LOCUS       NP_112399               1249 aa            linear   ROD 31-MAR-2024
DEFINITION  tripeptidyl-peptidase 2 [Rattus norvegicus].
ACCESSION   NP_112399 XP_003750741
VERSION     NP_112399.1
DBSOURCE    REFSEQ: accession NM_031137.2
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 1249)
  AUTHORS   Pashevin,D.O., Honcharov,S.V., Tumanovs'ka,L.V., Dosenko,V.Ie. and
            Moibenko,O.O.
  TITLE     [The changes in the activity of tripeptidyl peptidase II in
            experimental atherosclerosis and hypertension]
  JOURNAL   Fiziol Zh (1994) 60 (3), 27-31 (2014)
   PUBMED   25095668
  REMARK    GeneRIF: Changes in the activity of TPP II play an important role
            in the pathogenesis of blood vessels wall in atherosclerosis and
            arterial hypertension.
REFERENCE   2  (residues 1 to 1249)
  AUTHORS   Schonegge,A.M., Villa,E., Forster,F., Hegerl,R., Peters,J.,
            Baumeister,W. and Rockel,B.
  TITLE     The structure of human tripeptidyl peptidase II as determined by a
            hybrid approach
  JOURNAL   Structure 20 (4), 593-603 (2012)
   PUBMED   22483107
REFERENCE   3  (residues 1 to 1249)
  AUTHORS   Wray,C.J., Tomkinson,B., Robb,B.W. and Hasselgren,P.O.
  TITLE     Tripeptidyl-peptidase II expression and activity are increased in
            skeletal muscle during sepsis
  JOURNAL   Biochem Biophys Res Commun 296 (1), 41-47 (2002)
   PUBMED   12147224
  REMARK    GeneRIF: increase of expression and activity in skeletal muscle
            during sepsis
REFERENCE   4  (residues 1 to 1249)
  AUTHORS   Stoltze,L., Schirle,M., Schwarz,G., Schroter,C., Thompson,M.W.,
            Hersh,L.B., Kalbacher,H., Stevanovic,S., Rammensee,H.G. and
            Schild,H.
  TITLE     Two new proteases in the MHC class I processing pathway
  JOURNAL   Nat Immunol 1 (5), 413-418 (2000)
   PUBMED   11062501
REFERENCE   5  (residues 1 to 1249)
  AUTHORS   Beninga,J., Rock,K.L. and Goldberg,A.L.
  TITLE     Interferon-gamma can stimulate post-proteasomal trimming of the N
            terminus of an antigenic peptide by inducing leucine aminopeptidase
  JOURNAL   J Biol Chem 273 (30), 18734-18742 (1998)
   PUBMED   9668046
REFERENCE   6  (residues 1 to 1249)
  AUTHORS   Rose,C., Vargas,F., Facchinetti,P., Bourgeat,P., Bambal,R.B.,
            Bishop,P.B., Chan,S.M., Moore,A.N., Ganellin,C.R. and Schwartz,J.C.
  TITLE     Characterization and inhibition of a cholecystokinin-inactivating
            serine peptidase
  JOURNAL   Nature 380 (6573), 403-409 (1996)
   PUBMED   8602240
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jun 26, 2012 this sequence version replaced XP_003750741.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U50194.1, SRR26360172.1303098.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1249
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..1249
                     /product="tripeptidyl-peptidase 2"
                     /EC_number="3.4.14.10"
                     /note="TPP-II; tripeptidyl-peptidase II; tripeptidyl
                     aminopeptidase"
                     /calculated_mol_wt=138162
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P29144; propagated from
                     UniProtKB/Swiss-Prot (Q64560.3)"
     Region          14..489
                     /region_name="Peptidases_S8_Tripeptidyl_Aminopeptidase_II"
                     /note="Peptidase S8 family domain in Tripeptidyl
                     aminopeptidases_II; cd04857"
                     /db_xref="CDD:173796"
     Site            order(44,264,449)
                     /site_type="active"
                     /note="putative catalytic triad [active]"
                     /db_xref="CDD:173796"
     Site            order(190,264,328..330,362,449)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173796"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q64514; propagated from
                     UniProtKB/Swiss-Prot (Q64560.3)"
     Region          777..963
                     /region_name="TPPII"
                     /note="Tripeptidyl peptidase II; pfam12580"
                     /db_xref="CDD:463636"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29144; propagated from
                     UniProtKB/Swiss-Prot (Q64560.3)"
     Region          998..1018
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64560.3)"
     CDS             1..1249
                     /gene="Tpp2"
                     /gene_synonym="TPP-2"
                     /coded_by="NM_031137.2:14..3763"
                     /db_xref="GeneID:81815"
                     /db_xref="RGD:621584"
ORIGIN      
        1 mataateepf pfhgllpkke tgassflcry peydgrgvli avldtgvdpg apgmqvttdg
       61 kpkiidiidt tgsgdvntat evepkdgeit glsgrvlkip anwtnpsgky higikngydf
      121 ypkalkeriq kerkekiwdp ihrvalaeac rkqeefdian ngssqankli keelqsqvel
      181 lnsfekkysd pgpvydclvw hdgetwracv dsnengdlgk stvlrnykea qeygsfgtae
      241 mlnysvniyd dgnllsivts ggahgthvas iaaghfpeep erngvapgaq ilsikigdtr
      301 lstmetgtgl iramievinh kcdlvnysyg eathwpnsgr icevineavw khntiyvssa
      361 gnngpclstv gcpggttssv igvgayvspd mmvaeyslre klpanqytws srgpsadgal
      421 gvsisapgga iasvpnwtlr gtqlmngtsm sspnacggia lvlsglkann vdytvhsvrr
      481 alentaikad nievfaqghg iiqvdkaydy liqntsfanr lgftvtvgnn rgiylrdpvq
      541 vaapsdhgvg iepvfpente nsekisfqlh laltsnsswv qcpshlelmn qcrhinirvd
      601 prglreglhy tevcgydias pnagplfrvp itaviaakvn esshydlaft dvhfkpgqir
      661 rhfvevpega twaevtvcsc ssevsakfvl havqlvkqra yrshefykfc slpekgtlie
      721 afpvlggkai efciarwwas lsdvnidyti sfhgivctap qlnihasegi nrfdvqsslk
      781 yedlapcitl kswvqtlrpv naktrplgsr dvlpnnrqly emvltysfhq pksgevtpsc
      841 pllcellyes efdsqlwiif dqnkrqmgsg dayphqyslk lekgdytirl qirheqisdl
      901 drlkdlpfiv shrlsntlsl dihenhslal lgkkkssslt lppkynqpff vtslpddkip
      961 kgagpgcyla gsltlsktel gkkadvipvh yylippptkt kngskdkekd sekekdlkee
     1021 ftealrdlki qwmtkldstd iynelketyp aylplyvarl hqldaekerm krlneivdaa
     1081 navishidqt alavyiamkt dprpdaatik ndmdkqkstl vdalcrkgca ladhllhaqp
     1141 hdgaaagdae akeeegestl eslsetywet tkwtdlfdtk vltfaykhal vnkmygrglk
     1201 fatklveekp tkenwknciq lmkllgwthc asftenwlpi myppdycvf
//
