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O46427 (CATH_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-cathepsin H
Gene names
Name:CTSH
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important for the overall degradation of proteins in lysosomes.

Catalytic activity

Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.

Subunit structure

Composed of cathepsin H and mini chain; disulfide-linked. Cathepsin H may be split into heavy and light chain. All chains are held together by disulfide bonds.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

bradykinin catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

dichotomous subdivision of terminal units involved in lung branching

Inferred from sequence or structural similarity. Source: UniProtKB

immune response-regulating signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

membrane protein proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

metanephros development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neuropeptide catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein destabilization

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

surfactant homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

zymogen activation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentalveolar lamellar body

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionHLA-A specific activating MHC class I receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

aminopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

serine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 9775 Potential
PRO_0000026218
Peptide98 – 1058Cathepsin H mini chain
PRO_0000026219
Propeptide107 – 1159
PRO_0000026220
Chain116 – 335220Cathepsin H
PRO_0000026221
Chain116 – 292177Cathepsin H heavy chain By similarity
PRO_0000026222
Chain293 – 33543Cathepsin H light chain By similarity
PRO_0000026223

Sites

Active site1411
Active site2811
Active site3011

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Disulfide bond102 ↔ 327
Disulfide bond138 ↔ 181
Disulfide bond172 ↔ 214
Disulfide bond272 ↔ 322

Secondary structure

.......................................... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O46427 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: F728EB45292C3B55

FASTA33537,455
        10         20         30         40         50         60 
MWAVLSLLCA GAWLLGPPAC GASNLAVSSF EKLHFKSWMV QHQKKYSLEE YHHRLQVFVS 

        70         80         90        100        110        120 
NWRKINAHNA GNHTFKLGLN QFSDMSFDEI RHKYLWSEPQ NCSATKGNYL RGTGPYPPSM 

       130        140        150        160        170        180 
DWRKKGNFVS PVKNQGSCGS CWTFSTTGAL ESAVAIATGK MLSLAEQQLV DCAQNFNNHG 

       190        200        210        220        230        240 
CQGGLPSQAF EYIRYNKGIM GEDTYPYKGQ DDHCKFQPDK AIAFVKDVAN ITMNDEEAMV 

       250        260        270        280        290        300 
EAVALYNPVS FAFEVTNDFL MYRKGIYSST SCHKTPDKVN HAVLAVGYGE ENGIPYWIVK 

       310        320        330 
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV 

« Hide

References

[1]"Crystal structure of porcine cathepsin H determined at 2.1-A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function."
Guncar G., Podobnik M., Pungercar J., Strukelj B., Turk V., Turk D.
Structure 6:51-61(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Tissue: Peripheral blood and Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001169 mRNA. Translation: AAB93957.1.
RefSeqNP_999094.1. NM_213929.2.
UniGeneSsc.3593.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NB3X-ray2.80A/B/C/D116-334[»]
P/R/S/T98-105[»]
1NB5X-ray2.40A/B/C/D116-334[»]
P/R/S/T98-105[»]
8PCHX-ray2.10A116-334[»]
P98-105[»]
ProteinModelPortalO46427.
SMRO46427. Positions 116-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000001934.

Protein family/group databases

MEROPSC01.040.

Proteomic databases

PaxDbO46427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000001983; ENSSSCP00000001934; ENSSSCG00000001770.
GeneID396969.
KEGGssc:396969.

Organism-specific databases

CTD1512.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00750000117440.
HOGENOMHOG000230774.
HOVERGENHBG011513.
KOK01366.
OMAHKYLWSE.
OrthoDBEOG70KGPX.
TreeFamTF328985.

Enzyme and pathway databases

SABIO-RKO46427.

Gene expression databases

ArrayExpressO46427.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO46427.

Entry information

Entry nameCATH_PIG
AccessionPrimary (citable) accession number: O46427
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references