Reviewed, UniProtKB/Swiss-Prot Q01432 (AMPD3_HUMAN)

Names and origin

Protein names

Recommended name:
    AMP deaminase 3
    EC=3.5.4.6
Alternative name(s):
    AMP deaminase isoform E
    Erythrocyte AMP deaminase

Gene names

Name:

AMPD3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	767 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.
Catalytic activity	AMP + H2O = IMP + NH3.
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
Subunit structure	Homotetramer.
Tissue specificity	Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.
Involvement in disease	Defects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE) [MIM:102772]. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders. Ref.4 Ref.7 Ref.8 Ref.9
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	AMP catabolic process Traceable author statement. Source: ProtInc 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 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1B (identifier: Q01432-1)

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 1A (identifier: Q01432-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM
     208-767: Missing.

Isoform 1C (identifier: Q01432-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM
     652-767: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 767	767	AMP deaminase 3		PRO_0000194410
Sites
	Active site	377	1	Potential
	Active site	587	1	Potential
	Active site	663	1	Potential
	Active site	664	1	Potential
Natural variations
	Alternative sequence	1	1	M → MALSSEPAEM in isoform 1A.		VSP_001275
	Alternative sequence	1	1	M → MEPGSAEM in isoform 1C.		VSP_001276
	Alternative sequence	208 – 767	560	Missing in isoform 1A.		VSP_001277
	Alternative sequence	652 – 767	116	Missing in isoform 1C.		VSP_001278
	Natural variant	185	1	R → W: dbSNP rs11042836.		VAR_033499
	Natural variant	310	1	N → K in AMPDDE. Ref.7		VAR_042606
	Natural variant	311	1	V → L in AMPDDE. Ref.8		VAR_042607
	Natural variant	320	1	A → V in AMPDDE. Ref.7		VAR_042608
	Natural variant	324	1	M → T in AMPDDE. Ref.7		VAR_042609
	Natural variant	331	1	R → C in AMPDDE. Ref.7		VAR_042610
	Natural variant	402	1	R → C in AMPDDE. Ref.7		VAR_042611
	Natural variant	450	1	W → R in AMPDDE. Ref.7 Ref.9		VAR_042612
	Natural variant	455	1	Y → H: dbSNP rs36003153.		VAR_042613
	Natural variant	573	1	R → C in AMPDDE; enzyme inactive. dbSNP rs3741040. Ref.4		VAR_009881
	Natural variant	585	1	P → L in AMPDDE. Ref.7		VAR_042614
	Natural variant	712	1	Q → P in AMPDDE. Ref.9		VAR_042615

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1B [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 2E0A2C629003B98C	FASTA	767	88,812
	10 20 30 40 50 60 MPRQFPKLNI SEVDEQVRLL AEKVFAKVLR EEDSKDALSL FTVPEDCPIG QKEAKERELQ 70 80 90 100 110 120 KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PPQQDWKGPP AASPAMSPTT PVVTGATSLP 130 140 150 160 170 180 TPAPYAMPEF QRVTISGDYC AGITLEDYEQ AAKSLAKALM IREKYARLAY HRFPRITSQY 190 200 210 220 230 240 LGHPRADTAP PEEGLPDFHP PPLPQEDPYC LDDAPPNLDY LVHMQGGILF VYDNKKMLEH 250 260 270 280 290 300 QEPHSLPYPD LETYTVDMSH ILALITDGPT KTYCHRRLNF LESKFSLHEM LNEMSEFKEL 310 320 330 340 350 360 KSNPHRDFYN VRKVDTHIHA AACMNQKHLL RFIKHTYQTE PDRTVAEKRG RKITLRQVFD 370 380 390 400 410 420 GLHMDPYDLT VDSLDVHAGR QTFHRFDKFN SKYNPVGASE LRDLYLKTEN YLGGEYFARM 430 440 450 460 470 480 VKEVARELEE SKYQYSEPRL SIYGRSPEEW PNLAYWFIQH KVYSPNMRWI IQVPRIYDIF 490 500 510 520 530 540 RSKKLLPNFG KMLENIFLPL FKATINPQDH RELHLFLKYV TGFDSVDDES KHSDHMFSDK 550 560 570 580 590 600 SPNPDVWTSE QNPPYSYYLY YMYANIMVLN NLRRERGLST FLFRPHCGEA GSITHLVSAF 610 620 630 640 650 660 LTADNISHGL LLKKSPVLQY LYYLAQIPIA MSPLSNNSLF LEYSKNPLRE FLHKGLHVSL 670 680 690 700 710 720 STDDPMQFHY TKEALMEEYA IAAQVWKLST CDLCEIARNS VLQSGLSHQE KQKFLGQNYY 730 740 750 760 KEGPEGNDIR KTNVAQIRMA FRYETLCNEL SFLSDAMKSE EITALTN
	Isoform 1A. Checksum: 77821100D9737811	FASTA	216	24,119
	10 20 30 40 50 60 MALSSEPAEM PRQFPKLNIS EVDEQVRLLA EKVFAKVLRE EDSKDALSLF TVPEDCPIGQ 70 80 90 100 110 120 KEAKERELQK ELAEQKSVET AKRKKSFKMI RSQSLSLQMP PQQDWKGPPA ASPAMSPTTP 130 140 150 160 170 180 VVTGATSLPT PAPYAMPEFQ RVTISGDYCA GITLEDYEQA AKSLAKALMI REKYARLAYH 190 200 210 RFPRITSQYL GHPRADTAPP EEGLPDFHPP PLPQED
	Isoform 1C. Checksum: 0FDFC779DC4996F2	FASTA	658	76,269
	10 20 30 40 50 60 MEPGSAEMPR QFPKLNISEV DEQVRLLAEK VFAKVLREED SKDALSLFTV PEDCPIGQKE 70 80 90 100 110 120 AKERELQKEL AEQKSVETAK RKKSFKMIRS QSLSLQMPPQ QDWKGPPAAS PAMSPTTPVV 130 140 150 160 170 180 TGATSLPTPA PYAMPEFQRV TISGDYCAGI TLEDYEQAAK SLAKALMIRE KYARLAYHRF 190 200 210 220 230 240 PRITSQYLGH PRADTAPPEE GLPDFHPPPL PQEDPYCLDD APPNLDYLVH MQGGILFVYD 250 260 270 280 290 300 NKKMLEHQEP HSLPYPDLET YTVDMSHILA LITDGPTKTY CHRRLNFLES KFSLHEMLNE 310 320 330 340 350 360 MSEFKELKSN PHRDFYNVRK VDTHIHAAAC MNQKHLLRFI KHTYQTEPDR TVAEKRGRKI 370 380 390 400 410 420 TLRQVFDGLH MDPYDLTVDS LDVHAGRQTF HRFDKFNSKY NPVGASELRD LYLKTENYLG 430 440 450 460 470 480 GEYFARMVKE VARELEESKY QYSEPRLSIY GRSPEEWPNL AYWFIQHKVY SPNMRWIIQV 490 500 510 520 530 540 PRIYDIFRSK KLLPNFGKML ENIFLPLFKA TINPQDHREL HLFLKYVTGF DSVDDESKHS 550 560 570 580 590 600 DHMFSDKSPN PDVWTSEQNP PYSYYLYYMY ANIMVLNNLR RERGLSTFLF RPHCGEAGSI 610 620 630 640 650 THLVSAFLTA DNISHGLLLK KSPVLQYLYY LAQIPIAMSP LSNNSLFLEY SKNPLREF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase." Yamada Y., Goto H., Ogasawara N. Biochim. Biophys. Acta 1171:125-128(1992) [PubMed: 1420359] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons." Mahnke-Zizelman D.K., Sabina R.L. J. Biol. Chem. 267:20866-20877(1992) [PubMed: 1400401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte.
