LOCUS       NP_112647                563 aa            linear   ROD 31-MAR-2024
DEFINITION  tripeptidyl-peptidase 1 precursor [Rattus norvegicus].
ACCESSION   NP_112647
VERSION     NP_112647.2
DBSOURCE    REFSEQ: accession NM_031357.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Min,S., Kwon,S.M., Hong,J., Lee,Y.K., Park,T.J., Lim,S.B. and
            Yoon,G.
  TITLE     Mitoribosomal Deregulation Drives Senescence via TPP1-Mediated
            Telomere Deprotection
  JOURNAL   Cells 11 (13), 2079 (2022)
   PUBMED   35805162
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Shlevkov,E., Basu,H., Bray,M.A., Sun,Z., Wei,W., Apaydin,K.,
            Karhohs,K., Chen,P.F., Smith,J.L.M., Wiskow,O., Roet,K., Huang,X.,
            Eggan,K., Carpenter,A.E., Kleiman,R.J. and Schwarz,T.L.
  TITLE     A High-Content Screen Identifies TPP1 and Aurora B as Regulators of
            Axonal Mitochondrial Transport
  JOURNAL   Cell Rep 28 (12), 3224-3237 (2019)
   PUBMED   31533043
  REMARK    GeneRIF: A High-Content Screen Identifies TPP1 and Aurora B as
            Regulators of Axonal Mitochondrial Transport.
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Petrova,E.B., Dimitrova,M.B., Ivanov,I.P., Pavlova,V.G.,
            Dimitrova,S.G. and Kadiysky,D.S.
  TITLE     Effect of acute hypoxic shock on the rat brain morphology and
            tripeptidyl peptidase I activity
  JOURNAL   Acta Histochem 118 (5), 496-504 (2016)
   PUBMED   27263093
  REMARK    GeneRIF: TPPI activity was strictly regulated following hypoxic
            stress in the rat brain.
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Atanasova,D. and Lazarov,N.
  TITLE     Histochemical demonstration of tripeptidyl aminopeptidase I in the
            rat carotid body
  JOURNAL   Acta Histochem 117 (2), 219-222 (2015)
   PUBMED   25636608
  REMARK    GeneRIF: These findings also suggest that TPP I is involved in the
            general turnover of chemotransmitters between glomus cells and
            sensory nerve endings which emphasizes its importance for
            chemoreception under hypoxic conditions.
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Muslimov,I.A., Tuzhilin,A., Tang,T.H., Wong,R.K., Bianchi,R. and
            Tiedge,H.
  TITLE     Interactions of noncanonical motifs with hnRNP A2 promote
            activity-dependent RNA transport in neurons
  JOURNAL   J Cell Biol 205 (4), 493-510 (2014)
   PUBMED   24841565
  REMARK    GeneRIF: We describe a molecular mechanism in which inducible
            interactions of noncanonical RNA motif structures with targeting
            factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 form the
            basis for activity-dependent dendritic RNA targeting with CLN2.
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Vines,D.J. and Warburton,M.J.
  TITLE     Classical late infantile neuronal ceroid lipofuscinosis fibroblasts
            are deficient in lysosomal tripeptidyl peptidase I
  JOURNAL   FEBS Lett 443 (2), 131-135 (1999)
   PUBMED   9989590
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Vines,D. and Warburton,M.J.
  TITLE     Purification and characterisation of a tripeptidyl aminopeptidase I
            from rat spleen
  JOURNAL   Biochim Biophys Acta 1384 (2), 233-242 (1998)
   PUBMED   9659384
REFERENCE   8  (residues 1 to 563)
  AUTHORS   Sleat,D.E., Donnelly,R.J., Lackland,H., Liu,C.G., Sohar,I.,
            Pullarkat,R.K. and Lobel,P.
