Q8C255 (DPEP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 2
EC=3.4.13.19

Alternative name(s):
Membrane-bound dipeptidase 2
Short name=MBD-2

Gene names

Name:	Dpep2
Synonyms:	Mbd2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	478 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).
Catalytic activity	Hydrolysis of dipeptides.
Cofactor	Zinc By similarity.
Enzyme regulation	Inhibited by L-penicillamine. Ref.1
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Membrane; Lipid-anchor › GPI-anchor Ref.1.
Tissue specificity	Expressed in heart, lung, testis, spleen and skeletal muscle. Ref.1
Sequence similarities	Belongs to the peptidase M19 family.
Biophysicochemical properties	Kinetic parameters: KM=5 µM for LTD4 Ref.1

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein GPI-anchor Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored component of membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from electronic annotation. Source: InterPro exopeptidase activity Inferred from direct assay Ref.1. Source: MGI 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 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8C255-1)

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: Q8C255-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAWHGETYCL...VPACSALSKM
     176-179: ALNS → VKWIYSG
     334-340: DHFDHIR → EKGQQKHQFTPPRDTHFV

Isoform 3 (identifier: Q8C255-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 459	428	Dipeptidase 2		PRO_0000231605
	Propeptide	460 – 478	19	Removed in mature form Potential		PRO_0000231606
Sites
	Metal binding	91	1	Zinc 1; catalytic By similarity
	Metal binding	93	1	Zinc 1; catalytic By similarity
	Metal binding	190	1	Zinc 1; catalytic By similarity
	Metal binding	190	1	Zinc 2; catalytic By similarity
	Metal binding	263	1	Zinc 2; catalytic By similarity
	Metal binding	284	1	Zinc 2; catalytic By similarity
	Binding site	217	1	Substrate By similarity
	Binding site	295	1	Substrate By similarity
	Binding site	353	1	Substrate By similarity
Amino acid modifications
	Lipidation	459	1	GPI-anchor amidated serine Potential
	Glycosylation	113	1	N-linked (GlcNAc...) By similarity
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Disulfide bond	140 ↔ 219		By similarity
	Disulfide bond	291 ↔ 323		By similarity
	Disulfide bond	428		Interchain By similarity
Natural variations
	Alternative sequence	1 – 93	93	Missing in isoform 3.		VSP_017852
	Alternative sequence	1	1	M → MAWHGETYCLIGGYRVYGDA PLPTPAKAEQEEKPVPRRAP KRQRVQEESDQDLGCPGAKV PRLKLKHGGKGLSRPSSVPA CSALSKM in isoform 2.		VSP_017853
	Alternative sequence	176 – 179	4	ALNS → VKWIYSG in isoform 2.		VSP_017854
	Alternative sequence	334 – 340	7	DHFDHIR → EKGQQKHQFTPPRDTHFV in isoform 2.		VSP_017855
Experimental info
	Sequence conflict	78	1	A → T in BAE42354. Ref.2
	Sequence conflict	89	1	D → G in BAE42559. Ref.2
	Sequence conflict	99	1	R → G in BAE42559. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 0790B97009F5D41F	FASTA	478	52,664
	10 20 30 40 50 60 MSLTGLKGHW VLGHGLSVFL LVLLLLGPSQ PLIWTQTKPG FSGASTTSSI PRALTKPDIS 70 80 90 100 110 120 SIPTTPGNPN FPDLRDRARA LMQEFPLIDG HNDMPLVLRQ FYQNGLQDAN LRNFTHGQTS 130 140 150 160 170 180 LDRLKDGLVG AQFWSAYVPC QTQDRDALRL TLEQIDLIRR ICASYSELEL VTSVKALNST 190 200 210 220 230 240 QKLACLIGVE GGHSLDNSLA VLRSFYLLGV RYLTLTHTCN TPWAETSSKG VHAFYSSVTG 250 260 270 280 290 300 LTSFGEKVVA EMNRLGMMVD LSHVSDAAAR RALEVSQAPV IFSHSAARAV CPNARNLPDD 310 320 330 340 350 360 LLQLLKKNGG IVMVTFSVGV LPCNPLANVS TVADHFDHIR SVIGSEFIGI GGDYDGTKQF 370 380 390 400 410 420 PQGLEDVSTY PVLIEELLRR GWNEQELQGI LRGNLLRVFR QVEQVRDKSK WQSPLEDMIP 430 440 450 460 470 EEQLDSACHS ALRPQKQHPE KNQPETPEYH ILKFSHSKSS PHIVPSLAIV ATLLGLIV
	Isoform 2 [UniParc]. Checksum: 253DC762000875A4	FASTA	578	63,675
