Reviewed, UniProtKB/Swiss-Prot Q9DBT5 (AMPD2_MOUSE)

Names and origin

Protein names

Recommended name:
    AMP deaminase 2
    EC=3.5.4.6
Alternative name(s):
    AMP deaminase isoform L

Gene names

Name:

Ampd2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	AMP deaminase plays a critical role in energy metabolism By similarity.
Catalytic activity	AMP + H2O = IMP + NH3.
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	purine base metabolic process Inferred from electronic annotation. Source: InterPro purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	AMP deaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 798	798	AMP deaminase 2		PRO_0000194408
Sites
	Active site	398	1	Potential
	Active site	608	1	Potential
	Active site	684	1	Potential
	Active site	685	1	Potential
Amino acid modifications
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	37	1	Phosphoserine By similarity
	Modified residue	64	1	Phosphotyrosine Ref.4
	Modified residue	70	1	Phosphoserine By similarity
	Modified residue	87	1	Phosphoserine Ref.6
	Modified residue	109	1	Phosphoserine By similarity
	Modified residue	111	1	Phosphoserine Ref.5
	Modified residue	414	1	Phosphotyrosine By similarity
	Modified residue	420	1	Phosphoserine By similarity
	Modified residue	436	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9DBT5-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2BC4F37E4006C7D5	FASTA	798	92,024
	10 20 30 40 50 60 MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF SRSLAESELR 70 80 90 100 110 120 SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA KQDFLKTDSD SDLQLYKEQG 130 140 150 160 170 180 EGQGDRGLWE RDVVLEREFQ RVIISGEEKC GVPFTDLLDA AKSVVRALFI REKYMALSLQ 190 200 210 220 230 240 SFCPTTRRYL QQLAEKPLET RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG 250 260 270 280 290 300 LGLRMVRGVV HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ 310 320 330 340 350 360 YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL LRFIKRAMKR 370 380 390 400 410 420 HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD RNTFHRFDKF NAKYNPIGES 430 440 450 460 470 480 VLREIFIKTD NKISGKYFAH IIKEVMADLE ESKYQNAELR LSIYGRSRDE WDKLARWAVN 490 500 510 520 530 540 HKVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH 550 560 570 580 590 600 VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH 610 620 630 640 650 660 TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI AMSPLSNNSL 670 680 690 700 710 720 FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIATQVWKLS SCDMCELARN 730 740 750 760 770 780 SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV GYRYETLCQE LALITQAVQS 790 EMLETIPEEV GIVMSPGP

References

[1]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Lung.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[4]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, MASS SPECTROMETRY. Tissue: Mast cell.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK004759 mRNA. Translation: BAB23540.1. AK169980 mRNA. Translation: BAE41495.1. AL671854 Genomic DNA. Translation: CAM27248.1. BC016662 mRNA. Translation: AAH16662.2. Different initiation. BC049119 mRNA. Translation: AAH49119.1.
IPI	IPI00406639.
RefSeq	NP_083055.1.
UniGene	Mm.274335
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9DBT5.
PTM databases
PhosphoSite	Q9DBT5.
Proteomic databases
PRIDE	Q9DBT5.
Genome annotation databases
Ensembl	ENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889; Mus musculus. [Genome view] ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889; Mus musculus. [Genome view] ENSMUST00000106668; ENSMUSP00000102279; ENSMUSG00000027889; Mus musculus. [Genome view]
GeneID	109674.
KEGG	mmu:109674.
UCSC	uc008qxz.1. mouse.
Organism-specific databases
CTD	109674.
MGI	MGI:88016. Ampd2.
Phylogenomic databases
HOGENOM	Q9DBT5.
HOVERGEN	Q9DBT5.
Enzyme and pathway databases
BRENDA	3.5.4.6. 244.
Gene expression databases
ArrayExpress	Q9DBT5.
Bgee	Q9DBT5.
CleanEx	MM_AMPD2.
Genevestigator	Q9DBT5.
GermOnline	ENSMUSG00000027889. Mus musculus.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase. IPR006329. AMP_deaminase. IPR016297. AMP_deaminase_met. [Graphical view]
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
PIRSF	PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMs	TIGR01429. AMP_deaminase. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	362553.
SOURCE	Search...

Entry information

Entry name

AMPD2_MOUSE

Accession

Primary (citable) accession number: Q9DBT5
Secondary accession number(s): A2AE28, Q91YI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	June 1, 2001
Last modified:	October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)