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Protein

Cathepsin K

Gene

CTSK

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.

Catalytic activityi

Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391By similarity
Active sitei276 – 2761By similarity
Active sitei296 – 2961By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiI29.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin K (EC:3.4.22.38)
Alternative name(s):
Protein OC-2
Gene namesi
Name:CTSK
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3349.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence analysisAdd
BLAST
Propeptidei16 – 11499Activation peptidePRO_0000026305Add
BLAST
Chaini115 – 329215Cathepsin KPRO_0000026306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi136 ↔ 1771 Publication
Disulfide bondi170 ↔ 2101 Publication
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi269 ↔ 3181 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Predominantly expressed in osteclasts (bones).

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009540.

Chemistry

BindingDBiP43236.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi121 – 1244Combined sources
Helixi139 – 15618Combined sources
Helixi164 – 1707Combined sources
Helixi176 – 1783Combined sources
Helixi182 – 19211Combined sources
Beta strandi195 – 1973Combined sources
Helixi198 – 2003Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi224 – 2263Combined sources
Helixi232 – 24110Combined sources
Beta strandi245 – 2495Combined sources
Helixi254 – 2574Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi276 – 28611Combined sources
Beta strandi289 – 2957Combined sources
Beta strandi307 – 31610Combined sources
Helixi317 – 3193Combined sources
Beta strandi325 – 3273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F7DX-ray1.90A115-329[»]
ProteinModelPortaliP43236.
SMRiP43236. Positions 16-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43236.

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.
InParanoidiP43236.
KOiK01371.
OMAiKHISIHN.
OrthoDBiEOG786H3P.
TreeFamiTF313739.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015644. Peptidase_C1A_cathepsin-K.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF55. PTHR12411:SF55. 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.

P43236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWGLKVLLLP VVSFALHPEE ILDTQWELWK KTYSKQYNSK VDEISRRLIW
60 70 80 90 100
EKNLKHISIH NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPPSRS
110 120 130 140 150
HSNDTLYIPD WEGRTPDSID YRKKGYVTPV KNQGQCGSCW AFSSVGALEG
160 170 180 190 200
QLKKKTGKLL NLSPQNLVDC VSENYGCGGG YMTNAFQYVQ RNRGIDSEDA
210 220 230 240 250
YPYVGQDESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA RVGPVSVAID
260 270 280 290 300
ASLTSFQFYS KGVYYDENCS SDNVNHAVLA VGYGIQKGNK HWIIKNSWGE
310 320
SWGNKGYILM ARNKNNACGI ANLASFPKM
Length:329
Mass (Da):36,870
Last modified:November 1, 1995 - v1
Checksum:i875D8582876EB51F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14036 mRNA. Translation: BAA03125.1.
PIRiA49868.
RefSeqiNP_001076110.1. NM_001082641.1.
UniGeneiOcu.6195.

Genome annotation databases

EnsembliENSOCUT00000011087; ENSOCUP00000009540; ENSOCUG00000011090.
GeneIDi100009334.
KEGGiocu:100009334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14036 mRNA. Translation: BAA03125.1.
PIRiA49868.
RefSeqiNP_001076110.1. NM_001082641.1.
UniGeneiOcu.6195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F7DX-ray1.90A115-329[»]
ProteinModelPortaliP43236.
SMRiP43236. Positions 16-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009540.

Chemistry

BindingDBiP43236.
ChEMBLiCHEMBL3349.

Protein family/group databases

MEROPSiI29.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000011087; ENSOCUP00000009540; ENSOCUG00000011090.
GeneIDi100009334.
KEGGiocu:100009334.

Organism-specific databases

CTDi1513.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP43236.
KOiK01371.
OMAiKHISIHN.
OrthoDBiEOG786H3P.
TreeFamiTF313739.

Miscellaneous databases

EvolutionaryTraceiP43236.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015644. Peptidase_C1A_cathepsin-K.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF55. PTHR12411:SF55. 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...

Publicationsi

  1. "Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts."
    Tezuka K., Tezuka Y., Maejima A., Sato T., Nemoto K., Kamioka H., Hakeda Y., Kumegawa M.
    J. Biol. Chem. 269:1106-1109(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone.
  2. "Beta-substituted cyclohexanecarboxamide: a nonpeptidic framework for the design of potent inhibitors of cathepsin K."
    Crane S.N., Black W.C., Palmer J.T., Davis D.E., Setti E., Robichaud J., Paquet J., Oballa R.M., Bayly C.I., McKay D.J., Somoza J.R., Chauret N., Seto C., Scheigetz J., Wesolowski G., Masse F., Desmarais S., Ouellet M.
    J. Med. Chem. 49:1066-1079(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-329 IN COMPLEX WITH INHIBITORS, DISULFIDE BONDS.

Entry informationi

Entry nameiCATK_RABIT
AccessioniPrimary (citable) accession number: P43236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.