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Protein

Dipeptidase 3

Gene

DPEP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis (By similarity).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 bindingi97 – 971Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi99 – 991Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi196 – 1961Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi196 – 1961Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi269 – 2691Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi290 – 2901Zinc 2; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Meiosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_264461. Aflatoxin activation and detoxification.

Protein family/group databases

MEROPSiM19.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 3 (EC:3.4.13.19)
Gene namesi
Name:DPEP3
ORF Names:UNQ834/PRO1772
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:23029. DPEP3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134978786.

Polymorphism and mutation databases

BioMutaiDPEP3.
DMDMi91206587.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 463428Dipeptidase 3PRO_0000231609Add
BLAST
Propeptidei464 – 48825Removed in mature formSequence AnalysisPRO_0000231610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi146 ↔ 225PROSITE-ProRule annotation
Disulfide bondi297 ↔ 329PROSITE-ProRule annotation
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi434 – 434InterchainPROSITE-ProRule annotation
Lipidationi463 – 4631GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9H4B8.
PRIDEiQ9H4B8.

PTM databases

PhosphoSiteiQ9H4B8.

Expressioni

Gene expression databases

BgeeiQ9H4B8.
CleanExiHS_DPEP3.
GenevestigatoriQ9H4B8.

Organism-specific databases

HPAiHPA031870.
HPA058607.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.PROSITE-ProRule annotation

Protein-protein interaction databases

BioGridi122099. 4 interactions.
STRINGi9606.ENSP00000268793.

Structurei

3D structure databases

ProteinModelPortaliQ9H4B8.
SMRiQ9H4B8. Positions 80-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiQ9H4B8.
OrthoDBiEOG7SJD4N.
PhylomeDBiQ9H4B8.
TreeFamiTF324523.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028533. Dpep3.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF14. PTHR10443:SF14. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H4B8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPTGREGSR ALSRRYLRRL LLLLLLLLLR QPVTRAETTP GAPRALSTLG
60 70 80 90 100
SPSLFTTPGV PSALTTPGLT TPGTPKTLDL RGRAQALMRS FPLVDGHNDL
110 120 130 140 150
PQVLRQRYKN VLQDVNLRNF SHGQTSLDRL RDGLVGAQFW SASVSCQSQD
160 170 180 190 200
QTAVRLALEQ IDLIHRMCAS YSELELVTSA EGLNSSQKLA CLIGVEGGHS
210 220 230 240 250
LDSSLSVLRS FYVLGVRYLT LTFTCSTPWA ESSTKFRHHM YTNVSGLTSF
260 270 280 290 300
GEKVVEELNR LGMMIDLSYA SDTLIRRVLE VSQAPVIFSH SAARAVCDNL
310 320 330 340 350
LNVPDDILQL LKKNGGIVMV TLSMGVLQCN LLANVSTVAD HFDHIRAVIG
360 370 380 390 400
SEFIGIGGNY DGTGRFPQGL EDVSTYPVLI EELLSRSWSE EELQGVLRGN
410 420 430 440 450
LLRVFRQVEK VREESRAQSP VEAEFPYGQL STSCHSHLVP QNGHQATHLE
460 470 480
VTKQPTNRVP WRSSNASPYL VPGLVAAATI PTFTQWLC
Length:488
Mass (Da):53,687
Last modified:April 4, 2006 - v2
Checksum:iF14FEE5AFB3F4471
GO

Sequence cautioni

The sequence AAH57789.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG51910.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC15385.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAW83198.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481Missing in AAH57789 (PubMed:15489334).Curated
Sequence conflicti312 – 3121Missing in AAQ88756 (PubMed:12975309).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ291679 mRNA. Translation: CAC15385.1. Different initiation.
AY358390 mRNA. Translation: AAQ88756.1.
AK057401 mRNA. Translation: BAG51910.1. Different initiation.
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83198.1. Different initiation.
BC057789 mRNA. Translation: AAH57789.1. Different initiation.
RefSeqiNP_001123230.1. NM_001129758.1.
NP_071752.3. NM_022357.3.
UniGeneiHs.302028.

Genome annotation databases

EnsembliENST00000268793; ENSP00000268793; ENSG00000141096.
GeneIDi64180.
KEGGihsa:64180.
UCSCiuc002evc.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ291679 mRNA. Translation: CAC15385.1. Different initiation.
AY358390 mRNA. Translation: AAQ88756.1.
AK057401 mRNA. Translation: BAG51910.1. Different initiation.
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83198.1. Different initiation.
BC057789 mRNA. Translation: AAH57789.1. Different initiation.
RefSeqiNP_001123230.1. NM_001129758.1.
NP_071752.3. NM_022357.3.
UniGeneiHs.302028.

3D structure databases

ProteinModelPortaliQ9H4B8.
SMRiQ9H4B8. Positions 80-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122099. 4 interactions.
STRINGi9606.ENSP00000268793.

Protein family/group databases

MEROPSiM19.011.

PTM databases

PhosphoSiteiQ9H4B8.

Polymorphism and mutation databases

BioMutaiDPEP3.
DMDMi91206587.

Proteomic databases

PaxDbiQ9H4B8.
PRIDEiQ9H4B8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268793; ENSP00000268793; ENSG00000141096.
GeneIDi64180.
KEGGihsa:64180.
UCSCiuc002evc.4. human.

Organism-specific databases

CTDi64180.
GeneCardsiGC16M068009.
HGNCiHGNC:23029. DPEP3.
HPAiHPA031870.
HPA058607.
MIMi609926. gene.
neXtProtiNX_Q9H4B8.
PharmGKBiPA134978786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiQ9H4B8.
OrthoDBiEOG7SJD4N.
PhylomeDBiQ9H4B8.
TreeFamiTF324523.

Enzyme and pathway databases

ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_264461. Aflatoxin activation and detoxification.

Miscellaneous databases

GeneWikiiDPEP3.
GenomeRNAii64180.
NextBioi66099.
PROiQ9H4B8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4B8.
CleanExiHS_DPEP3.
GenevestigatoriQ9H4B8.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028533. Dpep3.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF14. PTHR10443:SF14. 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 second human homologue of renal membrane dipeptidase."
    Chen J.M., Fortunato M., Barrett A.J.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Tissue: Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Testis.

Entry informationi

Entry nameiDPEP3_HUMAN
AccessioniPrimary (citable) accession number: Q9H4B8
Secondary accession number(s): B3KQ48, Q6PEZ5, Q6UXE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: April 29, 2015
This is version 103 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.