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O97578

- CATC_CANFA

UniProt

O97578 - CATC_CANFA

Protein

Dipeptidyl peptidase 1

Gene

CTSC

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase By similarity.By similarity

    Catalytic activityi

    Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.

    Cofactori

    Binds 1 chloride ion per heavy chain.By similarity

    pH dependencei

    Optimum pH is 6.5. Active over a broad pH range.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei231 – 2311By similarity
    Binding sitei275 – 2751ChlorideBy similarity
    Binding sitei277 – 2771Chloride; via amide nitrogenBy similarity
    Binding sitei319 – 3191ChlorideBy similarity
    Active sitei377 – 3771By similarity
    Active sitei399 – 3991By similarity

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Chloride

    Protein family/group databases

    MEROPSiC01.070.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 1 (EC:3.4.14.1)
    Alternative name(s):
    Cathepsin C
    Cathepsin J
    Dipeptidyl peptidase I
    Short name:
    DPP-I
    Short name:
    DPPI
    Dipeptidyl transferase
    Cleaved into the following 6 chains:
    Alternative name(s):
    Dipeptidyl peptidase I exclusion domain chain
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 1
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 2
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 3
    Alternative name(s):
    Dipeptidyl peptidase I heavy chain 4
    Alternative name(s):
    Dipeptidyl peptidase I light chain
    Gene namesi
    Name:CTSC
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 109109Dipeptidyl peptidase 1 exclusion domain chainBy similarityPRO_0000026331Add
    BLAST
    Propeptidei110 – 19990By similarityPRO_0000026332Add
    BLAST
    Chaini200 – 366167Dipeptidyl peptidase 1 heavy chain 1PRO_0000026333Add
    BLAST
    Chaini201 – 366166Dipeptidyl peptidase 1 heavy chain 2PRO_0000026334Add
    BLAST
    Chaini203 – 366164Dipeptidyl peptidase 1 heavy chain 3PRO_0000026335Add
    BLAST
    Chaini204 – 366163Dipeptidyl peptidase 1 heavy chain 4PRO_0000026336Add
    BLAST
    Chaini367 – 43569Dipeptidyl peptidase 1 light chainPRO_0000026337Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi5 – 51N-linked (GlcNAc...)By similarity
    Disulfide bondi6 ↔ 93By similarity
    Glycosylationi28 – 281N-linked (GlcNAc...)By similarity
    Disulfide bondi29 ↔ 111By similarity
    Glycosylationi94 – 941N-linked (GlcNAc...)By similarity
    Disulfide bondi228 ↔ 271By similarity
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi264 ↔ 304By similarity
    Disulfide bondi294 ↔ 309By similarity

    Post-translational modificationi

    The N-terminus of the heavy chain is heterogeneously processed to produce four different chains.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiO97578.
    PRIDEiO97578.

    Interactioni

    Subunit structurei

    Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000006531.

    Structurei

    3D structure databases

    ProteinModelPortaliO97578.
    SMRiO97578. Positions 1-118.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000068022.
    HOVERGENiHBG005248.
    InParanoidiO97578.
    KOiK01275.

    Family and domain databases

    Gene3Di2.40.128.80. 1 hit.
    InterProiIPR014882. CathepsinC_exc.
    IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08773. CathepsinC_exc. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. Pept_C1. 1 hit.
    [Graphical view]
    SUPFAMiSSF75001. SSF75001. 1 hit.
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O97578-1 [UniParc]FASTAAdd to Basket

    « Hide

    DTPANCTHPE LLGTWVFQVG PAGSRSVNCS VMGPPEKKVV VHLEKLDTAY    50
    DNFGNTGHFT IIYNQGFEIV LNDYKWFAFF KYKEEGHKVT SYCNETMTGW 100
    VHDVLGRNWA CFTGTKMGTT SEKAKVNTKH IERLQENNSN RLYKYNYEFV 150
    KAINTIQKSW TATRYIEYET LTLRDMMTRV GGRKIPRPKP TPLTAEIHEE 200
    ISRLPTSWDW RNVRGTNFVS PVRNQASCGS CYAFASTAML EARIRILTNN 250
    TQTPILSPQE IVSCSQYAQG CEGGFPYLIA GKYAQDFGLV EEACFPYAGS 300
    DSPCKPNDCF RYYSSEYYYV GGFYGACNEA LMKLELVRHG PMAVAFEVYD 350
    DFFHYQKGIY YHTGLRDPFN PFELTNHAVL LVGYGTDSAS GMDYWIVKNS 400
    WGSRWGEDGY FRIRRGTDEC AIESIAVAAT PIPKL 435
    Length:435
    Mass (Da):49,412
    Last modified:May 1, 1999 - v1
    Checksum:iA80BC7C68CAB0727
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060171 mRNA. Translation: AAD02704.1.
    RefSeqiNP_001182763.1. NM_001195834.1.
    UniGeneiCfa.28653.

    Genome annotation databases

    GeneIDi403458.
    KEGGicfa:403458.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060171 mRNA. Translation: AAD02704.1 .
    RefSeqi NP_001182763.1. NM_001195834.1.
    UniGenei Cfa.28653.

    3D structure databases

    ProteinModelPortali O97578.
    SMRi O97578. Positions 1-118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000006531.

    Protein family/group databases

    MEROPSi C01.070.

    Proteomic databases

    PaxDbi O97578.
    PRIDEi O97578.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403458.
    KEGGi cfa:403458.

    Organism-specific databases

    CTDi 1075.

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000068022.
    HOVERGENi HBG005248.
    InParanoidi O97578.
    KOi K01275.

    Miscellaneous databases

    NextBioi 20816976.

    Family and domain databases

    Gene3Di 2.40.128.80. 1 hit.
    InterProi IPR014882. CathepsinC_exc.
    IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08773. CathepsinC_exc. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF75001. SSF75001. 1 hit.
    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. "Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I."
      Wolters P.J., Raymond W.W., Blount J.L., Caughey G.H.
      J. Biol. Chem. 273:15514-15520(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-8 AND 199-208.
      Tissue: Mast cell.

    Entry informationi

    Entry nameiCATC_CANFA
    AccessioniPrimary (citable) accession number: O97578
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 90 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3