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O46427

- CATH_PIG

UniProt

O46427 - CATH_PIG

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Protein
Pro-cathepsin H
Gene
CTSH
Organism
Sus scrofa (Pig)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411
Active sitei281 – 2811
Active sitei301 – 3011

GO - Molecular functioni

  1. HLA-A specific activating MHC class I receptor activity Source: UniProtKB
  2. aminopeptidase activity Source: UniProtKB
  3. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  4. cysteine-type endopeptidase activity Source: UniProtKB
  5. cysteine-type peptidase activity Source: UniProtKB
  6. endopeptidase activity Source: UniProtKB
  7. serine-type endopeptidase activity Source: UniProtKB
  8. thyroid hormone binding Source: UniProtKB

GO - Biological processi

  1. ERK1 and ERK2 cascade Source: UniProtKB
  2. T cell mediated cytotoxicity Source: UniProtKB
  3. bradykinin catabolic process Source: UniProtKB
  4. dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
  5. immune response-regulating signaling pathway Source: UniProtKB
  6. membrane protein proteolysis Source: UniProtKB
  7. metanephros development Source: UniProtKB
  8. negative regulation of apoptotic process Source: UniProtKB
  9. neuropeptide catabolic process Source: UniProtKB
  10. positive regulation of angiogenesis Source: UniProtKB
  11. positive regulation of apoptotic signaling pathway Source: Ensembl
  12. positive regulation of cell migration Source: UniProtKB
  13. positive regulation of cell proliferation Source: UniProtKB
  14. positive regulation of epithelial cell migration Source: UniProtKB
  15. positive regulation of gene expression Source: UniProtKB
  16. positive regulation of peptidase activity Source: UniProtKB
  17. protein destabilization Source: UniProtKB
  18. proteolysis Source: UniProtKB
  19. response to retinoic acid Source: UniProtKB
  20. surfactant homeostasis Source: UniProtKB
  21. zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

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
ProteomesiUP000008227: Chromosome 7

Subcellular locationi

GO - Cellular componenti

  1. alveolar lamellar body Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Propeptidei23 – 9775 Reviewed prediction
PRO_0000026218Add
BLAST
Peptidei98 – 1058Cathepsin H mini chain
PRO_0000026219
Propeptidei107 – 1159
PRO_0000026220
Chaini116 – 335220Cathepsin H
PRO_0000026221Add
BLAST
Chaini116 – 292177Cathepsin H heavy chain By similarity
PRO_0000026222Add
BLAST
Chaini293 – 33543Cathepsin H light chain By similarity
PRO_0000026223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi101 – 1011N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi102 ↔ 327
Disulfide bondi138 ↔ 181
Disulfide bondi172 ↔ 214
Glycosylationi230 – 2301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi272 ↔ 322

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO46427.

Expressioni

Gene expression databases

ArrayExpressiO46427.

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

STRINGi9823.ENSSSCP00000001934.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi122 – 1254
Helixi141 – 15818
Helixi166 – 1727
Helixi173 – 1764
Helixi180 – 1823
Helixi186 – 19611
Beta strandi199 – 2013
Turni202 – 2043
Helixi218 – 2203
Beta strandi221 – 2233
Beta strandi225 – 2306
Helixi236 – 24510
Beta strandi249 – 2535
Helixi257 – 2604
Beta strandi264 – 2674
Beta strandi270 – 2723
Turni276 – 2783
Beta strandi281 – 29111
Beta strandi294 – 3007
Beta strandi312 – 3165
Turni317 – 3204
Helixi321 – 3233
Beta strandi329 – 3335

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 116-335.

Miscellaneous databases

EvolutionaryTraceiO46427.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00750000117440.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
KOiK01366.
OMAiHKYLWSE.
OrthoDBiEOG70KGPX.
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

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MWAVLSLLCA GAWLLGPPAC GASNLAVSSF EKLHFKSWMV QHQKKYSLEE    50
YHHRLQVFVS NWRKINAHNA GNHTFKLGLN QFSDMSFDEI RHKYLWSEPQ 100
NCSATKGNYL RGTGPYPPSM DWRKKGNFVS PVKNQGSCGS CWTFSTTGAL 150
ESAVAIATGK MLSLAEQQLV DCAQNFNNHG CQGGLPSQAF EYIRYNKGIM 200
GEDTYPYKGQ DDHCKFQPDK AIAFVKDVAN ITMNDEEAMV EAVALYNPVS 250
FAFEVTNDFL MYRKGIYSST SCHKTPDKVN HAVLAVGYGE ENGIPYWIVK 300
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV 335
Length:335
Mass (Da):37,455
Last modified:June 1, 1998 - v1
Checksum:iF728EB45292C3B55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF001169 mRNA. Translation: AAB93957.1 .
RefSeqi NP_999094.1. NM_213929.2.
UniGenei Ssc.3593.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NB3 X-ray 2.80 A/B/C/D 116-334 [» ]
P/R/S/T 98-105 [» ]
1NB5 X-ray 2.40 A/B/C/D 116-334 [» ]
P/R/S/T 98-105 [» ]
8PCH X-ray 2.10 A 116-334 [» ]
P 98-105 [» ]
ProteinModelPortali O46427.
SMRi O46427. Positions 116-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000001934.

Protein family/group databases

MEROPSi C01.040.

Proteomic databases

PaxDbi O46427.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000001983 ; ENSSSCP00000001934 ; ENSSSCG00000001770 .
GeneIDi 396969.
KEGGi ssc:396969.

Organism-specific databases

CTDi 1512.

Phylogenomic databases

eggNOGi COG4870.
GeneTreei ENSGT00750000117440.
HOGENOMi HOG000230774.
HOVERGENi HBG011513.
KOi K01366.
OMAi HKYLWSE.
OrthoDBi EOG70KGPX.
TreeFami TF328985.

Enzyme and pathway databases

SABIO-RK O46427.

Miscellaneous databases

EvolutionaryTracei O46427.

Gene expression databases

ArrayExpressi O46427.

Family and domain databases

InterProi IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: July 9, 2014
This is version 96 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

External Data

Dasty 3

Similar proteinsi