LOCUS       NP_036921                767 aa            linear   ROD 30-MAR-2024
DEFINITION  dipeptidyl peptidase 4 [Rattus norvegicus].
ACCESSION   NP_036921
VERSION     NP_036921.2
DBSOURCE    REFSEQ: accession NM_012789.2
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 767)
  AUTHORS   Lin,L. and Wang,L.
  TITLE     Knockdown of DPP4 promotes the proliferation and the activation of
            the CREB/aromatase pathway in ovarian granulosa cells
  JOURNAL   Mol Med Rep 25 (2) (2022)
   PUBMED   35014677
  REMARK    GeneRIF: Knockdown of DPP4 promotes the proliferation and the
            activation of the CREB/aromatase pathway in ovarian granulosa
            cells.
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Zhao,R., Jin,X., Li,A., Xu,B., Shen,Y., Wang,W., Huang,J., Zhang,Y.
            and Li,X.
  TITLE     Precise Diabetic Wound Therapy: PLS Nanospheres Eliminate Senescent
            Cells via DPP4 Targeting and PARP1 Activation
  JOURNAL   Adv Sci (Weinh) 9 (1), e2104128 (2022)
   PUBMED   34738744
  REMARK    GeneRIF: Precise Diabetic Wound Therapy: PLS Nanospheres Eliminate
            Senescent Cells via DPP4 Targeting and PARP1 Activation.
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Adegoke,T.E., Sabinari,I.W., Areola,E.D., Ajao,F., Asafa,O.O.,
            Soluoku,T.K., Bello,A., Adesanmi,A.M., Yusuf,S.O., Omoleye,A.,
            Ayinla,M.T. and Olatunji,L.A.
  TITLE     Inhibition of dipeptidyl peptidase-4 averts free fatty acids
            deposition in the hearts of oral estrogen-progestin
            contraceptive-induced hyperinsulinemic female rats
  JOURNAL   Can J Physiol Pharmacol 99 (12), 1316-1323 (2021)
   PUBMED   34310895
  REMARK    GeneRIF: Inhibition of dipeptidyl peptidase-4 averts free fatty
            acids deposition in the hearts of oral estrogen-progestin
            contraceptive-induced hyperinsulinemic female rats.
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Guan,G.Y., Wei,N., Song,T., Zhao,C., Sun,Y., Pan,R.X., Zhang,L.L.,
            Xu,Y.Y., Dai,Y.M. and Han,H.
  TITLE     miR-448-3p alleviates diabetic vascular dysfunction by inhibiting
            endothelial-mesenchymal transition through DPP-4 dysregulation
  JOURNAL   J Cell Physiol 235 (12), 10024-10036 (2020)
   PUBMED   32542696
  REMARK    GeneRIF: miR-448-3p alleviates diabetic vascular dysfunction by
            inhibiting endothelial-mesenchymal transition through DPP-4
            dysregulation.
REFERENCE   5  (residues 1 to 767)
  AUTHORS   Yip,H.K., Lee,M.S., Li,Y.C., Shao,P.L., Chiang,J.Y., Sung,P.H.,
            Yang,C.H. and Chen,K.H.
  TITLE     Dipeptidyl Peptidase-4 deficiency effectively protects the brain
            and neurological function in rodent after acute Hemorrhagic Stroke
  JOURNAL   Int J Biol Sci 16 (16), 3116-3132 (2020)
   PUBMED   33162819
  REMARK    GeneRIF: Dipeptidyl Peptidase-4 deficiency effectively protects the
            brain and neurological function in rodent after acute Hemorrhagic
            Stroke.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Ogata,S., Misumi,Y., Tsuji,E., Takami,N., Oda,K. and Ikehara,Y.
  TITLE     Identification of the active site residues in dipeptidyl peptidase
            IV by affinity labeling and site-directed mutagenesis
  JOURNAL   Biochemistry 31 (9), 2582-2587 (1992)
   PUBMED   1347701
REFERENCE   7  (residues 1 to 767)
  AUTHORS   Hong,W.J. and Doyle,D.
