P10759 (AMPD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AMP deaminase 1
EC=3.5.4.6

Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase

Gene names

Name:

Ampd1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	747 AA.
Sequence status	Complete.
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.
Cofactor	Binds 1 zinc ion per subunit By similarity.
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.
Sequence similarities	Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	IMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway response to organic substance Inferred from direct assay PubMed 9730972. Source: RGD
Molecular_function	AMP deaminase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin heavy chain binding Inferred from direct assay PubMed 9730972. Source: RGD
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_0000194405
Regions
	Region	374 – 379	6	Substrate binding By similarity
	Region	650 – 653	4	Substrate binding By similarity
Sites
	Active site	594	1	Proton acceptor By similarity
	Metal binding	303	1	Zinc; catalytic By similarity
	Metal binding	305	1	Zinc; catalytic By similarity
	Metal binding	572	1	Zinc; catalytic By similarity
	Metal binding	649	1	Zinc; catalytic By similarity
	Binding site	305	1	Substrate By similarity
	Binding site	575	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10759 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: C8928B67F2DD9478	FASTA	747	86,432
	10 20 30 40 50 60 MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LREMQAHIFH 70 80 90 100 110 120 MENLSMSMDG RRKRRFQGRK TVNLSIPQSE TSSTKLSHIE EFISSSPTYE SVPDFQRVQI 130 140 150 160 170 180 TGDYASGVTV EDFEVVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEALVAIESF 190 200 210 220 230 240 YPVFTPPPKK GEDPFRREDL PANLGYHLKM KGGVIYIYPD EAAASRDEPK PYPYPNLDDF 250 260 270 280 290 300 LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV 310 320 330 340 350 360 DTHIHAAACM NQKHLLRFIK KSYHIDADRV VYSTKEKNLT LKELFAQLNM HPYDLTVDSL 370 380 390 400 410 420 DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVDAKYQ 430 440 450 460 470 480 HAEPRLSIYG RSPDEWSKLS SWFVGNRIYC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE 490 500 510 520 530 540 NIFLPVFEAT INPQTHPDLS VFLKHITGFD SVDDESKHSG HMFSSKSPKP EEWTMENNPS 550 560 570 580 590 600 YTYYAYYMYA NIMVLNCLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD NISHGLNLKK 610 620 630 640 650 660 SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP 670 680 690 700 710 720 LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKAKF LGNNYLEEGP VGNDIRRTNV 730 740 AQIRMAYRYE TWCYELNLIA EGLKSTE

References

[1]	"Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for tissue-specific and developmental regulation." Sabina R.L., Marquetant R., Desai N.M., Kaletha K., Holmes E.W. J. Biol. Chem. 262:12397-12400(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 536-548. Tissue: Muscle.
[2]	"A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5' splice donor site not present in the primary transcript of AMPD1." Mineo I., Clarke P.R., Sabina R.L., Holmes E.W. Mol. Cell. Biol. 10:5271-5278(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02811 mRNA. Translation: AAB54086.1. M58688 mRNA. Translation: AAA40726.1.
IPI	IPI00193319.
PIR	A27366.
RefSeq	NP_620231.1. NM_138876.1.
UniGene	Rn.9794.
3D structure databases
ProteinModelPortal	P10759.
ModBase	Search...
Proteomic databases
PaxDb	P10759.
PRIDE	P10759.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000025248; ENSRNOP00000025248; ENSRNOG00000018656.
GeneID	25028.
KEGG	rno:25028.
Organism-specific databases
CTD	270.
RGD	2109. Ampd1.
Phylogenomic databases
eggNOG	COG1816.
GeneTree	ENSGT00390000008190.
HOGENOM	HOG000092200.
HOVERGEN	HBG050494.
InParanoid	P10759.
KO	K01490.
OMA	NMTWMIQ.
OrthoDB	EOG402WRH.
Enzyme and pathway databases
UniPathway	UPA00591; UER00663.
Gene expression databases
Genevestigator	P10759.
GermOnline	ENSRNOG00000018656. Rattus norvegicus.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006329. AMP_deaminase. [Graphical view]
PANTHER	PTHR11359. PTHR11359. 1 hit.
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
NextBio	605167.

Entry information

Entry name

AMPD1_RAT

Accession

Primary (citable) accession number: P10759
Secondary accession number(s): P78501, Q6LDJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program