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P14740

- DPP4_RAT

UniProt

P14740 - DPP4_RAT

Protein

Dipeptidyl peptidase 4

Gene

Dpp4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones By similarity. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.By similarity

    Catalytic activityi

    Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by GPC3 and diprotin A.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei631 – 6311Charge relay systemPROSITE-ProRule annotation
    Active sitei709 – 7091Charge relay systemPROSITE-ProRule annotation
    Active sitei741 – 7411Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. collagen binding Source: RGD
    2. dipeptidyl-peptidase activity Source: UniProtKB
    3. peptide binding Source: RGD
    4. protease binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. receptor binding Source: UniProtKB
    7. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. endothelial cell migration Source: UniProtKB
    3. establishment of localization Source: RGD
    4. negative regulation of extracellular matrix disassembly Source: UniProtKB
    5. positive regulation of cell proliferation Source: UniProtKB
    6. proteolysis Source: RGD
    7. regulation of T cell mediated immunity Source: RGD
    8. T cell costimulation Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    BRENDAi3.4.14.5. 5301.

    Protein family/group databases

    MEROPSiS09.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 4 (EC:3.4.14.5)
    Alternative name(s):
    Bile canaliculus domain-specific membrane glycoprotein
    Dipeptidyl peptidase IV
    Short name:
    DPP IV
    GP110 glycoprotein
    T-cell activation antigen CD26
    CD_antigen: CD26
    Cleaved into the following 3 chains:
    Alternative name(s):
    Dipeptidyl peptidase IV membrane form
    Alternative name(s):
    Dipeptidyl peptidase IV soluble form
    Alternative name(s):
    Dipeptidyl peptidase IV 60 kDa soluble form
    Gene namesi
    Name:Dpp4
    Synonyms:Cd26
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2515. Dpp4.

    Subcellular locationi

    Chain Dipeptidyl peptidase 4 soluble form : Secreted
    Note: Detected in the serum and the seminal fluid.By similarity
    Cell membrane; Single-pass type II membrane protein. Apical cell membrane By similarity; Single-pass type II membrane protein By similarity. Cell projectioninvadopodium membrane By similarity; Single-pass type II membrane protein By similarity. Cell projectionlamellipodium membrane By similarity; Single-pass type II membrane protein By similarity. Cell junction By similarity. Membrane raft By similarity
    Note: Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface By similarity.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. cell junction Source: UniProtKB-SubCell
    3. cell surface Source: UniProtKB
    4. endocytic vesicle Source: UniProtKB
    5. endoplasmic reticulum Source: RGD
    6. extracellular region Source: UniProtKB-SubCell
    7. Golgi apparatus Source: RGD
    8. integral component of membrane Source: UniProtKB-KW
    9. invadopodium membrane Source: UniProtKB
    10. lamellipodium Source: UniProtKB
    11. lamellipodium membrane Source: UniProtKB-SubCell
    12. membrane raft Source: UniProtKB-SubCell
    13. plasma membrane Source: RGD

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi629 – 6291G → A: Reduced activity. 1 Publication
    Mutagenesisi629 – 6291G → R: Reduced activity. 1 Publication
    Mutagenesisi630 – 6301W → E: No effect on activity. 1 Publication
    Mutagenesisi631 – 6311S → A: Reduced activity. 1 Publication
    Mutagenesisi632 – 6321Y → F: No effect on activity. 1 Publication
    Mutagenesisi632 – 6321Y → G: Reduced activity. 1 Publication
    Mutagenesisi632 – 6321Y → L: Reduced activity. 1 Publication
    Mutagenesisi633 – 6331G → A: Reduced activity. 1 Publication
    Mutagenesisi633 – 6331G → S: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 767767Dipeptidyl peptidase 4 membrane formPRO_0000027219Add
    BLAST
    Chaini37 – 767731Dipeptidyl peptidase 4 soluble formPRO_0000027220Add
    BLAST
    Chaini281 – 767487Dipeptidyl peptidase 4 60 kDa soluble formPRO_0000027221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)1 Publication
    Glycosylationi90 – 901N-linked (GlcNAc...)1 Publication
    Glycosylationi148 – 1481N-linked (GlcNAc...)By similarity
    Glycosylationi217 – 2171N-linked (GlcNAc...)By similarity
    Glycosylationi227 – 2271N-linked (GlcNAc...)1 Publication
    Glycosylationi319 – 3191N-linked (GlcNAc...)1 Publication
    Disulfide bondi326 ↔ 3371 Publication
    Disulfide bondi383 ↔ 3951 Publication
    Disulfide bondi445 ↔ 4481 Publication
    Disulfide bondi455 ↔ 4731 Publication
    Glycosylationi521 – 5211N-linked (GlcNAc...)1 Publication
    Disulfide bondi650 ↔ 7631 Publication
    Glycosylationi686 – 6861N-linked (GlcNAc...)By similarity

    Post-translational modificationi

    The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing.By similarity
    N- and O-Glycosylated.By similarity
    Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP14740.
    PRIDEiP14740.

    Expressioni

    Tissue specificityi

    Expressed in bile ducts and other epithelial brush borders (small intestine, kidney, colon, pancreatic duct); acinar structures in salivary glands; endothelial structures and T cell areas in thymus, spleen and lymph node.1 Publication

    Gene expression databases

    GenevestigatoriP14740.

    Interactioni

    Subunit structurei

    Monomer. Heterodimer with Seprase (FAP). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Associates with collagen. Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Interacts (extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity. Interacts with CAV1 (via the N-terminus); the interaction is direct. Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11. Interacts with IGF2R; the interaction is direct. Interacts with GPC3 By similarity. Homodimer.By similarity1 Publication

    Protein-protein interaction databases

    IntActiP14740. 1 interaction.
    MINTiMINT-4655516.
    STRINGi10116.ENSRNOP00000045536.

    Structurei

    Secondary structure

    1
    767
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 486
    Beta strandi58 – 603
    Beta strandi62 – 7211
    Beta strandi74 – 829
    Beta strandi84 – 885
    Helixi90 – 934
    Helixi97 – 993
    Beta strandi100 – 1056
    Beta strandi109 – 12012
    Beta strandi122 – 1243
    Beta strandi126 – 1349
    Turni135 – 1384
    Beta strandi139 – 1413
    Beta strandi148 – 1503
    Beta strandi152 – 1554
    Beta strandi157 – 1604
    Beta strandi162 – 1665
    Beta strandi169 – 1757
    Turni189 – 1913
    Beta strandi192 – 1965
    Helixi199 – 2046
    Beta strandi207 – 2104
    Beta strandi212 – 2143
    Beta strandi216 – 22712
    Beta strandi233 – 2386
    Beta strandi248 – 2536
    Beta strandi263 – 2719
    Helixi273 – 2764
    Beta strandi283 – 2853
    Turni289 – 2935
    Beta strandi296 – 30510
    Beta strandi308 – 32922
    Turni330 – 3334
    Beta strandi334 – 3363
    Helixi339 – 3413
    Beta strandi342 – 3465
    Beta strandi348 – 3503
    Beta strandi352 – 3565
    Beta strandi366 – 3749
    Beta strandi376 – 3783
    Beta strandi380 – 3889
    Turni391 – 3933
    Beta strandi396 – 3983
    Beta strandi401 – 4033
    Beta strandi405 – 4117
    Beta strandi413 – 4219
    Helixi423 – 4253
    Beta strandi430 – 4389
    Beta strandi443 – 4508
    Turni452 – 4543
    Beta strandi455 – 4628
    Beta strandi466 – 4738
    Beta strandi475 – 4784
    Beta strandi480 – 4889
    Beta strandi491 – 4966
    Helixi499 – 5046
    Helixi505 – 5073
    Beta strandi512 – 5209
    Beta strandi523 – 5319
    Beta strandi541 – 5477
    Helixi564 – 5707
    Beta strandi575 – 5795
    Beta strandi585 – 5873
    Helixi589 – 5924
    Helixi593 – 5953
    Turni599 – 6013
    Helixi602 – 61615
    Beta strandi620 – 63011
    Helixi632 – 64110
    Turni642 – 6443
    Beta strandi649 – 6557
    Helixi660 – 6623
    Helixi665 – 6728
    Turni677 – 6804
    Helixi681 – 6866
    Helixi690 – 6989
    Beta strandi699 – 7068
    Beta strandi710 – 7123
    Helixi714 – 72613
    Beta strandi732 – 7365
    Helixi746 – 76419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GBCX-ray2.80A/B38-767[»]
    2GBFX-ray3.10A/B38-767[»]
    2GBGX-ray3.00A/B38-767[»]
    2GBIX-ray3.30A/B38-767[»]
    2I3ZX-ray2.90A/B38-767[»]
    2OAEX-ray3.00A/B38-767[»]
    4FFVX-ray2.40A/B38-767[»]
    4FFWX-ray2.90A/B38-767[»]
    ProteinModelPortaliP14740.
    SMRiP14740. Positions 38-767.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14740.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini29 – 767739ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2822Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family. DPPIV subfamily.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1506.
    HOGENOMiHOG000231875.
    HOVERGENiHBG005527.
    InParanoidiP14740.
    KOiK01278.
    PhylomeDBiP14740.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14740-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT    50
    FRVKSYSLRW VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI 100
    SDYSVSPDRL FVLLEYNYVK QWRHSYTASY SIYDLNKRQL ITEEKIPNNT 150
    QWITWSQEGH KLAYVWKNDI YVKIEPHLPS HRITSTGKEN VIFNGINDWV 200
    YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS DESLQYPKTV 250
    WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD 300
    VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG 350
    WCGRFRPAEP HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK 400
    GAWEVISIEA LTSDYLYYIS NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL 450
    NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL YTLHRSTDQK ELRVLEDNSA 500
    LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK YPLLIDVYAG 550
    PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG 600
    TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC 650
    GIAVAPVSRW EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE 700
    YLLIHGTADD NVHFQQSAQI SKALVDAGVD FQAMWYTDED HGIASSTAHQ 750
    HIYSHMSHFL QQCFSLR 767
    Length:767
    Mass (Da):88,089
    Last modified:December 7, 2004 - v2
    Checksum:iED947174F1F3E440
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381R → A in AAA41096. (PubMed:2563382)Curated
    Sequence conflicti54 – 541Missing AA sequence (PubMed:1970322)Curated
    Sequence conflicti183 – 1831I → T in AAA41272. (PubMed:3479775)Curated
    Sequence conflicti332 – 3321T → N in AAA41272. (PubMed:3479775)Curated
    Sequence conflicti352 – 3521C → V in AAA41272. (PubMed:3479775)Curated
    Sequence conflicti394 – 3941V → D in AAA41272. (PubMed:3479775)Curated
    Sequence conflicti562 – 5621L → F in AAA41272. (PubMed:3479775)Curated
    Sequence conflicti624 – 6241R → Q in AAA41272. (PubMed:3479775)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04591 mRNA. Translation: AAA41096.1.
    J02997 mRNA. Translation: AAA41272.1.
    PIRiA39914.
    RefSeqiNP_036921.1. NM_012789.1.
    UniGeneiRn.91364.

