P81425

PR
Gene name
DPP4 (CD26)
Protein name
Dipeptidyl peptidase 4
Names
Species
Bos taurus (Bovine)
KEGG Pathway
bta:281122
EC number
3.4.14.5: Dipeptidyl-peptidases and tripeptidyl-peptidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-69 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P81425

Entry ID Method Resolution Chain Position Source
AF-P81425-F1 Predicted AlphaFoldDB

69 variants for P81425

Variant ID(s) Position Change Description Diseaes Association Provenance
rs455301580 2 K>E No EVA
rs432643545 22 T>P No EVA
rs478133742 33 D>E No EVA
rs438730618 34 A>P No EVA
rs438730618 34 A>S No EVA
rs463628661 36 T>I No EVA
rs482021416 37 D>A No EVA
rs449017897 40 R>S No EVA
rs467265946 41 T>A No EVA
rs446376383 45 A>D No EVA
rs451140566 46 D>E No EVA
rs432671158 46 D>H No EVA
rs469669742 49 K>* No EVA
rs436563770 51 T>P No EVA
rs455143146 52 F>L No EVA
rs434096433 54 M>R No EVA
rs441660945 75 I>S No EVA
rs460809300 87 I>T No EVA
rs469431645 113 I>L No EVA
rs440398913 122 Q>P No EVA
rs1117179225 137 N>K No EVA
rs440135571 169 N>S No EVA
rs378991725 199 D>N No EVA
rs3423132401 251 V>M No EVA
rs448265489 261 V>L No EVA
rs434585909 265 I>T No EVA
rs719669768 277 P>L No EVA
rs471811811 353 V>G No EVA
rs476761672 398 K>I No EVA
rs451762861 404 I>S No EVA
rs434688676 454 Q>L No EVA
rs467642899 455 Y>C No EVA
rs469517618 466 Y>* No EVA
rs436372339 466 Y>D No EVA
rs450869269 470 R>S No EVA
rs456157905 489 E>D No EVA
rs437578771 490 L>R No EVA
rs464274987 491 R>K No EVA
rs433766398 498 D>H No EVA
rs466745148 504 Q>K No EVA
rs448178928 507 Q>K No EVA
rs481410082 511 K>M No EVA
rs450027290 518 L>* No EVA
rs482791519 519 H>P No EVA
rs466585938 546 Y>* No EVA
rs452788677 550 C>F No EVA
rs464565300 560 L>V No EVA
rs438184473 575 A>T No EVA
rs457451827 584 Y>D No EVA
rs471078296 588 K>N No EVA
rs474947026 596 R>I No EVA
rs442073753 597 L>V No EVA
rs454006325 598 G>* No EVA
rs458878683 607 E>D No EVA
rs714111111 625 I>V No EVA
rs463479050 662 D>G No EVA
rs482126407 664 V>L No EVA
rs442720772 668 R>S No EVA
rs479678726 670 M>R No EVA
rs465105298 675 P>L No EVA
rs476996051 678 N>S No EVA
rs450471387 682 Y>D No EVA
rs455206095 710 V>L No EVA
rs435046021 721 A>P No EVA
rs453653485 722 L>Q No EVA
rs471973891 723 V>L No EVA
rs439063442 727 V>A No EVA
rs452513958 733 W>G No EVA
rs470787195 741 I>F No EVA

1 associated diseases with P81425

[MIM: 116300]: Cataract 30, multiple types (CTRCT30)

An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:19126778, ECO:0000269|PubMed:26694549, ECO:0000269|PubMed:28450710}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:19126778, ECO:0000269|PubMed:26694549, ECO:0000269|PubMed:28450710}. Note=The disease is caused by variants affecting the gene represented in this entry.

7 regional properties for P81425

Type Name Position InterPro Accession
domain C2 domain 89 - 211 IPR000008-1
domain C2 domain 251 - 384 IPR000008-2
domain Synaptotagmin 255 - 270 IPR001565-1
domain Synaptotagmin 270 - 283 IPR001565-2
domain Synaptotagmin 327 - 342 IPR001565-3
domain Synaptotagmin 347 - 357 IPR001565-4
domain Rabphilin/Doc2, first C2 domain 90 - 213 IPR047022

