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P14740

- DPP4_RAT

UniProt

P14740 - DPP4_RAT

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Protein

Dipeptidyl peptidase 4

Gene

Dpp4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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.By similarityPROSITE-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
Complete GO annotation...

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:3.4.14.5By similarity)
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2822Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini29 – 767739ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. endocytic vesicle Source: UniProtKB
  4. endoplasmic reticulum Source: RGD
  5. extracellular region Source: UniProtKB-KW
  6. Golgi apparatus Source: RGD
  7. integral component of membrane Source: UniProtKB-KW
  8. invadopodium membrane Source: UniProtKB
  9. lamellipodium Source: UniProtKB
  10. plasma membrane Source: RGD
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

        10         20         30         40         50
MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT
60 70 80 90 100
FRVKSYSLRW VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI
110 120 130 140 150
SDYSVSPDRL FVLLEYNYVK QWRHSYTASY SIYDLNKRQL ITEEKIPNNT
160 170 180 190 200
QWITWSQEGH KLAYVWKNDI YVKIEPHLPS HRITSTGKEN VIFNGINDWV
210 220 230 240 250
YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS DESLQYPKTV
260 270 280 290 300
WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD
310 320 330 340 350
VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG
360 370 380 390 400
WCGRFRPAEP HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK
410 420 430 440 450
GAWEVISIEA LTSDYLYYIS NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL
460 470 480 490 500
NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL YTLHRSTDQK ELRVLEDNSA
510 520 530 540 550
LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK YPLLIDVYAG
560 570 580 590 600
PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG
610 620 630 640 650
TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC
660 670 680 690 700
GIAVAPVSRW EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE
710 720 730 740 750
YLLIHGTADD NVHFQQSAQI SKALVDAGVD FQAMWYTDED HGIASSTAHQ
760
HIYSHMSHFL QQCFSLR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 138 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