Reviewed, UniProtKB/Swiss-Prot O60911 (CATL2_HUMAN)

Names and origin

Protein names

Recommended name:
    Cathepsin L2
    EC=3.4.22.43
Alternative name(s):
    Cathepsin V
    Cathepsin U

Gene names

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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).
Subcellular location	LysosomePotential.
Tissue specificity	Predominantly expressed in the thymus and testis. Also expressed in corneal epithelium, and to a lesser extent in conjuctival epithelium and skin.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Glycoprotein Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Uncategorized	cathepsin L activity Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
srp-6	O01462	1	EBI-1549974,EBI-1549936	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 113

96

Activation peptide

Chain

114 – 334

221

Cathepsin L2

Sites

Active site

138

1

Active site

276

1

Active site

301

1

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

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)
	O60911-1 [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: 9563472] [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: 9727401] [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: 10029531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, 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: 10382972] [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: 12975309] [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: 15164053] [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: 15489334] [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: 11027133] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[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

EMBLGenBankDDBJ

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.

RefSeq

NP_001324.2.

UniGene

Hs.660866

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FH0	X-ray	1.60	A/B	114-334	[»]

SMR

O60911. Positions 21-334.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60911.

Protein family/group databases

MEROPS

C01.009.
I29.010.

Proteomic databases

PeptideAtlas

O60911.

Genome annotation databases

Ensembl

ENSG00000136943. Homo sapiens. [Contig view]

GeneID

1515.

KEGG

hsa:1515.

Organism-specific databases

H-InvDB

HIX0034737.

HGNC

HGNC:2538. CTSL2.

HPA

CAB017112.

MIM

603308. gene.

PharmGKB

PA27036.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

O60911.

HOVERGEN

O60911.

Gene expression databases

ArrayExpress

O60911.

CleanEx

HS_CTSL2.

GermOnline

ENSG00000136943. Homo sapiens.

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. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

BLOCKS

Search...

Other Resources

SOURCE

Search...

ProtoNet

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:	July 22, 2008
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)