  TITLE     Association of mutations in a lysosomal protein with classical
            late-infantile neuronal ceroid lipofuscinosis
  JOURNAL   Science 277 (5333), 1802-1805 (1997)
   PUBMED   9295267
REFERENCE   9  (residues 1 to 563)
  AUTHORS   Page,A.E., Fuller,K., Chambers,T.J. and Warburton,M.J.
  TITLE     Purification and characterization of a tripeptidyl peptidase I from
            human osteoclastomas: evidence for its role in bone resorption
  JOURNAL   Arch Biochem Biophys 306 (2), 354-359 (1993)
   PUBMED   8215436
REFERENCE   10 (residues 1 to 563)
  AUTHORS   Maekawa,R., Yamada,J. and Nikaido,H.
  TITLE     Genetical studies of low plasma alkaline phosphatase (ALP) activity
            in the IS strain of rats
  JOURNAL   Jikken Dobutsu 31 (1), 13-19 (1982)
   PUBMED   6951716
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Nov 26, 2020 this sequence version replaced NP_112647.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB043870.1, BC081775.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..563
                     /product="tripeptidyl-peptidase 1 precursor"
                     /EC_number="3.4.14.9"
                     /note="TPP-1; TPP-I; tripeptidyl-peptidase I; tripeptidyl
                     aminopeptidase; ceroid-lipofuscinosis, neuronal 2"
                     /calculated_mol_wt=59357
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1975
     Region          34..173
                     /region_name="Pro-peptidase_S53"
                     /note="Activation domain of S53 peptidases; cd11377"
                     /db_xref="CDD:206778"
     Site            order(50,52..53,55,61..62,65,79..80,82,85,168..169,
                     171..172)
                     /site_type="other"
                     /note="peptidase domain interface [polypeptide binding]"
                     /db_xref="CDD:206778"
     mat_peptide     196..563
                     /product="Tripeptidyl-peptidase 1. /id=PRO_0000027385"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQV6.1)"
                     /calculated_mol_wt=39837
     Region          199..557
                     /region_name="Peptidases_S53"
                     /note="Peptidase domain in the S53 family; cd04056"
                     /db_xref="CDD:173788"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV6.1)"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV6.1)"
     Site            order(272,276,324..327,357,359..360,475)
                     /site_type="active"
                     /db_xref="CDD:173788"
     Site            order(272,276,475)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173788"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV6.1)"
     Site            313
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV6.1)"
     Site            443
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EQV6.1)"
     Site            order(517..518,539,543)
                     /site_type="other"
                     /note="calcium binding site [ion binding]"
                     /db_xref="CDD:173788"
     CDS             1..563
                     /gene="Tpp1"
                     /gene_synonym="Cln2"
                     /coded_by="NM_031357.2:6..1697"
                     /db_xref="GeneID:83534"
                     /db_xref="RGD:621296"
ORIGIN      
        1 mglqarflgl lalviagkct hspepdqrwm lppgwvslgr vdpeeelslt falkqqnldr
       61 lselvqavsd pssprygkyl tledvaelvq pspltlctvq kwllaagard chsvttqdfl
      121 tcwlsvrqae lllpgaefhr yvggpakthi irsphpyqlp qalaphvdfv aglhrfppls
      181 sprqrpepqg vgpvglhlgv tpsvlrqryn ltardvgsgt tnnsqacaqf leqyfhnsdl
      241 tefmrlfgss fahqasvarv vgkqgrgrag ieasldveyl msaganistw vysspgrhea
      301 qepflqwlll lsnesslphv htvsygdded slssvyiqrv ntefmkaaar gltllfasgd
      361 tgagcwsvsg rhkfrpsfpa sspyvttvgg tsfknpflvt nevvdyisgg gfsnvfpqps
      421 yqeeavaqfl kssshlppss yfnasgrayp dvaalsdgyw vvsnmvpipw vsgtsastpv
      481 fggilsline hrllngrppl gflnprlyqq hgaglfdvth gchesclnee vegqgfcsgp
      541 gwdpvtgwgt pnfpallktl lnp
//
