Q9H4A9 (DPEP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 2
EC=3.4.13.19

Gene names

Name:	DPEP2
ORF Names:	UNQ284/PRO323

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4) 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-anchor › GPI-anchor By similarity.
Sequence similarities	Belongs to the peptidase M19 family.
Sequence caution	The sequence AAQ88819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H4A9-1)

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.

Isoform 2 (identifier: Q9H4A9-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 463	431	Dipeptidase 2		PRO_0000231603
	Propeptide	464 – 486	23	Removed in mature form Potential		PRO_0000231604
Sites
	Metal binding	89	1	Zinc 1; catalytic By similarity
	Metal binding	91	1	Zinc 1; catalytic By similarity
	Metal binding	188	1	Zinc 1; catalytic By similarity
	Metal binding	188	1	Zinc 2; catalytic By similarity
	Metal binding	261	1	Zinc 2; catalytic By similarity
	Metal binding	282	1	Zinc 2; catalytic By similarity
	Binding site	215	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	351	1	Substrate By similarity
Amino acid modifications
	Lipidation	463	1	GPI-anchor amidated serine Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	176	1	N-linked (GlcNAc...) Potential
	Glycosylation	235	1	N-linked (GlcNAc...) Ref.7
	Disulfide bond	138 ↔ 217		By similarity
	Disulfide bond	289 ↔ 321		By similarity
	Disulfide bond	426		Interchain By similarity
Natural variations
	Alternative sequence	43 – 129	87	Missing in isoform 2.		VSP_017851
	Natural variant	201	1	P → R. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Corresponds to variant rs255051 [ dbSNP | Ensembl ].		VAR_060230
	Natural variant	468	1	H → D. Corresponds to variant rs1133090 [ dbSNP | Ensembl ].		VAR_033894

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: B08130A393809D04	FASTA	486	53,306
	10 20 30 40 50 60 MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RALTTLGAPR AHTMPGTYAP 70 80 90 100 110 120 STTLSSPSTQ GLQEQARALM RDFPLVDGHN DLPLVLRQVY QKGLQDVNLR NFSYGQTSLD 130 140 150 160 170 180 RLRDGLVGAQ FWSAYVPCQT QDRDALRLTL EQIDLIRRMC ASYSELELVT SAKALNDTQK 190 200 210 220 230 240 LACLIGVEGG HSLDNSLSIL PTFYMLGVRY LTLTHTCNTP WAESSAKGVH SFYNNISGLT 250 260 270 280 290 300 DFGEKVVAEM NRLGMMVDLS HVSDAVARRA LEVSQAPVIF SHSAARGVCN SARNVPDDIL 310 320 330 340 350 360 QLLKKNGGVV MVSLSMGVIQ CNPSANVSTV ADHFDHIKAV IGSKFIGIGG DYDGAGKFPQ 370 380 390 400 410 420 GLEDVSTYPV LIEELLSRGW SEEELQGVLR GNLLRVFRQV EKVQEENKWQ SPLEDKFPDE 430 440 450 460 470 480 QLSSSCHSDL SRLRQRQSLT SGQELTEIPI HWTAKLPAKW SVSESSPHMA PVLAVVATFP VLILWL
	Isoform 2 [UniParc]. Checksum: 7BB6FA876E7D7B9E	FASTA	399	43,828
	10 20 30 40 50 60 MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RAQFWSAYVP CQTQDRDALR 70 80 90 100 110 120 LTLEQIDLIR RMCASYSELE LVTSAKALND TQKLACLIGV EGGHSLDNSL SILPTFYMLG 130 140 150 160 170 180 VRYLTLTHTC NTPWAESSAK GVHSFYNNIS GLTDFGEKVV AEMNRLGMMV DLSHVSDAVA 190 200 210 220 230 240 RRALEVSQAP VIFSHSAARG VCNSARNVPD DILQLLKKNG GVVMVSLSMG VIQCNPSANV 250 260 270 280 290 300 STVADHFDHI KAVIGSKFIG IGGDYDGAGK FPQGLEDVST YPVLIEELLS RGWSEEELQG 310 320 330 340 350 360 VLRGNLLRVF RQVEKVQEEN KWQSPLEDKF PDEQLSSSCH SDLSRLRQRQ SLTSGQELTE 370 380 390 IPIHWTAKLP AKWSVSESSP HMAPVLAVVA TFPVLILWL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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. , 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], 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]	"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. , 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] 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, MASS SPECTROMETRY. Tissue: Plasma.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00007127. IPI00290954.
RefSeq	NP_071750.1. NM_022355.3.
UniGene	Hs.372633.
3D structure databases
ProteinModelPortal	Q9H4A9.
SMR	Q9H4A9. Positions 72-428.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H4A9. 1 interaction.
STRING	9606.ENSP00000268795.
Protein family/group databases
MEROPS	M19.002.
Polymorphism databases
DMDM	296434482.
Proteomic databases
PaxDb	Q9H4A9.
PRIDE	Q9H4A9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000393847; ENSP00000377430; ENSG00000167261. ENST00000412757; ENSP00000412549; ENSG00000167261. ENST00000572888; ENSP00000458977; ENSG00000167261.
GeneID	64174.
KEGG	hsa:64174.
UCSC	uc002eve.3. human.
Organism-specific databases
CTD	64174.
GeneCards	GC16M068021.
HGNC	HGNC:23028. DPEP2.
HPA	HPA035644.
MIM	609925. gene.
neXtProt	NX_Q9H4A9.
PharmGKB	PA134985997.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2355.
HOGENOM	HOG000072016.
HOVERGEN	HBG002339.
InParanoid	Q9H4A9.
OMA	CKNARNV.
OrthoDB	EOG4X97J0.
PhylomeDB	Q9H4A9.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09532-MONOMER.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9H4A9.
Bgee	Q9H4A9.
CleanEx	HS_DPEP2.
Genevestigator	Q9H4A9.
GermOnline	ENSG00000167261. Homo sapiens.
Family and domain databases
InterPro	IPR000180. Pept_M19_AS. IPR008257. Peptidase_M19. [Graphical view]
PANTHER	PTHR10443. PTHR10443. 1 hit.
Pfam	PF01244. Peptidase_M19. 1 hit. [Graphical view]
PROSITE	PS00869. RENAL_DIPEPTIDASE_1. 1 hit. PS51365. RENAL_DIPEPTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64174.
NextBio	66091.
SOURCE	Search...

Entry information

Entry name

DPEP2_HUMAN

Accession

Primary (citable) accession number: Q9H4A9
Secondary accession number(s): B2RCF8, Q6UX92, Q8TC95

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.