    Genome annotation databases

    GeneIDi25253.
    KEGGirno:25253.
    UCSCiRGD:2515. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04591 mRNA. Translation: AAA41096.1 .
    J02997 mRNA. Translation: AAA41272.1 .
    PIRi A39914.
    RefSeqi NP_036921.1. NM_012789.1.
    UniGenei Rn.91364.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GBC X-ray 2.80 A/B 38-767 [» ]
    2GBF X-ray 3.10 A/B 38-767 [» ]
    2GBG X-ray 3.00 A/B 38-767 [» ]
    2GBI X-ray 3.30 A/B 38-767 [» ]
    2I3Z X-ray 2.90 A/B 38-767 [» ]
    2OAE X-ray 3.00 A/B 38-767 [» ]
    4FFV X-ray 2.40 A/B 38-767 [» ]
    4FFW X-ray 2.90 A/B 38-767 [» ]
    ProteinModelPortali P14740.
    SMRi P14740. Positions 38-767.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P14740. 1 interaction.
    MINTi MINT-4655516.
    STRINGi 10116.ENSRNOP00000045536.

    Chemistry

    BindingDBi P14740.
    ChEMBLi CHEMBL4653.

    Protein family/group databases

    MEROPSi S09.003.

    Proteomic databases

    PaxDbi P14740.
    PRIDEi P14740.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25253.
    KEGGi rno:25253.
    UCSCi RGD:2515. rat.

    Organism-specific databases

    CTDi 1803.
    RGDi 2515. Dpp4.

    Phylogenomic databases

    eggNOGi COG1506.
    HOGENOMi HOG000231875.
    HOVERGENi HBG005527.
    InParanoidi P14740.
    KOi K01278.
    PhylomeDBi P14740.

    Enzyme and pathway databases

    BRENDAi 3.4.14.5. 5301.

    Miscellaneous databases

    EvolutionaryTracei P14740.
    NextBioi 605879.
    PROi P14740.

    Gene expression databases

    Genevestigatori P14740.

    Family and domain databases

    Gene3Di 2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view ]
    Pfami PF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Ogata S., Misumi Y., Ikehara Y.
      J. Biol. Chem. 264:3596-3601(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes."
      Hong W., Doyle D.
      Proc. Natl. Acad. Sci. U.S.A. 84:7962-7966(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Membrane orientation of rat gp110 as studied by in vitro translation."
      Hong W.J., Doyle D.
      J. Biol. Chem. 263:16892-16898(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40.
    4. "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."
      McCaughan G.W., Wickson J.E., Creswick P.F., Gorrell M.D.
      Hepatology 11:534-544(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-58, TISSUE SPECIFICITY.
    5. "N-terminal amino acid sequence of the 60-kDa protein of rat kidney dipeptidyl peptidase IV."
      Iwaki-Egawa S., Watanabe Y., Fujimoto Y.
      Biol. Chem. Hoppe-Seyler 374:973-975(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 281-302, MUTAGENESIS OF GLY-629; TRP-630; SER-631; TRY-632 AND GLY-633.
      Tissue: Kidney.
    6. "Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis."
      Ogata S., Misumi Y., Tsuji E., Takami N., Oda K., Ikehara Y.
      Biochemistry 31:2582-2587(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 624-648.
    7. "Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV."
      Hong W., Doyle D.
      J. Cell Biol. 111:323-328(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIGNAL-ANCHOR.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 38-767 IN COMPLEX WITH INHIBITORS, GLYCOSYLATION AT ASN-83; ASN-90; ASN-227; ASN-319 AND ASN-521, DISULFIDE BONDS.

    Entry informationi

    Entry nameiDPP4_RAT
    AccessioniPrimary (citable) accession number: P14740
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3