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Q9H4B8 (DPEP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidase 3

EC=3.4.13.19
Gene names
Name:DPEP3
ORF Names:UNQ834/PRO1772
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis By similarity.

Catalytic activity

Hydrolysis of dipeptides.

Cofactor

Zinc By similarity.

Enzyme regulation

Inhibited by L-penicillamine By similarity.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Membrane; Lipid-anchorGPI-anchor By similarity.

Sequence similarities

Belongs to the peptidase M19 family.

Sequence caution

The sequence AAH57789.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAG51910.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAC15385.1 differs from that shown. Reason: Erroneous initiation.

The sequence EAW83198.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 463428Dipeptidase 3
PRO_0000231609
Propeptide464 – 48825Removed in mature form Potential
PRO_0000231610

Sites

Metal binding971Zinc 1; catalytic By similarity
Metal binding991Zinc 1; catalytic By similarity
Metal binding1961Zinc 1; catalytic By similarity
Metal binding1961Zinc 2; catalytic By similarity
Metal binding2691Zinc 2; catalytic By similarity
Metal binding2901Zinc 2; catalytic By similarity

Amino acid modifications

Lipidation4631GPI-anchor amidated serine Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Disulfide bond146 ↔ 225 By similarity
Disulfide bond297 ↔ 329 By similarity
Disulfide bond434Interchain By similarity

Experimental info

Sequence conflict481Missing in AAH57789. Ref.6
Sequence conflict3121Missing in AAQ88756. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H4B8 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: F14FEE5AFB3F4471

FASTA48853,687
        10         20         30         40         50         60 
MQPTGREGSR ALSRRYLRRL LLLLLLLLLR QPVTRAETTP GAPRALSTLG SPSLFTTPGV 

        70         80         90        100        110        120 
PSALTTPGLT TPGTPKTLDL RGRAQALMRS FPLVDGHNDL PQVLRQRYKN VLQDVNLRNF 

       130        140        150        160        170        180 
SHGQTSLDRL RDGLVGAQFW SASVSCQSQD QTAVRLALEQ IDLIHRMCAS YSELELVTSA 

       190        200        210        220        230        240 
EGLNSSQKLA CLIGVEGGHS LDSSLSVLRS FYVLGVRYLT LTFTCSTPWA ESSTKFRHHM 

       250        260        270        280        290        300 
YTNVSGLTSF GEKVVEELNR LGMMIDLSYA SDTLIRRVLE VSQAPVIFSH SAARAVCDNL 

       310        320        330        340        350        360 
LNVPDDILQL LKKNGGIVMV TLSMGVLQCN LLANVSTVAD HFDHIRAVIG SEFIGIGGNY 

       370        380        390        400        410        420 
DGTGRFPQGL EDVSTYPVLI EELLSRSWSE EELQGVLRGN LLRVFRQVEK VREESRAQSP 

       430        440        450        460        470        480 
VEAEFPYGQL STSCHSHLVP QNGHQATHLE VTKQPTNRVP WRSSNASPYL VPGLVAAATI 


PTFTQWLC 

« Hide

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001123230.1. NM_001129758.1.
NP_071752.3. NM_022357.3.
UniGeneHs.302028.

3D structure databases

ProteinModelPortalQ9H4B8.
SMRQ9H4B8. Positions 80-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122099. 1 interaction.
STRING9606.ENSP00000268793.

Protein family/group databases

MEROPSM19.004.

PTM databases

PhosphoSiteQ9H4B8.

Polymorphism databases

DMDM91206587.

Proteomic databases

PaxDbQ9H4B8.
PRIDEQ9H4B8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268793; ENSP00000268793; ENSG00000141096.
GeneID64180.
KEGGhsa:64180.
UCSCuc002evc.4. human.

Organism-specific databases

CTD64180.
GeneCardsGC16M068009.
HGNCHGNC:23029. DPEP3.
HPAHPA031870.
HPA058607.
MIM609926. gene.
neXtProtNX_Q9H4B8.
PharmGKBPA134978786.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2355.
HOGENOMHOG000072016.
HOVERGENHBG002339.
InParanoidQ9H4B8.
OrthoDBEOG7SJD4N.
TreeFamTF324523.

Gene expression databases

BgeeQ9H4B8.
CleanExHS_DPEP3.
GenevestigatorQ9H4B8.

Family and domain databases

InterProIPR028533. Dpep3.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF14. PTHR10443:SF14. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDPEP3.
GenomeRNAi64180.
NextBio66099.
PROQ9H4B8.
SOURCESearch...

Entry information

Entry nameDPEP3_HUMAN
AccessionPrimary (citable) accession number: Q9H4B8
Secondary accession number(s): B3KQ48, Q6PEZ5, Q6UXE4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: February 19, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM