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O97578

- CATC_CANFA

UniProt

O97578 - CATC_CANFA

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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

Functioni

Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase 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 – 2311 By similarity
Binding sitei275 – 2751Chloride By similarity
Binding sitei277 – 2771Chloride; via amide nitrogen By similarity
Binding sitei319 – 3191Chloride By similarity
Active sitei377 – 3771 By similarity
Active sitei399 – 3991 By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 109109Dipeptidyl peptidase 1 exclusion domain chain By similarityPRO_0000026331Add
BLAST
Propeptidei110 – 19990 By 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 ↔ 93 By similarity
Glycosylationi28 – 281N-linked (GlcNAc...) By similarity
Disulfide bondi29 ↔ 111 By similarity
Glycosylationi94 – 941N-linked (GlcNAc...) By similarity
Disulfide bondi228 ↔ 271 By similarity
Glycosylationi249 – 2491N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi264 ↔ 304 By similarity
Disulfide bondi294 ↔ 309 By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

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

Non-terminal residue

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: May 14, 2014
This is version 89 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

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