TPP1_CANLF
ID TPP1_CANLF Reviewed; 563 AA.
AC Q9XSB8; Q45VT9;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Tripeptidyl-peptidase 1;
DE Short=TPP-1;
DE EC=3.4.14.9;
DE AltName: Full=Lysosomal pepstatin-insensitive protease;
DE Short=LPIC;
DE AltName: Full=Tripeptidyl aminopeptidase;
DE AltName: Full=Tripeptidyl-peptidase I;
DE Short=TPP-I;
DE Flags: Precursor;
GN Name=TPP1; Synonyms=CLN2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu P.-C., Katz M.L., Siakotos A.N., Grob S.E., Johnson G.S.;
RT "Coding sequence and exon/intron organization of the canine CLN2 gene and
RT its exclusion as the locus for ceroid lipofuscinosis in English setter
RT dogs.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-427.
RC STRAIN=Tibetan terrier;
RX PubMed=15771740; DOI=10.1111/j.1365-2052.2005.01254.x;
RA Droegemueller C., Woehlke A., Distl O.;
RT "Evaluation of the canine TPP1 gene as a candidate for neuronal ceroid
RT lipofuscinosis in Tibetan terrier and Polish Owczarek Nizinny dogs.";
RL Anim. Genet. 36:178-179(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-427.
RC STRAIN=Tibetan terrier;
RA Sanders D.N., Katz M.L., Johnson G.S.;
RT "Coding sequence and exon/intron organization of the canine TTP-1 gene and
RT exclusion of TPP-1 mutations as the cause of hereditary ceroid
RT lipofuscinosis in English Setter and Tibetan Terrier dogs.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I
CC activity. May act as a non-specific lysosomal peptidase which generates
CC tripeptides from the breakdown products produced by lysosomal
CC proteinases. Requires substrates with an unsubstituted N-terminus (By
CC similarity). {ECO:0000250|UniProtKB:Q9EQV6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide, but
CC also has endopeptidase activity.; EC=3.4.14.9;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:O14773};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O14773};
CC -!- SUBUNIT: Monomer. Interacts with CLN5. Interacts with CLN3 (By
CC similarity). {ECO:0000250|UniProtKB:O14773}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O14773}.
CC Melanosome {ECO:0000250|UniProtKB:O14773}.
CC -!- PTM: Activated by autocatalytic proteolytical processing upon
CC acidification. N-glycosylation is required for processing and activity
CC (By similarity). {ECO:0000250|UniProtKB:O14773}.
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DR EMBL; AF114167; AAD25043.1; -; Genomic_DNA.
DR EMBL; DQ100344; AAZ38727.1; -; Genomic_DNA.
DR RefSeq; NP_001013869.1; NM_001013847.1.
DR AlphaFoldDB; Q9XSB8; -.
DR SMR; Q9XSB8; -.
DR STRING; 9615.ENSCAFP00000009732; -.
DR MEROPS; S53.003; -.
DR PaxDb; Q9XSB8; -.
DR PRIDE; Q9XSB8; -.
DR GeneID; 485337; -.
DR KEGG; cfa:485337; -.
DR CTD; 1200; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR InParanoid; Q9XSB8; -.
DR OrthoDB; 1294880at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0035727; F:lysophosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; ISS:UniProtKB.
DR GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Metal-binding; Protease; Reference proteome; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT PROPEP 20..195
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT /id="PRO_0000027372"
FT CHAIN 196..563
FT /note="Tripeptidyl-peptidase 1"
FT /id="PRO_0000027373"
FT DOMAIN 199..563
FT /note="Peptidase S53"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT ACT_SITE 475
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..122
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT DISULFID 365..526
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT DISULFID 522..537
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT VARIANT 427
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:15771740, ECO:0000269|Ref.3"
SQ SEQUENCE 563 AA; 61362 MW; 21465A44C34934F4 CRC64;
MRLRTCLLGL LALCVASKCS YSPEPDQQRT LPPGWVSLGR VDSEEELSLT FALRQQNVER
LSKLVQAVSD PGSPHYGKYL TLEDVAELVR PSPLTFRTVQ KWLSAAGARN CHSVTTQDFL
TCWLSVRQAE LLLSGAEFHR YVGGPTEIHV IRSLRPYQLP KALAPHVDFV GGLHRFPPTS
SLRQRPEPQV SGTVGLHLGV TPSVIRQRYN LTAQDVGSGT TNNSQACAQF LEQYFHASDL
AEFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHES
QEPFLQWLLL LSNESALPHV HTVSYGDDED SLSSAYIQRV NTEFMKAAAR GLTLLFASGD
SGAGCWSVSR RHQFRPSFPA SSPYVTTVGG TSFQNPFRVT TEIVDYISGG GFSNVFPQPS
YQEEAVVQFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNSVPIPW VSGTSASTPV
FGGILSLINE HRLLSGLPPL GFLNPRLYQQ RGAGLFDVTR GCHESCLNEE VQGQGFCSGP
GWDPVTGWGT PNFPALLKAL IKP
