M., Mehler E. Biochemistry 38:2377-2385(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Kidney and Thymus.
[4]	"Genomic organization and chromosomal localization of the human cathepsin L2 gene." Itoh R., Kawamoto S., Adachi W., Kinoshita S., Okubo K. DNA Res. 6:137-140(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Crystal structure of human cathepsin V." Somoza J.R., Zhan H., Bowman K.K., Yu L., Mortara K.D., Palmer J.T., Clark J.M., McGrath M.E. Biochemistry 39:12543-12551(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), ACTIVE SITE.
[9]	Erratum Somoza J.R., Zhan H., Bowman K.K., Yu L., Mortara K.D., Palmer J.T., Clark J.M., McGrath M.E. Biochemistry 40:4200-4200(2001)
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y14734 mRNA. Translation: CAA75029.1.
AB001928 mRNA. Translation: BAA25909.1.
AF070448 mRNA. Translation: AAC23598.1.
AB019534 Genomic DNA. Translation: BAA34365.1.
AY358641 mRNA. Translation: AAQ89004.1.
AL445670 Genomic DNA. Translation: CAI15053.1.
BC023504 mRNA. Translation: AAH23504.1.
BC110512 mRNA. Translation: AAI10513.1.

IPI

IPI00000013.

RefSeq

NP_001188504.1. NM_001201575.1.
NP_001324.2. NM_001333.3.

UniGene

Hs.610096.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FH0	X-ray	1.60	A/B	114-334	[»]
3H6S	X-ray	2.22	A/B/C/D	114-334	[»]
3KFQ	X-ray	1.99	A/B	114-334	[»]

ProteinModelPortal

O60911.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60911. 1 interaction.

STRING

9606.ENSP00000259470.

Protein family/group databases

MEROPS

I29.010.

PTM databases

PhosphoSite

O60911.

Proteomic databases

PaxDb

O60911.

PeptideAtlas

O60911.

PRIDE

O60911.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000259470; ENSP00000259470; ENSG00000136943.
ENST00000538255; ENSP00000445052; ENSG00000136943.

GeneID

1515.

KEGG

hsa:1515.

UCSC

uc004awt.3. human.

Organism-specific databases

CTD

1515.

GeneCards

GC09M099794.

HGNC

HGNC:2538. CTSL2.

HPA

CAB017112.

MIM

603308. gene.

neXtProt

NX_O60911.

PharmGKB

PA27036.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4870.

HOGENOM

HOG000230774.

HOVERGEN

HBG011513.

InParanoid

O60911.

KO

K01375.

OMA

FDQNLDT.

OrthoDB

EOG48PMKF.

PhylomeDB

O60911.

Enzyme and pathway databases

BRENDA

3.4.22.43. 2681.

Reactome

REACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

SABIO-RK

O60911.

Gene expression databases

Bgee

O60911.

CleanEx

HS_CTSL2.

Genevestigator

O60911.

GermOnline

ENSG00000136943. Homo sapiens.

Family and domain databases

InterPro

IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_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. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O60911.

ChEMBL

CHEMBL3272.

ChiTaRS

CTSL2. human.

EvolutionaryTrace

O60911.

GenomeRNAi

1515.

NextBio

6277.

SOURCE

Search...

Entry information

Entry name

CATL2_HUMAN

Accession

Primary (citable) accession number: O60911
Secondary accession number(s): O60233, Q2TB86, Q5T1U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.