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O46427

- CATH_PIG

UniProt

O46427 - CATH_PIG

Protein

Pro-cathepsin H

Gene

CTSH

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    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. aminopeptidase activity Source: UniProtKB
    2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    3. cysteine-type endopeptidase activity Source: UniProtKB
    4. cysteine-type peptidase activity Source: UniProtKB
    5. endopeptidase activity Source: UniProtKB
    6. HLA-A specific activating MHC class I receptor activity Source: UniProtKB
    7. serine-type endopeptidase activity Source: UniProtKB
    8. thyroid hormone binding Source: UniProtKB

    GO - Biological processi

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

    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

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 9775Sequence AnalysisPRO_0000026218Add
    BLAST
    Peptidei98 – 1058Cathepsin H mini chainPRO_0000026219
    Propeptidei107 – 1159PRO_0000026220
    Chaini116 – 335220Cathepsin HPRO_0000026221Add
    BLAST
    Chaini116 – 292177Cathepsin H heavy chainBy similarityPRO_0000026222Add
    BLAST
    Chaini293 – 33543Cathepsin H light chainBy similarityPRO_0000026223Add
    BLAST

    Amino acid modifications

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

    IntActiO46427. 2 interactions.
    STRINGi9823.ENSSSCP00000001934.

    Structurei

    Secondary structure

    1
    335
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO46427.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    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

    « Hide

    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

    IntActi O46427. 2 interactions.
    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: October 1, 2014
    This is version 97 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