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UniProtKB/Swiss-Prot entry P25774


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

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Entry information
Entry name CATS_HUMAN
Primary accession number P25774
Secondary accession numbers Q5T5I0 Q9BUG3
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on February 21, 2006 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 98)
Name and origin of the protein
Protein name Cathepsin S [Precursor]
Synonym EC 3.4.22.27
Gene name
Name: CTSS
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], AND VARIANT THR-161.
TISSUE=Alveolar macrophage;
PubMed=1373132 [NCBI, ExPASy, EBI, Israel, Japan]
Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A.;
"Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease.";
J. Biol. Chem. 267:7258-7262(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=1377692 [NCBI, ExPASy, EBI, Israel, Japan]
Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C.;
"Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S.";
J. Biol. Chem. 267:13708-13713(1992).
[3]
SEQUENCE REVISION TO 211.
Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-161.
PubMed=8157683 [NCBI, ExPASy, EBI, Israel, Japan]
Shi G.-P., Webb A.C., Foster K.E., Knoll J.H.M., Lemere C.A., Munger J.S., Chapman H.A.;
"Human cathepsin S: chromosomal localization, gene structure, and tissue distribution.";
J. Biol. Chem. 269:11530-11536(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-113.
TISSUE=Pancreas;
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]
3D-STRUCTURE MODELING OF 115-331.
DOI=10.1093/protein/11.11.1007; PubMed=9876921 [NCBI, ExPASy, EBI, Israel, Japan]
Fengler A., Brandt W.;
"Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics.";
Protein Eng. 11:1007-1013(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 115-331.
DOI=10.1107/S0907444901021825; PubMed=11856830 [NCBI, ExPASy, EBI, Israel, Japan]
Turkenburg J.P., Lamers M.B., Brzozowski A.M., Wright L.M., Hubbard R.E., Sturt S.L., Williams D.H.;
"Structure of a Cys25-->Ser mutant of human cathepsin S.";
Acta Crystallogr. D 58:451-455(2002).
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
S93414; AAB22005.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M86553; AAA35655.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M90696; AAC37592.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07374; AAB60643.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07370; AAB60643.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07371; AAB60643.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07372; AAB60643.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07373; AAB60643.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356292; CAI13657.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002642; AAH02642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42482; A42482.
RefSeq NP_004070.3; -.
UniGene Hs.181301
3D structure databases
PDB
1BXF; Model; -; A=115-331.[ExPASy / RCSB / EBI]
1GLO; X-ray; 2.20 A; A=115-331.[ExPASy / RCSB / EBI]
1MS6; X-ray; 1.90 A; A=115-331.[ExPASy / RCSB / EBI]
1NPZ; X-ray; 2.00 A; A/B=115-331.[ExPASy / RCSB / EBI]
1NQC; X-ray; 1.80 A; A=115-331.[ExPASy / RCSB / EBI]
2C0Y; X-ray; 2.10 A; A=17-331.[ExPASy / RCSB / EBI]
2F1G; X-ray; 1.90 A; A/B=112-331.[ExPASy / RCSB / EBI]
2FQ9; X-ray; 1.65 A; A/B=114-331.[ExPASy / RCSB / EBI]
2FRA; X-ray; 1.90 A; A/B=114-331.[ExPASy / RCSB / EBI]
2FRQ; X-ray; 1.60 A; A/B=114-331.[ExPASy / RCSB / EBI]
2FT2; X-ray; 1.70 A; A/B=114-331.[ExPASy / RCSB / EBI]
2FUD; X-ray; 1.95 A; A/B=114-331.[ExPASy / RCSB / EBI]
2FYE; X-ray; 2.20 A; A=115-331.[ExPASy / RCSB / EBI]
2G6D; X-ray; 2.50 A; A=115-331.[ExPASy / RCSB / EBI]
2G7Y; X-ray; 2.00 A; A/B=114-331.[ExPASy / RCSB / EBI]
2H7J; X-ray; 1.50 A; A/B=112-331.[ExPASy / RCSB / EBI]
2HH5; X-ray; 1.80 A; A/B=112-331.[ExPASy / RCSB / EBI]
2HHN; X-ray; 1.55 A; A/B=112-331.[ExPASy / RCSB / EBI]
2HXZ; X-ray; 1.90 A; A/B/C=112-331.[ExPASy / RCSB / EBI]
2OP3; X-ray; 1.60 A; A/B=112-331.[ExPASy / RCSB / EBI]
2R9M; X-ray; 1.97 A; A/B=115-331.[ExPASy / RCSB / EBI]
2R9N; X-ray; 2.00 A; A/B=115-331.[ExPASy / RCSB / EBI]
2R9O; X-ray; 2.00 A; A/B=115-331.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BXF; -.
1GLO; -.
1MS6; -.
1NPZ; -.
1NQC; -.
2C0Y; -.
2F1G; -.
2FQ9; -.
2FRA; -.
2FRQ; -.
2FT2; -.
2FUD; -.
2FYE; -.
2G6D; -.
2G7Y; -.
2H7J; -.
2HH5; -.
2HHN; -.
2HXZ; -.
2OP3; -.
2R9M; -.
2R9N; -.
2R9O; -.
SMR P25774; 18-331.
ModBase P25774.
Protein family/group databases
MEROPS C01.034; -.
I29.004; -.
PTM databases
PhosphoSite P25774; -.
Organism-specific databases
H-InvDB HIX0001035; -.
HGNC HGNC:2545; CTSS.
GenAtlas CTSS.
HPA CAB000460; -.
HPA002988; -.
MIM 116845; gene. [NCBI / EBI]
PharmGKB PA27041; -.
GeneCards P25774.
Gene expression databases
ArrayExpress P25774; -.
CleanEx HS_CTSS; -.
GermOnline ENSG00000163131; 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:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
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 P25774.
ProtoNet P25774.
Proteomic databases
PeptideAtlas P25774; -.
Genome annotation databases
Ensembl ENSG00000163131; Homo sapiens. [Contig view]
GeneID 1520; -.
KEGG hsa:1520; -.
Phylogenomic databases
HOGENOM P25774; -.
HOVERGEN P25774; -.
Other
BindingDB P25774; -.
NextBio 6291; -.
SOURCE CTSS; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Glycoprotein; Hydrolase; Lysosome; Polymorphism; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    16  16     Potential. 
PROPEP   17   114  98     Activation peptide. PRO_0000026313
CHAIN   115   331  217     Cathepsin S. PRO_0000026314
ACT_SITE   139   139        By similarity. 
ACT_SITE   278   278        By similarity. 
ACT_SITE   298   298        By similarity. 
CARBOHYD   104   104        N-linked (GlcNAc...) (Potential). 
DISULFID   126   224         
DISULFID   136   180         
DISULFID   170   213         
DISULFID   272   320         
VARIANT   113   113  1     R -> W (in dbSNP:rs2230061 [NCBI], dbSNP:rs10888390 [NCBI] and dbSNP:rs17357778 [NCBI]). VAR_025385 
VARIANT   161   161  1     S -> T (in dbSNP:rs1059604 [NCBI]). VAR_025386 [3D]
CONFLICT   92    92        M -> T (in Ref. 1 and 4). 
HELIX   121   124  4      
HELIX   139   156  18      
HELIX   164   170  7      
HELIX   173   175  3      
HELIX   185   195  11      
STRAND   198   200  3      
TURN   201   203  3      
HELIX   217   219  3      
STRAND   220   222  3      
STRAND   225   229  5      
HELIX   235   244  10      
STRAND   248   252  5      
HELIX   257   261  5      
STRAND   264   267  4      
STRAND   278   288  11      
STRAND   291   297  7      
STRAND   309   313  5      
STRAND   315   318  4      
HELIX   319   321  3      
TURN   322   324  3      
STRAND   327   330  4      
Sequence information
Length: 331 AA [This is the length of the unprocessed precursor] Molecular weight: 37496 Da [This is the MW of the unprocessed precursor] CRC64: 86093619DB6F0269 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM 

        70         80         90        100        110        120 
LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ WQRNITYKSN PNRILPDSVD 

       130        140        150        160        170        180 
WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC STEKYGNKGC 

       190        200        210        220        230        240 
NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE 

       250        260        270        280        290        300 
AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW 

       310        320        330 
GHNFGEEGYI RMARNKGNHC GIASFPSYPE I 

P25774 in FASTA format

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