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O60911

- CATL2_HUMAN

UniProt

O60911 - CATL2_HUMAN

Protein

Cathepsin L2

Gene

CTSV

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    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 endopeptidase activity Source: ProtInc
    3. cysteine-type peptidase activity Source: ProtInc
    4. 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. cellular response to starvation Source: Ensembl
    4. decidualization Source: Ensembl
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. multicellular organismal aging Source: Ensembl
    8. nerve development Source: Ensembl
    9. response to glucocorticoid Source: Ensembl
    10. response to glucose Source: Ensembl
    11. response to gonadotropin Source: Ensembl
    12. Sertoli cell differentiation Source: Ensembl
    13. spermatogenesis Source: Ensembl

    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. external side of plasma membrane Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. lysosomal lumen Source: Reactome
    5. microvillus Source: Ensembl
    6. neuron projection Source: Ensembl
    7. perikaryon Source: Ensembl

    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. 1 interaction.
    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.
    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

    MNLSLVLAAF CLGIASAVPK FDQNLDTKWY QWKATHRRLY GANEEGWRRA    50
    VWEKNMKMIE LHNGEYSQGK HGFTMAMNAF GDMTNEEFRQ MMGCFRNQKF 100
    RKGKVFREPL FLDLPKSVDW RKKGYVTPVK NQKQCGSCWA FSATGALEGQ 150
    MFRKTGKLVS LSEQNLVDCS RPQGNQGCNG GFMARAFQYV KENGGLDSEE 200
    SYPYVAVDEI CKYRPENSVA NDTGFTVVAP GKEKALMKAV ATVGPISVAM 250
    DAGHSSFQFY KSGIYFEPDC SSKNLDHGVL VVGYGFEGAN SNNSKYWLVK 300
    NSWGPEWGSN GYVKIAKDKN NHCGIATAAS YPNV 334
    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. 1 interaction.
    IntActi O60911. 1 interaction.
    MINTi MINT-2797137.
    STRINGi 9606.ENSP00000259470.

    Chemistry

    BindingDBi O60911.
    ChEMBLi CHEMBL2111361.

    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.
    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

    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 1, 2014
    This is version 143 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