Functions

Description
EC Number 3.4.14.5 Dipeptidyl-peptidases and tripeptidyl-peptidases
Subcellular Localization
  • [Dipeptidyl peptidase 4 soluble form]: Secreted
  • Detected in the serum and the seminal fluid
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
apical plasma membrane The region of the plasma membrane located at the apical end of the cell.
cell surface The external part of the cell wall and/or plasma membrane.
endocytic vesicle A membrane-bounded intracellular vesicle formed by invagination of the plasma membrane around an extracellular substance. Endocytic vesicles fuse with early endosomes to deliver the cargo for further sorting.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
intercellular canaliculus An extremely narrow tubular channel located between adjacent cells. An instance of this is the secretory canaliculi occurring between adjacent parietal cells in the gastric mucosa of vertebrates.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
lamellipodium membrane The portion of the plasma membrane surrounding a lamellipodium.
membrane raft Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

8 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
chemorepellent activity Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a lower concentration of that signal.
dipeptidyl-peptidase activity Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain.
protease binding Binding to a protease or a peptidase.
protein homodimerization activity Binding to an identical protein to form a homodimer.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
signaling receptor binding Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
virus receptor activity Combining with a virus component and mediating entry of the virus into the cell.

13 GO annotations of biological process

Name Definition
behavioral fear response An acute behavioral change resulting from a perceived external threat.
cell adhesion The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
endothelial cell migration The orderly movement of an endothelial cell into the extracellular matrix to form an endothelium.
locomotory exploration behavior The specific movement from place to place of an organism in response to a novel environment.
negative regulation of extracellular matrix disassembly Any process that decreases the rate, frequency or extent of extracellular matrix disassembly. Extracellular matrix disassembly is a process that results in the breakdown of the extracellular matrix.
negative regulation of neutrophil chemotaxis Any process that decreases the frequency, rate, or extent of neutrophil chemotaxis. Neutrophil chemotaxis is the directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding.
positive regulation of cell population proliferation Any process that activates or increases the rate or extent of cell proliferation.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
psychomotor behavior The specific behavior of an organism that combines cognitive functions and physical movement. For example, driving a car, throwing a ball, or playing a musical instrument.
regulation of cell-cell adhesion mediated by integrin Any process that modulates the frequency, rate, or extent of cell-cell adhesion mediated by integrin.
response to hypoxia Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
T cell activation The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
T cell costimulation The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the T cell receptor to augment T cell activation.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P81425 DPP4 Dipeptidyl peptidase 4 Bos taurus (Bovine) PR
Q6NXK7 Dpp10 Inactive dipeptidyl peptidase 10 Mus musculus (Mouse) PR
Q10MJ1 GEP Probable glutamyl endopeptidase, chloroplastic Oryza sativa subsp japonica (Rice) PR
Q18253 dpf-2 Dipeptidyl peptidase family member 2 Caenorhabditis elegans PR
10 20 30 40 50 60
MKTPWKVLLG LLAIAALVTV ITVPVVLLTK GNDASTDSRR TYTLADYLKN TFRMKFYNLR
70 80 90 100 110 120
WVSDHEYLYK QENNILLFNA EYGNSSIFLE NSTFDEFGHS INDYSVSPDR QYILFEYNYV
130 140 150 160 170 180
KQWRHSYTAS YDIYDLNKRQ LITEERIPNN TQWITWSSVG HKLAYVWNND IYVKNEPNSP
190 200 210 220 230 240
SQRITWTGKK DVIYNGITDW VYEEEVFSAY SALWWSPNST FLAYAQFNDT EVPLIEYSFY
250 260 270 280 290 300
SDESLQYPKT VKIPYPKAGA VNPTIKFFVV NISSLSPNIN ATSQQIVPPG SVLIGDHYLC
310 320 330 340 350 360
DVTWVTEERI SLQWLRRIQN YSIMDICDYD RSTGRWISSV GRQHIEISTT GWVGRFRPAE
370 380 390 400 410 420
PHFTSDGNSF YKIISNEEGY KHICHFQTDK RNCTFITKGA WEVIGIEALT SDYLYYISNE
430 440 450 460 470 480
YKGMPGARNL YKIQLNDYTK VTCLSCELNP DRCQYYSVSF SQEAKYYQLR CSGPGLPLYT
490 500 510 520 530 540
LHNSNNDKEL RVLENNSDLD QVLQDVQMPS KKLDFIHLHG TKFWYQMILP PHFDKSKKYP
550 560 570 580 590 600
LLLEVYAGPC SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAINRRLGTF
610 620 630 640 650 660
EVEDQIEATR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI AVAPVSKWEY
670 680 690 700 710 720
YDSVYTERYM GLPTPEDNLD SYRNSTVMSR AENFKQVEYL LIHGTADDNV HFQQSAQISK
730 740 750 760
ALVDAGVDFQ SMWYTDEDHG IASSTAHQHI YTHMSHFLKQ CFSLL