CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005729
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dipeptidyl peptidase 4 
Protein Synonyms/Alias
 Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; Thymocyte-activating molecule; THAM; CD26; Dipeptidyl peptidase 4 membrane form; Dipeptidyl peptidase IV membrane form; Dipeptidyl peptidase 4 soluble form; Dipeptidyl peptidase IV soluble form 
Gene Name
 Dpp4 
Gene Synonyms/Alias
 Cd26 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
609EAARQFVKMGFVDSKacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 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). 
Sequence Annotation
 ACT_SITE 624 624 Charge relay system (By similarity).
 ACT_SITE 702 702 Charge relay system (By similarity).
 ACT_SITE 734 734 Charge relay system (By similarity).
 CARBOHYD 83 83 N-linked (GlcNAc...) (By similarity).
 CARBOHYD 90 90 N-linked (GlcNAc...) (By similarity).
 CARBOHYD 145 145 N-linked (GlcNAc...); atypical.
 CARBOHYD 213 213 N-linked (GlcNAc...) (Potential).
 CARBOHYD 223 223 N-linked (GlcNAc...) (By similarity).
 CARBOHYD 315 315 N-linked (GlcNAc...) (By similarity).
 CARBOHYD 328 328 N-linked (GlcNAc...) (Potential).
 CARBOHYD 514 514 N-linked (GlcNAc...).
 CARBOHYD 679 679 N-linked (GlcNAc...) (By similarity).
 DISULFID 322 333 By similarity.
 DISULFID 379 388 By similarity.
 DISULFID 438 441 By similarity.
 DISULFID 448 466 By similarity.
 DISULFID 643 756 By similarity.  
Keyword
 Aminopeptidase; Cell adhesion; Cell junction; Cell membrane; Cell projection; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease; Receptor; Reference proteome; Secreted; Serine protease; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 760 AA 
Protein Sequence
MKTPWKVLLG LLGVAALVTI ITVPIVLLSK DEAAADSRRT YSLADYLKST FRVKSYSLWW 60
VSDFEYLYKQ ENNILLLNAE HGNSSIFLEN STFESFGYHS VSPDRLFVLL EYNYVKQWRH 120
SYTASYNIYD VNKRQLITEE KIPNNTQWIT WSPEGHKLAY VWKNDIYVKV EPHLPSHRIT 180
STGEENVIYN GITDWVYEEE VFGAYSALWW SPNNTFLAYA QFNDTGVPLI EYSFYSDESL 240
QYPKTVWIPY PKAGAVNPTV KFFIVNIDSL SSSSSAAPIQ IPAPASVARG DHYLCDVVWA 300
TEERISLQWL RRIQNYSVMA ICDYDKINLT WNCPSEQQHV EMSTTGWVGR FRPAEPHFTS 360
DGSSFYKIIS DKDGYKHICH FPKDKKDCTF ITKGAWEVIS IEALTSDYLY YISNQYKEMP 420
GGRNLYKIQL TDHTNVKCLS CDLNPERCQY YAVSFSKEAK YYQLGCWGPG LPLYTLHRST 480
DHKELRVLED NSALDRMLQD VQMPSKKLDF IVLNETRFWY QMILPPHFDK SKKYPLLLDV 540
YAGPCSQKAD ASFRLNWATY LASTENIIVA SFDGRGSGYQ GDKIMHAINR RLGTLEVEDQ 600
IEAARQFVKM GFVDSKRVAI WGWSYGGYVT SMVLGSGSGV FKCGIAVAPV SRWEYYDSVY 660
TERYMGLPIP EDNLDHYRNS TVMSRAEHFK QVEYLLIHGT ADDNVHFQQS AQISKALVDA 720
GVDFQAMWYT DEDHGIASST AHQHIYSHMS HFLQQCFSLH 760 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO:0009986; C:cell surface; ISS:UniProtKB.
 GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0046581; C:intercellular canaliculus; IDA:MGI.
 GO:0071438; C:invadopodium membrane; ISS:UniProtKB.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
 GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0008239; F:dipeptidyl-peptidase activity; ISS:UniProtKB.
 GO:0002020; F:protease binding; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0005102; F:receptor binding; ISS:UniProtKB.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
 GO:0010716; P:negative regulation of extracellular matrix disassembly; ISS:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0042110; P:T cell activation; IEA:Compara.
 GO:0031295; P:T cell costimulation; ISS:UniProtKB. 
Interpro
 IPR002471; Pept_S9_AS.
 IPR001375; Peptidase_S9.
 IPR002469; Peptidase_S9B. 
Pfam
 PF00930; DPPIV_N
 PF00326; Peptidase_S9 
SMART
  
PROSITE
 PS00708; PRO_ENDOPEP_SER 
PRINTS