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Protein

Cathepsin L2

Gene

CTSV

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine protease. May have an important role in corneal physiology.2 Publications

Catalytic activityi

The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1381 Publication1
Active sitei2771 Publication1
Active sitei3011 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciZFISH:HS06256-MONOMER.
BRENDAi3.4.22.43. 2681.
ReactomeiR-HSA-1236977. Endosomal/Vacuolar pathway.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2132295. MHC class II antigen presentation.
SABIO-RKO60911.

Protein family/group databases

MEROPSiI29.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L2 (EC:3.4.22.43)
Alternative name(s):
Cathepsin U
Cathepsin V
Gene namesi
Name:CTSV
Synonyms:CATL2, CTSL2, CTSU
ORF Names:UNQ268/PRO305
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2538. CTSV.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi1515.
OpenTargetsiENSG00000136943.
PharmGKBiPA27036.

Chemistry databases

ChEMBLiCHEMBL3272.
GuidetoPHARMACOLOGYi2352.

Polymorphism and mutation databases

BioMutaiCTSV.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002627718 – 113Activation peptideAdd BLAST96
ChainiPRO_0000026278114 – 334Cathepsin L2Add BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi135 ↔ 178
Disulfide bondi169 ↔ 211
Glycosylationi221N-linked (GlcNAc...)1 Publication1
Disulfide bondi270 ↔ 323
Glycosylationi292N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO60911.
PaxDbiO60911.
PeptideAtlasiO60911.
PRIDEiO60911.

PTM databases

iPTMnetiO60911.
PhosphoSitePlusiO60911.

Expressioni

Tissue specificityi

Predominantly expressed in the thymus and testis. Also expressed in corneal epithelium, and to a lesser extent in conjunctival epithelium and skin.3 Publications

Gene expression databases

BgeeiENSG00000136943.
CleanExiHS_CTSL2.
ExpressionAtlasiO60911. baseline and differential.
GenevisibleiO60911. HS.

Organism-specific databases

HPAiCAB017112.

Interactioni

Protein-protein interaction databases

BioGridi107895. 22 interactors.
IntActiO60911. 15 interactors.
MINTiMINT-2797137.
STRINGi9606.ENSP00000259470.

Chemistry databases

BindingDBiO60911.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi120 – 123Combined sources4
Helixi138 – 155Combined sources18
Helixi163 – 169Combined sources7
Helixi171 – 173Combined sources3
Helixi177 – 179Combined sources3
Helixi183 – 193Combined sources11
Beta strandi196 – 198Combined sources3
Turni199 – 201Combined sources3
Helixi215 – 217Combined sources3
Beta strandi218 – 220Combined sources3
Beta strandi225 – 227Combined sources3
Helixi233 – 242Combined sources10
Beta strandi246 – 250Combined sources5
Helixi255 – 258Combined sources4
Beta strandi262 – 265Combined sources4
Beta strandi272 – 274Combined sources3
Beta strandi277 – 289Combined sources13
Beta strandi293 – 300Combined sources8
Beta strandi312 – 316Combined sources5
Beta strandi318 – 321Combined sources4
Helixi322 – 324Combined sources3
Turni325 – 327Combined sources3
Beta strandi330 – 332Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FH0X-ray1.60A/B114-334[»]
3H6SX-ray2.22A/B/C/D114-334[»]
3KFQX-ray1.99A/B114-334[»]
ProteinModelPortaliO60911.
SMRiO60911.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60911.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiO60911.
KOiK01375.
OMAiANEEGWR.
OrthoDBiEOG091G0AKT.
PhylomeDBiO60911.
TreeFamiTF313739.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O60911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLSLVLAAF CLGIASAVPK FDQNLDTKWY QWKATHRRLY GANEEGWRRA
60 70 80 90 100
VWEKNMKMIE LHNGEYSQGK HGFTMAMNAF GDMTNEEFRQ MMGCFRNQKF
110 120 130 140 150
RKGKVFREPL FLDLPKSVDW RKKGYVTPVK NQKQCGSCWA FSATGALEGQ
160 170 180 190 200
MFRKTGKLVS LSEQNLVDCS RPQGNQGCNG GFMARAFQYV KENGGLDSEE
210 220 230 240 250
SYPYVAVDEI CKYRPENSVA NDTGFTVVAP GKEKALMKAV ATVGPISVAM
260 270 280 290 300
DAGHSSFQFY KSGIYFEPDC SSKNLDHGVL VVGYGFEGAN SNNSKYWLVK
310 320 330
NSWGPEWGSN GYVKIAKDKN NHCGIATAAS YPNV
Length:334
Mass (Da):37,329
Last modified:December 1, 2000 - v2
Checksum:iCD2DE51AC5F242C8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti81G → P in CAA75029 (PubMed:9563472).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6723.1.
RefSeqiNP_001188504.1. NM_001201575.1.
NP_001324.2. NM_001333.3.
UniGeneiHs.610096.

Genome annotation databases

EnsembliENST00000259470; ENSP00000259470; ENSG00000136943.
ENST00000538255; ENSP00000445052; ENSG00000136943.
GeneIDi1515.
KEGGihsa:1515.
UCSCiuc004awt.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6723.1.
RefSeqiNP_001188504.1. NM_001201575.1.
NP_001324.2. NM_001333.3.
UniGeneiHs.610096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FH0X-ray1.60A/B114-334[»]
3H6SX-ray2.22A/B/C/D114-334[»]
3KFQX-ray1.99A/B114-334[»]
ProteinModelPortaliO60911.
SMRiO60911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107895. 22 interactors.
IntActiO60911. 15 interactors.
MINTiMINT-2797137.
STRINGi9606.ENSP00000259470.

Chemistry databases

BindingDBiO60911.
ChEMBLiCHEMBL3272.
GuidetoPHARMACOLOGYi2352.

Protein family/group databases

MEROPSiI29.010.

PTM databases

iPTMnetiO60911.
PhosphoSitePlusiO60911.

Polymorphism and mutation databases

BioMutaiCTSV.

Proteomic databases

MaxQBiO60911.
PaxDbiO60911.
PeptideAtlasiO60911.
PRIDEiO60911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259470; ENSP00000259470; ENSG00000136943.
ENST00000538255; ENSP00000445052; ENSG00000136943.
GeneIDi1515.
KEGGihsa:1515.
UCSCiuc004awt.4. human.

Organism-specific databases

CTDi1515.
DisGeNETi1515.
GeneCardsiCTSV.
HGNCiHGNC:2538. CTSV.
HPAiCAB017112.
MIMi603308. gene.
neXtProtiNX_O60911.
OpenTargetsiENSG00000136943.
PharmGKBiPA27036.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiO60911.
KOiK01375.
OMAiANEEGWR.
OrthoDBiEOG091G0AKT.
PhylomeDBiO60911.
TreeFamiTF313739.

Enzyme and pathway databases

BioCyciZFISH:HS06256-MONOMER.
BRENDAi3.4.22.43. 2681.
ReactomeiR-HSA-1236977. Endosomal/Vacuolar pathway.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2132295. MHC class II antigen presentation.
SABIO-RKO60911.

Miscellaneous databases

EvolutionaryTraceiO60911.
GeneWikiiCathepsin_L2.
GenomeRNAii1515.
PROiO60911.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136943.
CleanExiHS_CTSL2.
ExpressionAtlasiO60911. baseline and differential.
GenevisibleiO60911. HS.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATL2_HUMAN
AccessioniPrimary (citable) accession number: O60911
Secondary accession number(s): O60233, Q2TB86, Q5T1U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 1, 2000
Last modified: November 2, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.