  TITLE     Molecular dissection of the NH2-terminal signal/anchor sequence of
            rat dipeptidyl peptidase IV
  JOURNAL   J Cell Biol 111 (2), 323-328 (1990)
   PUBMED   1974258
REFERENCE   8  (residues 1 to 767)
  AUTHORS   McCaughan,G.W., Wickson,J.E., Creswick,P.F. and Gorrell,M.D.
  TITLE     Identification of the bile canalicular cell surface molecule GP110
            as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue
            distribution, purification and N-terminal amino acid sequence
  JOURNAL   Hepatology 11 (4), 534-544 (1990)
   PUBMED   1970322
REFERENCE   9  (residues 1 to 767)
  AUTHORS   Ogata,S., Misumi,Y. and Ikehara,Y.
  TITLE     Primary structure of rat liver dipeptidyl peptidase IV deduced from
            its cDNA and identification of the NH2-terminal signal sequence as
            the membrane-anchoring domain
  JOURNAL   J Biol Chem 264 (6), 3596-3601 (1989)
   PUBMED   2563382
REFERENCE   10 (residues 1 to 767)
  AUTHORS   Hong,W.J. and Doyle,D.
  TITLE     Membrane orientation of rat gp110 as studied by in vitro
            translation
  JOURNAL   J Biol Chem 263 (32), 16892-16898 (1988)
   PUBMED   3182821
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Mar 11, 2021 this sequence version replaced NP_036921.1.
            
            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 :: J02997.1, SRR26360190.3189808.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMN16676784 [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..767
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..767
                     /product="dipeptidyl peptidase 4"
                     /EC_number="3.4.14.5"
                     /note="DPP IV; GP110 glycoprotein; dipeptidyl peptidase
                     IV; T-cell activation antigen CD26; bile canaliculus
                     domain-specific membrane glycoprotein"
                     /calculated_mol_wt=87955
     Site            7..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14740.2)"
     Region          36..56
                     /region_name="DPPIV_rep"
                     /note="Dipeptidyl peptidase IV (DPP IV) low complexity
                     region; pfam18811"
                     /db_xref="CDD:465875"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16768443; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16768443; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Region          106..479
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16768443; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Site            319
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16768443; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Site            521
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16768443; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     Region          560..764
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     Site            686
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P14740.2)"
     CDS             1..767
                     /gene="Dpp4"
                     /gene_synonym="CD26; DPPIV"
                     /coded_by="NM_012789.2:90..2393"
                     /db_xref="GeneID:25253"
                     /db_xref="RGD:2515"
ORIGIN      
        1 mktpwkvllg llgvaalvti itvpvvllnk deaaadsrrt ytladylknt frvksyslrw
       61 vsdseylykq ennillfnae hgnssiflen stfeifgdsi sdysvspdrl fvlleynyvk
      121 qwrhsytasy siydlnkrql iteekipnnt qwitwsqegh klayvwkndi yvkiephlps
      181 hritstgken vifngindwv yeeeifgays alwwspngtf layaqfndtg vplieysfys
      241 deslqypktv wipypkagav nptvkffivn tdslsstttt ipmqitapas vttgdhylcd
      301 vawvsedris lqwlrriqny svmaicdydk tnlvwncptt qehietsatg wvgrfrpaep
      361 hftsdgssfy kivsdkdgyk hicqfqkdrk peqdctfitk gawevisiea ltsdylyyis
      421 neykempggr nlykiqltdh tnkkclscdl npercqyysv slskeakyyq lgcrgpglpl
      481 ytlhrstdqk elrvlednsa ldkmlqdvqm pskkldfivl netrfwyqmi lpphfdkskk
      541 ypllidvyag pcsqkadaaf rlnwatylas teniivasfd grgsgyqgdk imhainkrlg
      601 tlevedqiea arqflkmgfv dskqvaiwgw syggyvtsmv lgsgsgvfkc giavapvsrw
      661 eyydsvyter ymglptpedn ldhyrnstvm sraenfkqve yllihgtadd nvhfqqsaqi
      721 skalvdagvd fqamwytded hgiasstahq hiyshmshfl qqcfslr
//
