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UniProtKB/Swiss-Prot entry P07711


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATL1_HUMAN
Primary accession number P07711
Secondary accession numbers Q6IAV1 Q96QJ0
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on October 1, 1989 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 107)
Name and origin of the protein
Protein name Cathepsin L1 [Precursor]
Synonyms EC 3.4.22.15
Major excreted protein
MEP
Contains Cathepsin L1 heavy chain
Cathepsin L1 light chain
Gene name
Name: CTSL1
Synonyms: CTSL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3421948 [NCBI, ExPASy, EBI, Israel, Japan]
Gal S., Gottesman M.M.;
"Isolation and sequence of a cDNA for human pro-(cathepsin L).";
Biochem. J. 253:303-306(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2835398 [NCBI, ExPASy, EBI, Israel, Japan]
Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.;
"Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts.";
J. Clin. Invest. 81:1621-1629(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon endothelium;
The German cDNA consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02465; PubMed=15164053 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 114-288 AND 292-333.
DOI=10.1016/0014-5793(88)80028-0; PubMed=3342889 [NCBI, ExPASy, EBI, Israel, Japan]
Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.;
"Amino acid sequences of the human kidney cathepsins H and L.";
FEBS Lett. 228:341-345(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 113-154.
DOI=10.1093/nar/15.7.3186; PubMed=3550705 [NCBI, ExPASy, EBI, Israel, Japan]
Joseph L.J., Lapid S., Sukhatme V.P.;
"The major ras induced protein in NIH3T3 cells is cathepsin L.";
Nucleic Acids Res. 15:3186-3186(1987).
[9]
PROTEIN SEQUENCE OF 114-154 AND 292-333.
PubMed=3545185 [NCBI, ExPASy, EBI, Israel, Japan]
Mason R.W., Walker J.E., Northrop F.D.;
"The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line.";
Biochem. J. 240:373-377(1986).
[10]
GLYCOSYLATION AT ASN-221.
DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-333.
PubMed=8896443 [NCBI, ExPASy, EBI, Israel, Japan]
Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M.;
"Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.";
EMBO J. 15:5492-5503(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-333.
DOI=10.1016/S0014-5793(97)00216-0; PubMed=9141479 [NCBI, ExPASy, EBI, Israel, Japan]
Fujishima A., Imai Y., Nomura T., Fujisawa Y., Yamamoto Y., Sugarawa T.;
"The crystal structure of human cathepsin L complexed with E-64.";
FEBS Lett. 407:47-50(1997).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-333.
Cygler M., Coulombe R.;
Submitted (AUG-1999) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X12451; CAA30981.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20496; AAA66974.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457053; CAG33334.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537395; CAD97637.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL160279; CAI16308.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012612; AAH12612.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05256; CAA28877.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S01002; KHHUL.
RefSeq NP_001903.1; -.
NP_666023.1; -.
UniGene Hs.418123
3D structure databases
PDB
1CJL; X-ray; 2.20 A; A=22-333.[ExPASy / RCSB / EBI]
1CS8; X-ray; 1.80 A; A=19-333.[ExPASy / RCSB / EBI]
1ICF; X-ray; 2.00 A; A/C=114-288, B/D=292-333.[ExPASy / RCSB / EBI]
1MHW; X-ray; 1.90 A; A/B=114-288, C/D=292-333.[ExPASy / RCSB / EBI]
2NQD; X-ray; 1.75 A; B=113-333.[ExPASy / RCSB / EBI]
2VHS; X-ray; 1.50 A; A/B/C/D=114-333.[ExPASy / RCSB / EBI]
3BC3; X-ray; 2.20 A; A/B=114-333.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CJL; -.
1CS8; -.
1ICF; -.
1MHW; -.
2NQD; -.
2VHS; -.
3BC3; -.
ModBase P07711.
Protein-protein interaction databases
IntAct P07711; -.
Protein family/group databases
MEROPS C01.032; -.
I29.001; -.
Organism-specific databases
H-InvDB HIX0008146; -.
HGNC HGNC:2537; CTSL1.
GenAtlas CTSL1.
HPA CAB000459; -.
MIM 116880; gene. [NCBI / EBI]
PharmGKB PA27035; -.
GeneCards P07711.
Gene expression databases
ArrayExpress P07711; -.
CleanEx HS_CTSL1; -.
GermOnline ENSG00000135047; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005764; Cellular component: lysosome (non-traceable author statement from UniProtKB).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.
PANTHER PTHR12411; Peptidase_C1A; 1.
Pfam PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
BLOCKS P07711.
ProtoNet P07711.
Proteomic databases
PeptideAtlas P07711; -.
Genome annotation databases
Ensembl ENSG00000135047; Homo sapiens. [Contig view]
GeneID 1514; -.
KEGG hsa:1514; -.
Phylogenomic databases
HOGENOM P07711; -.
HOVERGEN P07711; -.
Other
BindingDB P07711; -.
DrugBank DB00040; Glucagon recombinant.
LinkHub P07711; -.
NextBio 6271; -.
SOURCE CTSL1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
PROPEP   18   113  96     Activation peptide. PRO_0000026244
CHAIN   114   288  175     Cathepsin L1 heavy chain. PRO_0000026245
PROPEP   289   291  3      PRO_0000026246
CHAIN   292   333  42     Cathepsin L1 light chain. PRO_0000026247
ACT_SITE   138   138         
ACT_SITE   276   276         
ACT_SITE   300   300         
CARBOHYD   221   221        N-linked (GlcNAc...). 
DISULFID   135   178         
DISULFID   169   211         
DISULFID   269   322        Interchain (between heavy and light chains). 
CONFLICT   56    56        M -> V (in Ref. 6; AAH12612). 
CONFLICT   268   268        D -> N (in Ref. 7; AA sequence). 
TURN   120   124  5      
HELIX   138   155  18      
HELIX   163   169  7      
HELIX   171   173  3      
HELIX   183   193  11      
STRAND   196   198  3      
TURN   199   201  3      
HELIX   215   217  3      
STRAND   218   220  3      
STRAND   224   227  4      
HELIX   232   241  10      
STRAND   244   249  6      
HELIX   254   257  4      
STRAND   261   264  4      
STRAND   276   285  10      
STRAND   294   299  6      
STRAND   311   315  5      
STRAND   317   320  4      
HELIX   321   323  3      
TURN   324   326  3      
STRAND   329   332  4      
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 37564 Da [This is the MW of the unprocessed precursor] CRC64: 8CD17D00EF859D85 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE 

        70         80         90        100        110        120 
LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW 

       130        140        150        160        170        180 
REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG 

       190        200        210        220        230        240 
GLMDYAFQYV QDNGGLDSEE SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA 

       250        260        270        280        290        300 
TVGPISVAID AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN 

       310        320        330 
SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV 

P07711 in FASTA format

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