	10 20 30 40 50 60 MAWHGETYCL IGGYRVYGDA PLPTPAKAEQ EEKPVPRRAP KRQRVQEESD QDLGCPGAKV 70 80 90 100 110 120 PRLKLKHGGK GLSRPSSVPA CSALSKMSLT GLKGHWVLGH GLSVFLLVLL LLGPSQPLIW 130 140 150 160 170 180 TQTKPGFSGA STTSSIPRAL TKPDISSIPT TPGNPNFPDL RDRARALMQE FPLIDGHNDM 190 200 210 220 230 240 PLVLRQFYQN GLQDANLRNF THGQTSLDRL KDGLVGAQFW SAYVPCQTQD RDALRLTLEQ 250 260 270 280 290 300 IDLIRRICAS YSELELVTSV KVKWIYSGTQ KLACLIGVEG GHSLDNSLAV LRSFYLLGVR 310 320 330 340 350 360 YLTLTHTCNT PWAETSSKGV HAFYSSVTGL TSFGEKVVAE MNRLGMMVDL SHVSDAAARR 370 380 390 400 410 420 ALEVSQAPVI FSHSAARAVC PNARNLPDDL LQLLKKNGGI VMVTFSVGVL PCNPLANVST 430 440 450 460 470 480 VAEKGQQKHQ FTPPRDTHFV SVIGSEFIGI GGDYDGTKQF PQGLEDVSTY PVLIEELLRR 490 500 510 520 530 540 GWNEQELQGI LRGNLLRVFR QVEQVRDKSK WQSPLEDMIP EEQLDSACHS ALRPQKQHPE 550 560 570 KNQPETPEYH ILKFSHSKSS PHIVPSLAIV ATLLGLIV
	Isoform 3 [UniParc]. Checksum: D28E45A1A5169543	FASTA	385	42,667
	10 20 30 40 50 60 MPLVLRQFYQ NGLQDANLRN FTHGQTSLDR LKDGLVGAQF WSAYVPCQTQ DRDALRLTLE 70 80 90 100 110 120 QIDLIRRICA SYSELELVTS VKALNSTQKL ACLIGVEGGH SLDNSLAVLR SFYLLGVRYL 130 140 150 160 170 180 TLTHTCNTPW AETSSKGVHA FYSSVTGLTS FGEKVVAEMN RLGMMVDLSH VSDAAARRAL 190 200 210 220 230 240 EVSQAPVIFS HSAARAVCPN ARNLPDDLLQ LLKKNGGIVM VTFSVGVLPC NPLANVSTVA 250 260 270 280 290 300 DHFDHIRSVI GSEFIGIGGD YDGTKQFPQG LEDVSTYPVL IEELLRRGWN EQELQGILRG 310 320 330 340 350 360 NLLRVFRQVE QVRDKSKWQS PLEDMIPEEQ LDSACHSALR PQKQHPEKNQ PETPEYHILK 370 380 FSHSKSSPHI VPSLAIVATL LGLIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two additional members of the membrane-bound dipeptidase family." Habib G.M., Shi Z.-Z., Cuevas A.A., Lieberman M.W. FASEB J. 17:1313-1315(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION. Strain: C57BL/6. Tissue: Heart, Lung and Spleen.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Strain: C57BL/6J and NOD. Tissue: Dendritic cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF488552 mRNA. Translation: AAP84986.1. AK089244 mRNA. Translation: BAC40810.1. AK155417 mRNA. Translation: BAE33255.1. AK170094 mRNA. Translation: BAE41559.1. AK170970 mRNA. Translation: BAE42149.1. AK171044 mRNA. Translation: BAE42209.1. AK171122 mRNA. Translation: BAE42264.1. AK171155 mRNA. Translation: BAE42280.1. AK171196 mRNA. Translation: BAE42306.1. AK171268 mRNA. Translation: BAE42354.1. AK171503 mRNA. Translation: BAE42494.1. AK171606 mRNA. Translation: BAE42559.1.
RefSeq	NP_795887.2. NM_176913.3. XP_006531142.1. XM_006531079.1. XP_006531143.1. XM_006531080.1.
UniGene	Mm.248357.
3D structure databases
ProteinModelPortal	Q8C255.
SMR	Q8C255. Positions 74-430.
ModBase	Search...
MobiDB	Search...
Protein family/group databases
MEROPS	M19.004.
Proteomic databases
PaxDb	Q8C255.
PRIDE	Q8C255.
Protocols and materials databases
DNASU	319446.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034373; ENSMUSP00000034373; ENSMUSG00000053687. [Q8C255-1] ENSMUST00000081998; ENSMUSP00000080659; ENSMUSG00000053687. [Q8C255-2] ENSMUST00000117555; ENSMUSP00000113877; ENSMUSG00000053687. [Q8C255-3]
GeneID	319446.
KEGG	mmu:319446.
UCSC	uc009nev.1. mouse. [Q8C255-3] uc009ney.1. mouse. [Q8C255-2]
Organism-specific databases
CTD	64174.
MGI	MGI:2442042. Dpep2.
Phylogenomic databases
eggNOG	COG2355.
GeneTree	ENSGT00390000017920.
HOGENOM	HOG000072016.
HOVERGEN	HBG002339.
OMA	IEATHRQ.
OrthoDB	EOG7SJD4N.
PhylomeDB	Q8C255.
TreeFam	TF324523.
Gene expression databases
Bgee	Q8C255.
CleanEx	MM_DPEP2. MM_MBD2.
Genevestigator	Q8C255.
Family and domain databases
InterPro	IPR028531. Dpep2. IPR000180. Renal_dipep_AS. IPR008257. Renal_dipep_fam. [Graphical view]
PANTHER	PTHR10443. PTHR10443. 1 hit. PTHR10443:SF15. PTHR10443:SF15. 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
NextBio	394746.
PRO	Q8C255.
SOURCE	Search...

Entry information

Entry name

DPEP2_MOUSE

Accession

Primary (citable) accession number: Q8C255
Secondary accession number(s): Q3TAV9 , Q3TBF7, Q3TBK3, Q3TBM9, Q7TQ53

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	March 1, 2003
Last modified:	April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program