Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pro-cathepsin H

Gene

CTSH

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for the overall degradation of proteins in lysosomes.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1411
Active sitei2811
Active sitei3011

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

ReactomeiR-SSC-5683826. Surfactant metabolism.
R-SSC-6798695. Neutrophil degranulation.
SABIO-RKO46427.

Protein family/group databases

MEROPSiC01.040.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-cathepsin H
Cleaved into the following 4 chains:
Gene namesi
Name:CTSH
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000002621823 – 97Sequence analysisAdd BLAST75
PeptideiPRO_000002621998 – 105Cathepsin H mini chain8
PropeptideiPRO_0000026220107 – 1159
ChainiPRO_0000026221116 – 335Cathepsin HAdd BLAST220
ChainiPRO_0000026222116 – 292Cathepsin H heavy chainBy similarityAdd BLAST177
ChainiPRO_0000026223293 – 335Cathepsin H light chainBy similarityAdd BLAST43

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi72N-linked (GlcNAc...)Sequence analysis1
Glycosylationi101N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi102 ↔ 327
Disulfide bondi138 ↔ 181
Disulfide bondi172 ↔ 214
Glycosylationi230N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi272 ↔ 322

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO46427.
PeptideAtlasiO46427.
PRIDEiO46427.

Expressioni

Gene expression databases

BgeeiENSSSCG00000001770.
ExpressionAtlasiO46427. baseline.
GenevisibleiO46427. SS.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiO46427. 2 interactors.
STRINGi9823.ENSSSCP00000001934.

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi122 – 125Combined sources4
Helixi141 – 158Combined sources18
Helixi166 – 172Combined sources7
Helixi173 – 176Combined sources4
Helixi180 – 182Combined sources3
Helixi186 – 196Combined sources11
Beta strandi199 – 201Combined sources3
Turni202 – 204Combined sources3
Helixi218 – 220Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi225 – 230Combined sources6
Helixi236 – 245Combined sources10
Beta strandi249 – 253Combined sources5
Helixi257 – 260Combined sources4
Beta strandi264 – 267Combined sources4
Beta strandi270 – 272Combined sources3
Turni276 – 278Combined sources3
Beta strandi281 – 291Combined sources11
Beta strandi294 – 300Combined sources7
Beta strandi312 – 316Combined sources5
Turni317 – 320Combined sources4
Helixi321 – 323Combined sources3
Beta strandi329 – 333Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliO46427.
SMRiO46427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO46427.

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.
InParanoidiO46427.
KOiK01366.
OMAiYSTEEYH.
OrthoDBiEOG091G0AKT.
TreeFamiTF328985.

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.

O46427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWAVLSLLCA GAWLLGPPAC GASNLAVSSF EKLHFKSWMV QHQKKYSLEE
60 70 80 90 100
YHHRLQVFVS NWRKINAHNA GNHTFKLGLN QFSDMSFDEI RHKYLWSEPQ
110 120 130 140 150
NCSATKGNYL RGTGPYPPSM DWRKKGNFVS PVKNQGSCGS CWTFSTTGAL
160 170 180 190 200
ESAVAIATGK MLSLAEQQLV DCAQNFNNHG CQGGLPSQAF EYIRYNKGIM
210 220 230 240 250
GEDTYPYKGQ DDHCKFQPDK AIAFVKDVAN ITMNDEEAMV EAVALYNPVS
260 270 280 290 300
FAFEVTNDFL MYRKGIYSST SCHKTPDKVN HAVLAVGYGE ENGIPYWIVK
310 320 330
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV
Length:335
Mass (Da):37,455
Last modified:June 1, 1998 - v1
Checksum:iF728EB45292C3B55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001169 mRNA. Translation: AAB93957.1.
RefSeqiNP_999094.1. NM_213929.2.
UniGeneiSsc.3593.

Genome annotation databases

EnsembliENSSSCT00000001983; ENSSSCP00000001934; ENSSSCG00000001770.
GeneIDi396969.
KEGGissc:396969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001169 mRNA. Translation: AAB93957.1.
RefSeqiNP_999094.1. NM_213929.2.
UniGeneiSsc.3593.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliO46427.
SMRiO46427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO46427. 2 interactors.
STRINGi9823.ENSSSCP00000001934.

Protein family/group databases

MEROPSiC01.040.

Proteomic databases

PaxDbiO46427.
PeptideAtlasiO46427.
PRIDEiO46427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000001983; ENSSSCP00000001934; ENSSSCG00000001770.
GeneIDi396969.
KEGGissc:396969.

Organism-specific databases

CTDi1512.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiO46427.
KOiK01366.
OMAiYSTEEYH.
OrthoDBiEOG091G0AKT.
TreeFamiTF328985.

Enzyme and pathway databases

ReactomeiR-SSC-5683826. Surfactant metabolism.
R-SSC-6798695. Neutrophil degranulation.
SABIO-RKO46427.

Miscellaneous databases

EvolutionaryTraceiO46427.

Gene expression databases

BgeeiENSSSCG00000001770.
ExpressionAtlasiO46427. baseline.
GenevisibleiO46427. SS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiCATH_PIG
AccessioniPrimary (citable) accession number: O46427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 114 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.