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O60911 (CATL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin L2

EC=3.4.22.43
Alternative name(s):
Cathepsin U
Cathepsin V
Gene names
Name:CTSV
Synonyms:CATL2, CTSL2, CTSU
ORF Names:UNQ268/PRO305
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell differentiation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

decidualization

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

multicellular organismal aging

Inferred from electronic annotation. Source: Ensembl

nerve development

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to gonadotropin

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

lysosomal lumen

Traceable author statement. Source: Reactome

microvillus

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: Ensembl

cysteine-type endopeptidase activity

Traceable author statement Ref.1. Source: ProtInc

cysteine-type peptidase activity

Traceable author statement Ref.1. Source: ProtInc

peptide binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 11396Activation peptide
PRO_0000026277
Chain114 – 334221Cathepsin L2
PRO_0000026278

Sites

Active site1381 Ref.9
Active site2771 Ref.9
Active site3011 Ref.9

Amino acid modifications

Glycosylation2211N-linked (GlcNAc...) Ref.8
Glycosylation2921N-linked (GlcNAc...) Ref.8
Disulfide bond135 ↔ 178
Disulfide bond169 ↔ 211
Disulfide bond270 ↔ 323

Experimental info

Sequence conflict811G → P in CAA75029. Ref.1

Secondary structure

........................................... 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60911 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: CD2DE51AC5F242C8

FASTA33437,329
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Determination of cathepsin V activity and intracellular trafficking by N-glycosylation."
Niwa Y., Suzuki T., Dohmae N., Umezawa K., Simizu S.
FEBS Lett. 586:3601-3607(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-221 AND ASN-292.
[9]"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.
[10]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.
CCDSCCDS6723.1.
RefSeqNP_001188504.1. NM_001201575.1.
NP_001324.2. NM_001333.3.
XP_006717023.1. XM_006716960.1.
UniGeneHs.610096.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FH0X-ray1.60A/B114-334[»]
3H6SX-ray2.22A/B/C/D114-334[»]
3KFQX-ray1.99A/B114-334[»]
ProteinModelPortalO60911.
SMRO60911. Positions 21-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107895. 1 interaction.
IntActO60911. 1 interaction.
MINTMINT-2797137.
STRING9606.ENSP00000259470.

Chemistry

BindingDBO60911.
ChEMBLCHEMBL2111361.

Protein family/group databases

MEROPSC01.009.

PTM databases

PhosphoSiteO60911.

Proteomic databases

MaxQBO60911.
PaxDbO60911.
PeptideAtlasO60911.
PRIDEO60911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259470; ENSP00000259470; ENSG00000136943.
ENST00000538255; ENSP00000445052; ENSG00000136943.
GeneID1515.
KEGGhsa:1515.
UCSCuc004awt.3. human.

Organism-specific databases

CTD1515.
GeneCardsGC09M099791.
HGNCHGNC:2538. CTSV.
HPACAB017112.
MIM603308. gene.
neXtProtNX_O60911.
PharmGKBPA27036.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidO60911.
KOK01375.
OMAANEEGWR.
OrthoDBEOG786H3P.
PhylomeDBO60911.
TreeFamTF313739.

Enzyme and pathway databases

BRENDA3.4.22.43. 2681.
ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.
SABIO-RKO60911.

Gene expression databases

BgeeO60911.
CleanExHS_CTSL2.
GenevestigatorO60911.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSL2. human.
EvolutionaryTraceO60911.
GeneWikiCathepsin_L2.
GenomeRNAi1515.
NextBio6277.
PROO60911.
SOURCESearch...

Entry information

Entry nameCATL2_HUMAN
AccessionPrimary (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 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM