[1]	PROTEIN SEQUENCE OF 2-99. TISSUE=Skeletal muscle; PubMed=2993260 [NCBI, ExPASy, EBI, Israel, Japan] Kizaki T., Takasawa T., Mizuno Y., Shiokawa H.; "Amino acid sequence of acylphosphatase from rabbit skeletal muscle."; J. Biochem. 97:1155-1161(1985).
[2]	PROTEIN SEQUENCE OF 2-99. TISSUE=Skeletal muscle; DOI=10.1016/0003-9861(85)90565-X; PubMed=2994566 [NCBI, ExPASy, EBI, Israel, Japan] Manao G., Camici G., Cappugi G., Stefani M., Liguri G., Berti A., Ramponi G.; "Rabbit skeletal muscle acylphosphatase: the amino acid sequence of form Ra1."; Arch. Biochem. Biophys. 241:418-423(1985).

Comments

FUNCTION: Its physiological role is not yet clear.
CATALYTIC ACTIVITY: An acylphosphate + H₂O = a carboxylate + phosphate.
SUBUNIT: Monomer (RA1) and homodimer (RA3); disulfide linked.
SIMILARITY: Belongs to the acylphosphatase family.
SIMILARITY: Contains 1 acylphosphatase-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases
PIR	A91988; QPRB.
3D structure databases
HSSP	P00818; 1APS. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR	P00820; 2-99.
ModBase	P00820.
Family and domain databases
InterPro	IPR001792; Acylphosphatase. Graphical view of domain structure.
PANTHER	PTHR10029; Acylphosphatase; 1.
Pfam	PF00708; Acylphosphatase; 1. Pfam graphical view of domain structure.
PRINTS	PR00112; ACYLPHPHTASE.
ProDom	PD001884; Acylphosphatase; 1. [Domain structure / List of seq. sharing at least 1 domain]
PROSITE	PS00150; ACYLPHOSPHATASE_1; 1. PS00151; ACYLPHOSPHATASE_2; 1. PS51160; ACYLPHOSPHATASE_3; 1. PROSITE graphical view of domain structure (profiles).
BLOCKS	P00820.
ProtoNet	P00820.
Genome annotation databases
Ensembl	ENSOCUG00000015408; Oryctolagus cuniculus. [Contig view]
Phylogenomic databases
HOVERGEN	P00820; -.
Other
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Glutathionylation; Hydrolase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 99`	`98`	`Acylphosphatase-2.`	`PRO_0000158545`
`DOMAIN`	`9 99`	`91`	`Acylphosphatase-like.`
`ACT_SITE`	`24 24`		`Potential.`
`ACT_SITE`	`42 42`		`Potential.`
`MOD_RES`	`2 2`		`N-acetylserine.`
`MOD_RES`	`22 22`		`S-glutathionyl cysteine; alternate.`
`DISULFID`	`22 22`		`Interchain; alternate.`

Sequence information

Length: 99 AA [This is the length of the unprocessed precursor]

Molecular weight: 10992 Da [This is the MW of the unprocessed precursor]

CRC64: 1EB9AA7CF8F13620 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTAGPLKSV DYEVFGRVQG VCFRMYTEGE AKKIGVVGWV KNTSKGTVTG QVQGPEDKVN 

        70         80         90 
SMKSWLSKVG SPSSRIDRTN FSNEKTISKL EYSNFSIRY

P00820 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools