Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dipeptidase 2

Gene

DPEP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).By similarity

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Zn2+PROSITE-ProRule annotation

Enzyme regulationi

Inhibited by L-penicillamine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi91 – 911Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi188 – 1881Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi188 – 1881Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei215 – 2151SubstratePROSITE-ProRule annotation
Metal bindingi261 – 2611Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi282 – 2821Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei293 – 2931SubstratePROSITE-ProRule annotation
Binding sitei351 – 3511SubstratePROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS09532-MONOMER.
ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_264461. Aflatoxin activation and detoxification.

Protein family/group databases

MEROPSiM19.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 2 (EC:3.4.13.19)
Gene namesi
Name:DPEP2
ORF Names:UNQ284/PRO323
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:23028. DPEP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134985997.

Polymorphism and mutation databases

BioMutaiDPEP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 463431Dipeptidase 2PRO_0000231603Add
BLAST
Propeptidei464 – 48623Removed in mature formSequence AnalysisPRO_0000231604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication
Disulfide bondi138 ↔ 217PROSITE-ProRule annotation
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi235 – 2351N-linked (GlcNAc...)1 Publication
Disulfide bondi289 ↔ 321PROSITE-ProRule annotation
Disulfide bondi426 – 426InterchainPROSITE-ProRule annotation
Lipidationi463 – 4631GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9H4A9.
PRIDEiQ9H4A9.

Expressioni

Gene expression databases

BgeeiQ9H4A9.
CleanExiHS_DPEP2.
ExpressionAtlasiQ9H4A9. baseline and differential.
GenevisibleiQ9H4A9. HS.

Organism-specific databases

HPAiHPA035644.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.PROSITE-ProRule annotation

Protein-protein interaction databases

BioGridi122097. 19 interactions.
IntActiQ9H4A9. 1 interaction.
STRINGi9606.ENSP00000377430.

Structurei

3D structure databases

ProteinModelPortaliQ9H4A9.
SMRiQ9H4A9. Positions 72-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiQ9H4A9.
KOiK01273.
OMAiEVQNSCR.
OrthoDBiEOG7SJD4N.
PhylomeDBiQ9H4A9.
TreeFamiTF324523.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028531. Dpep2.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF9. PTHR10443:SF9. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H4A9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RALTTLGAPR
60 70 80 90 100
AHTMPGTYAP STTLSSPSTQ GLQEQARALM RDFPLVDGHN DLPLVLRQVY
110 120 130 140 150
QKGLQDVNLR NFSYGQTSLD RLRDGLVGAQ FWSAYVPCQT QDRDALRLTL
160 170 180 190 200
EQIDLIRRMC ASYSELELVT SAKALNDTQK LACLIGVEGG HSLDNSLSIL
210 220 230 240 250
PTFYMLGVRY LTLTHTCNTP WAESSAKGVH SFYNNISGLT DFGEKVVAEM
260 270 280 290 300
NRLGMMVDLS HVSDAVARRA LEVSQAPVIF SHSAARGVCN SARNVPDDIL
310 320 330 340 350
QLLKKNGGVV MVSLSMGVIQ CNPSANVSTV ADHFDHIKAV IGSKFIGIGG
360 370 380 390 400
DYDGAGKFPQ GLEDVSTYPV LIEELLSRGW SEEELQGVLR GNLLRVFRQV
410 420 430 440 450
EKVQEENKWQ SPLEDKFPDE QLSSSCHSDL SRLRQRQSLT SGQELTEIPI
460 470 480
HWTAKLPAKW SVSESSPHMA PVLAVVATFP VLILWL
Length:486
Mass (Da):53,306
Last modified:May 18, 2010 - v2
Checksum:iB08130A393809D04
GO
Isoform 2 (identifier: Q9H4A9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-129: Missing.

Note: No experimental confirmation available.
Show »
Length:399
Mass (Da):43,828
Checksum:i7BB6FA876E7D7B9E
GO

Sequence cautioni

The sequence AAQ88819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011P → R.5 Publications
Corresponds to variant rs255051 [ dbSNP | Ensembl ].
VAR_060230
Natural varianti468 – 4681H → D.
Corresponds to variant rs1133090 [ dbSNP | Ensembl ].
VAR_033894

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 12987Missing in isoform 2. 1 PublicationVSP_017851Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ295149 mRNA. Translation: CAC14667.1.
AK315090 mRNA. Translation: BAG37555.1.
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83200.1.
BC024021 mRNA. Translation: AAH24021.1.
AY358454 mRNA. Translation: AAQ88819.1. Different initiation.
CCDSiCCDS10857.1. [Q9H4A9-1]
RefSeqiNP_071750.1. NM_022355.3.
UniGeneiHs.372633.

Genome annotation databases

EnsembliENST00000393847; ENSP00000377430; ENSG00000167261.
ENST00000572888; ENSP00000458977; ENSG00000167261.
GeneIDi64174.
KEGGihsa:64174.
UCSCiuc002eve.4. human. [Q9H4A9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ295149 mRNA. Translation: CAC14667.1.
AK315090 mRNA. Translation: BAG37555.1.
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83200.1.
BC024021 mRNA. Translation: AAH24021.1.
AY358454 mRNA. Translation: AAQ88819.1. Different initiation.
CCDSiCCDS10857.1. [Q9H4A9-1]
RefSeqiNP_071750.1. NM_022355.3.
UniGeneiHs.372633.

3D structure databases

ProteinModelPortaliQ9H4A9.
SMRiQ9H4A9. Positions 72-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122097. 19 interactions.
IntActiQ9H4A9. 1 interaction.
STRINGi9606.ENSP00000377430.

Protein family/group databases

MEROPSiM19.004.

Polymorphism and mutation databases

BioMutaiDPEP2.

Proteomic databases

PaxDbiQ9H4A9.
PRIDEiQ9H4A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393847; ENSP00000377430; ENSG00000167261.
ENST00000572888; ENSP00000458977; ENSG00000167261.
GeneIDi64174.
KEGGihsa:64174.
UCSCiuc002eve.4. human. [Q9H4A9-1]

Organism-specific databases

CTDi64174.
GeneCardsiGC16M068021.
HGNCiHGNC:23028. DPEP2.
HPAiHPA035644.
MIMi609925. gene.
neXtProtiNX_Q9H4A9.
PharmGKBiPA134985997.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiQ9H4A9.
KOiK01273.
OMAiEVQNSCR.
OrthoDBiEOG7SJD4N.
PhylomeDBiQ9H4A9.
TreeFamiTF324523.

Enzyme and pathway databases

BioCyciMetaCyc:HS09532-MONOMER.
ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_264461. Aflatoxin activation and detoxification.

Miscellaneous databases

GenomeRNAii64174.
NextBioi66091.
PROiQ9H4A9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4A9.
CleanExiHS_DPEP2.
ExpressionAtlasiQ9H4A9. baseline and differential.
GenevisibleiQ9H4A9. HS.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028531. Dpep2.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF9. PTHR10443:SF9. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a human homologue of renal membrane dipeptidase."
    Chen J.M., Fortunato M., Barrett A.J.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-201.
    Tissue: Uterus.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-201.
    Tissue: Testis.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-201.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ARG-201.
    Tissue: Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-486 (ISOFORM 1), VARIANT ARG-201.
  7. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111 AND ASN-235.
    Tissue: Plasma.

Entry informationi

Entry nameiDPEP2_HUMAN
AccessioniPrimary (citable) accession number: Q9H4A9
Secondary accession number(s): B2RCF8, Q6UX92, Q8TC95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 18, 2010
Last modified: June 24, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.