[3]	"Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing." Mahnke-Zizelman D.K., Eddy R., Shows T.B., Sabina R.L. Biochim. Biophys. Acta 1306:75-92(1996) [PubMed: 8611627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[4]	"A point mutation responsible for human erythrocyte AMP deaminase deficiency." Yamada Y., Goto H., Ogasawara N. Hum. Mol. Genet. 3:331-334(1994) [PubMed: 8004104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AMPDDE CYS-573.
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B). Tissue: Testis.
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations." Yamada Y., Goto H., Murase T., Ogasawara N. Hum. Mol. Genet. 3:2243-2245(1994) [PubMed: 7881427] [Abstract] Cited for: VARIANTS AMPDDE LYS-310; VAL-320; THR-324; CYS-331; CYS-402; ARG-450 AND LEU-585.
[8]	"Gene mutations responsible for human erythrocyte AMP deaminase deficiency in Poles." Yamada Y., Makarewicz W., Goto H., Nomura N., Kitoh H., Ogasawara N. Adv. Exp. Med. Biol. 431:347-350(1998) [PubMed: 9598089] [Abstract] Cited for: VARIANT AMPDDE LEU-311.
[9]	"A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3." Yamada Y., Goto H., Wakamatsu N., Ogasawara N. Hum. Mutat. 17:78-78(2001) [PubMed: 11139257] [Abstract] Cited for: VARIANTS AMPDDE ARG-450 AND PRO-712.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D12775 mRNA. Translation: BAA02240.1. M84720 mRNA. Translation: AAA58365.1. M84721 mRNA. Translation: AAA58366.1. M84722 mRNA. Translation: AAA58367.1. U29926 , U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60410.1. U29926 , U29912, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60408.1. U29926 , U29927, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60409.1. D31646 Genomic DNA. Translation: BAA06505.1. AK302970 mRNA. Translation: BAH13863.1. CH471064 Genomic DNA. Translation: EAW68569.1.
IPI	IPI00300573. IPI00411384. IPI00941882.
PIR	S68146. S68147.
RefSeq	NP_000471.1. NP_001020560.1. NP_001020561.1.
UniGene	Hs.501890
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q01432.
PTM databases
PhosphoSite	Q01432.
Proteomic databases
PRIDE	Q01432.
Genome annotation databases
Ensembl	ENST00000256183; ENSP00000256183; ENSG00000133805; Homo sapiens. [Genome view] ENST00000396553; ENSP00000379801; ENSG00000133805; Homo sapiens. [Genome view] ENST00000396554; ENSP00000379802; ENSG00000133805; Homo sapiens. [Genome view] ENST00000431080; ENSP00000389509; ENSG00000133805; Homo sapiens. [Genome view] ENST00000444303; ENSP00000396000; ENSG00000133805; Homo sapiens. [Genome view]
GeneID	272.
KEGG	hsa:272.
UCSC	uc001min.1. human. uc009yfx.1. human.
Organism-specific databases
CTD	272.
GeneCards	GC11P010428.
H-InvDB	HIX0036031.
HGNC	HGNC:470. AMPD3.
MIM	102772. gene+phenotype.
Orphanet	45. Adenosine monophosphate deaminase deficiency.
PharmGKB	PA24778.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q01432.
HOVERGEN	Q01432.
Enzyme and pathway databases
BRENDA	3.5.4.6. 247.
Reactome	REACT_1698. Metablism of nucleotides.
Gene expression databases
ArrayExpress	Q01432.
Bgee	Q01432.
CleanEx	HS_AMPD3.
Genevestigator	Q01432.
GermOnline	ENSG00000133805. Homo sapiens.
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	1073.
SOURCE	Search...

Entry information

Entry name

AMPD3_HUMAN

Accession

Primary (citable) accession number: Q01432
Secondary accession number(s): B7Z877

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	October 13, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.