LOCUS       NP_114179                500 aa            linear   ROD 03-APR-2024
DEFINITION  dipeptidyl peptidase 2 precursor [Rattus norvegicus].
ACCESSION   NP_114179
VERSION     NP_114179.1
DBSOURCE    REFSEQ: accession NM_031973.1
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 500)
  AUTHORS   Danyukova,T., Ariunbat,K., Thelen,M., Brocke-Ahmadinejad,N.,
            Mole,S.E. and Storch,S.
  TITLE     Loss of CLN7 results in depletion of soluble lysosomal proteins and
            impaired mTOR reactivation
  JOURNAL   Hum Mol Genet 27 (10), 1711-1722 (2018)
   PUBMED   29514215
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Araki,H., Li,Y., Yamamoto,Y., Haneda,M., Nishi,K., Kikkawa,R. and
            Ohkubo,I.
  TITLE     Purification, molecular cloning, and immunohistochemical
            localization of dipeptidyl peptidase II from the rat kidney and its
            identity with quiescent cell proline dipeptidase
  JOURNAL   J Biochem 129 (2), 279-288 (2001)
   PUBMED   11173530
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Fukasawa,K.M., Fukasawa,K., Higaki,K., Shiina,N., Ohno,M., Ito,S.,
            Otogoto,J. and Ota,N.
  TITLE     Cloning and functional expression of rat kidney dipeptidyl
            peptidase II
  JOURNAL   Biochem J 353 (Pt 2), 283-290 (2001)
   PUBMED   11139392
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Chiravuri,M., Agarraberes,F., Mathieu,S.L., Lee,H. and Huber,B.T.
  TITLE     Vesicular localization and characterization of a novel
            post-proline-cleaving aminodipeptidase, quiescent cell proline
            dipeptidase
  JOURNAL   J Immunol 165 (10), 5695-5702 (2000)
   PUBMED   11067927
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB048711.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB048711.1, AB038232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN16093045
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..500
                     /product="dipeptidyl peptidase 2 precursor"
                     /EC_number="3.4.14.2"
                     /note="dipeptidyl peptidase 2; DPP II; dipeptidyl
                     aminopeptidase II; quiescent cell proline dipeptidase;
                     dipeptidyl peptidase II"
                     /calculated_mol_wt=51704
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3429
     mat_peptide     37..500
                     /product="Dipeptidyl peptidase 2. /id=PRO_0000027319"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPB1.1)"
                     /calculated_mol_wt=51402
     Region          48..475
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPB1.1)"
     Site            96
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPB1.1)"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPB1.1)"
     Site            366
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPB1.1)"
     Site            373
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPB1.1)"
     Site            438
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPB1.1)"
     CDS             1..500
                     /gene="Dpp7"
                     /gene_synonym="Dpp2"
                     /coded_by="NM_031973.1:33..1535"
                     /db_xref="GeneID:83799"
                     /db_xref="RGD:71073"
ORIGIN      
        1 mglhpcspvd hgvpswvlvl lltlglcslq atadsvldpd frenyfeqym dhfnfesfsn
       61 ktfgqrflvs dkfwkmgegp iffytgnegd iwslannsgf ivelaaqqea llvfaehryy
      121 gkslpfgvqs tqrgytqllt veqaladfav llqalrhnlg vqdaptiafg gsyggmlsay
      181 mrmkyphlva galaasapvi avaglgnpdq ffrdvtadfy gqspkcaqav rdafqqikdl
      241 flqgaydtis qnfgtcqsls spkdltqlfg farnaftvla mmdypyptnf lgplpanpvk
      301 vgcerllseg qrimglrala glvynssgme pcfdiyqmyq scadptgcgt gsnarawdyq
      361 acteinltfd snnvtdmfpe ipfsdelrqq ycldtwgvwp rpdwlqtsfw ggdlkaasni
      421 ifsngdldpw agggiqrnls tsiiavtiqg gahhldlras nsedppsvve vrkleatlir
      481 ewvaaarlkq paeaqwpgpk
//
