Reviewed, UniProtKB/Swiss-Prot P23109 (AMPD1_HUMAN)

Names and origin

Protein names

Recommended name:
    AMP deaminase 1
    EC=3.5.4.6
Alternative name(s):
    Myoadenylate deaminase
    AMP deaminase isoform M

Gene names

Name:

AMPD1

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	747 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 AMPD1 are the cause of adenosine monophosphate deaminase deficiency muscle type (AMPDDM) [MIM:102770]. AMPDDM is a metabolic disorder resulting in exercise-related myopathy. It is characterized by exercise-induced muscle aches, cramps, and early fatigue. Ref.5
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Molecular function	Hydrolase
Technical term	Complete proteome
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 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 747	747	AMP deaminase 1		PRO_0000194403
Sites
	Active site	363	1	By similarity
	Active site	573	1	By similarity
	Active site	649	1	By similarity
	Active site	650	1	By similarity
Natural variations
	Natural variant	22	1	E → K: dbSNP rs2273268.		VAR_048860
	Natural variant	48	1	P → L Polymorphism; activity comparable to wild-type. Ref.4		VAR_013270
	Natural variant	388	1	R → W in AMPDDM; loss of activity. Ref.5		VAR_013271
	Natural variant	425	1	R → H in AMPDDM; loss of activity. Ref.5		VAR_013272
	Natural variant	633	1	P → H in a colorectal cancer sample; somatic mutation. Ref.6		VAR_035801

Sequences

	Sequence		Length	Mass (Da)
	P23109-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 1E15EBEE98B95763	FASTA	747	86,490
	10 20 30 40 50 60 MPLFKLPAEE KQIDDAMRNF AEKVFASEVK DEGGRQEISP FDVDEICPIS HHEMQAHIFH 70 80 90 100 110 120 LETLSTSTEA RRKKRFQGRK TVNLSIPLSE TSSTKLSHID EYISSSPTYQ TVPDFQRVQI 130 140 150 160 170 180 TGDYASGVTV EDFEIVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEAWVANESF 190 200 210 220 230 240 YPVFTPPVKK GEDPFRTDNL PENLGYHLKM KDGVVYVYPN EAAVSKDEPK PLPYPNLDTF 250 260 270 280 290 300 LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV 310 320 330 340 350 360 DTHIHAAACM NQKHLLRFIK KSYQIDADRV VYSTKEKNLT LKELFAKLKM HPYDLTVDSL 370 380 390 400 410 420 DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVEAKYQ 430 440 450 460 470 480 HAEPRLSIYG RSPDEWSKLS SWFVCNRIHC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE 490 500 510 520 530 540 NIFMPVFEAT INPQADPELS VFLKHITGFD SVDDESKHSG HMFSSKSPKP QEWTLEKNPS 550 560 570 580 590 600 YTYYAYYMYA NIMVLNSLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD DISHGLNLKK 610 620 630 640 650 660 SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP 670 680 690 700 710 720 LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKVKF LGDNYLEEGP AGNDIRRTNV 730 740 AQIRMAYRYE TWCYELNLIA EGLKSTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the human and rat myoadenylate deaminase genes." Sabina R.L., Morisaki T., Clarke P., Eddy R., Shows T.B., Morton C.C., Holmes E.W. J. Biol. Chem. 265:9423-9433(1990) [PubMed: 2345176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular analysis of the myoadenylate deaminase deficiencies." Sabina R.L., Fishbein W.N., Pezeshkpour G., Clarke P.R., Holmes E.W. Neurology 42:170-179(1992) [PubMed: 1370861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Molecular basis of AMP deaminase deficiency in skeletal muscle." Morisaki T., Gross M., Morisaki H., Pongratz D., Zoellner N., Holmes E.W. Proc. Natl. Acad. Sci. U.S.A. 89:6457-6461(1992) [PubMed: 1631143] [Abstract] Cited for: VARIANT LEU-48.
[5]	"First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient." Morisaki H., Higuchi I., Abe M., Osame M., Morisaki T. Hum. Mutat. 16:467-472(2000) [PubMed: 11102975] [Abstract] Cited for: VARIANTS AMPDDM TRP-388 AND HIS-425.
[6]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-633.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	M37931 , M37920, M37921, M37922, M37923, M37924, M37927, M37928, M37929, M37930 Genomic DNA. Translation: AAG24258.1. M60092 mRNA. Translation: AAA57281.1. AL096773 Genomic DNA. Translation: CAI18830.1.
IPI	IPI00448879.
PIR	I39444.
RefSeq	NP_000027.1.
UniGene	Hs.89570
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P23109.
Proteomic databases
PRIDE	P23109.
Genome annotation databases
Ensembl	ENSG00000116748. Homo sapiens. [Contig view]
GeneID	270.
KEGG	hsa:270.
UCSC	uc001efe.1. human.
Organism-specific databases
GeneCards	GC01M114927.
H-InvDB	HIX0000913.
HGNC	HGNC:468. AMPD1.
MIM	102770. gene+phenotype.
Orphanet	45. Adenosine monophosphate deaminase deficiency.
PharmGKB	PA24776.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P23109.
Enzyme and pathway databases
BRENDA	3.5.4.6. 247.
Reactome	REACT_1698. Metablism of nucleotides.
Gene expression databases
ArrayExpress	P23109.
Bgee	P23109.
CleanEx	HS_AMPD1.
GermOnline	ENSG00000116748. 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
DrugBank	DB00131. Adenosine monophosphate.
NextBio	1061.
SOURCE	Search...

Entry information

Entry name

AMPD1_HUMAN

Accession

Primary (citable) accession number: P23109
Secondary accession number(s): Q5TF00

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	July 7, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)