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O60911

- CATL2_HUMAN

UniProt

O60911 - CATL2_HUMAN

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Protein

Cathepsin L2

Gene

CTSV

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 13811 Publication
Active sitei277 – 27711 Publication
Active sitei301 – 30111 Publication

GO - Molecular functioni

  1. aminopeptidase activity Source: Ensembl
  2. cysteine-type carboxypeptidase activity Source: Ensembl
  3. cysteine-type endopeptidase activity Source: ProtInc
  4. cysteine-type peptidase activity Source: ProtInc
  5. peptide binding Source: Ensembl

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. autophagic cell death Source: Ensembl
  3. catagen Source: Ensembl
  4. cellular response to starvation Source: Ensembl
  5. decidualization Source: Ensembl
  6. extracellular matrix disassembly Source: Reactome
  7. extracellular matrix organization Source: Reactome
  8. hair follicle morphogenesis Source: Ensembl
  9. multicellular organismal aging Source: Ensembl
  10. negative regulation of keratinocyte proliferation Source: Ensembl
  11. nerve development Source: Ensembl
  12. protein autoprocessing Source: Ensembl
  13. regulation of actin cytoskeleton reorganization Source: Ensembl
  14. response to glucocorticoid Source: Ensembl
  15. response to glucose Source: Ensembl
  16. response to gonadotropin Source: Ensembl
  17. Sertoli cell differentiation Source: Ensembl
  18. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.43. 2681.
ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
REACT_118572. Degradation of the extracellular matrix.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
SABIO-RKO60911.

Protein family/group databases

MEROPSiC01.009.

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:2538. CTSV.

Subcellular locationi

Lysosome Curated

GO - Cellular componenti

  1. cytoplasmic vesicle Source: Ensembl
  2. external side of plasma membrane Source: Ensembl
  3. extracellular region Source: Reactome
  4. extracellular space Source: Ensembl
  5. extracellular vesicular exosome Source: UniProt
  6. lysosomal lumen Source: Reactome
  7. microvillus Source: Ensembl
  8. neuron projection Source: Ensembl
  9. nucleolus Source: Ensembl
  10. perikaryon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27036.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 11396Activation peptidePRO_0000026277Add
BLAST
Chaini114 – 334221Cathepsin L2PRO_0000026278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 178
Disulfide bondi169 ↔ 211
Glycosylationi221 – 2211N-linked (GlcNAc...)1 Publication
Disulfide bondi270 ↔ 323
Glycosylationi292 – 2921N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO60911.
PaxDbiO60911.
PeptideAtlasiO60911.
PRIDEiO60911.

PTM databases

PhosphoSiteiO60911.

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

BgeeiO60911.
CleanExiHS_CTSL2.
GenevestigatoriO60911.

Organism-specific databases

HPAiCAB017112.

Interactioni

Protein-protein interaction databases

BioGridi107895. 9 interactions.
IntActiO60911. 1 interaction.
MINTiMINT-2797137.
STRINGi9606.ENSP00000259470.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi120 – 1234
Helixi138 – 15518
Helixi163 – 1697
Helixi171 – 1733
Helixi177 – 1793
Helixi183 – 19311
Beta strandi196 – 1983
Turni199 – 2013
Helixi215 – 2173
Beta strandi218 – 2203
Beta strandi225 – 2273
Helixi233 – 24210
Beta strandi246 – 2505
Helixi255 – 2584
Beta strandi262 – 2654
Beta strandi272 – 2743
Beta strandi277 – 28913
Beta strandi293 – 3008
Beta strandi312 – 3165
Beta strandi318 – 3214
Helixi322 – 3243
Turni325 – 3273
Beta strandi330 – 3323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FH0X-ray1.60A/B114-334[»]
3H6SX-ray2.22A/B/C/D114-334[»]
3KFQX-ray1.99A/B114-334[»]
ProteinModelPortaliO60911.
SMRiO60911. Positions 21-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60911.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiO60911.
KOiK01375.
OMAiANEEGWR.
OrthoDBiEOG786H3P.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811G → P in CAA75029. (PubMed:9563472)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
XP_006717023.1. XM_006716960.1.
UniGeneiHs.610096.

Genome annotation databases

EnsembliENST00000259470; ENSP00000259470; ENSG00000136943.
ENST00000538255; ENSP00000445052; ENSG00000136943.
GeneIDi1515.
KEGGihsa:1515.
UCSCiuc004awt.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6723.1.
RefSeqi NP_001188504.1. NM_001201575.1.
NP_001324.2. NM_001333.3.
XP_006717023.1. XM_006716960.1.
UniGenei Hs.610096.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O60911.
SMRi O60911. Positions 21-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107895. 9 interactions.
IntActi O60911. 1 interaction.
MINTi MINT-2797137.
STRINGi 9606.ENSP00000259470.

Chemistry

BindingDBi O60911.
ChEMBLi CHEMBL3272.

Protein family/group databases

MEROPSi C01.009.

PTM databases

PhosphoSitei O60911.

Proteomic databases

MaxQBi O60911.
PaxDbi O60911.
PeptideAtlasi O60911.
PRIDEi O60911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259470 ; ENSP00000259470 ; ENSG00000136943 .
ENST00000538255 ; ENSP00000445052 ; ENSG00000136943 .
GeneIDi 1515.
KEGGi hsa:1515.
UCSCi uc004awt.3. human.

Organism-specific databases

CTDi 1515.
GeneCardsi GC09M099791.
HGNCi HGNC:2538. CTSV.
HPAi CAB017112.
MIMi 603308. gene.
neXtProti NX_O60911.
PharmGKBi PA27036.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4870.
GeneTreei ENSGT00760000118871.
HOGENOMi HOG000230774.
HOVERGENi HBG011513.
InParanoidi O60911.
KOi K01375.
OMAi ANEEGWR.
OrthoDBi EOG786H3P.
PhylomeDBi O60911.
TreeFami TF313739.

Enzyme and pathway databases

BRENDAi 3.4.22.43. 2681.
Reactomei REACT_111168. Endosomal/Vacuolar pathway.
REACT_118572. Degradation of the extracellular matrix.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
SABIO-RK O60911.

Miscellaneous databases

ChiTaRSi CTSL2. human.
EvolutionaryTracei O60911.
GeneWikii Cathepsin_L2.
GenomeRNAii 1515.
NextBioi 6277.
PROi O60911.
SOURCEi Search...

Gene expression databases

Bgeei O60911.
CleanExi HS_CTSL2.
Genevestigatori O60911.

Family and domain databases

InterProi 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), ACTIVE SITE.

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: October 29, 2014
This is version 144 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

External Data

Dasty 3