[1]	PROTEIN SEQUENCE OF 2-99. TISSUE=Muscle; PubMed=6248536 [NCBI, ExPASy, EBI, Israel, Japan] Cappugi G., Manao G., Camici G., Ramponi G.; "The complete amino acid sequence of horse muscle acylphosphatase."; J. Biol. Chem. 255:6868-6874(1980).
[2]	STRUCTURE BY NMR OF ALPHA HELICES. DOI=10.1016/0022-2836(89)90377-X; PubMed=2538623 [NCBI, ExPASy, EBI, Israel, Japan] Saudek V., Atkinson R.A., Williams R.J.P., Ramponi G.; "Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy."; J. Mol. Biol. 205:229-239(1989).
[3]	STRUCTURE BY NMR OF BETA-STRUCTURES. DOI=10.1016/0022-2836(89)90263-5; PubMed=2547076 [NCBI, ExPASy, EBI, Israel, Japan] Saudek V., Wormald M.R., Williams R.J.P., Boyd J., Stefani M., Ramponi G.; "Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy."; J. Mol. Biol. 207:405-415(1989).
[4]	STRUCTURE BY NMR. DOI=10.1016/0022-2836(92)91005-A; PubMed=1313885 [NCBI, ExPASy, EBI, Israel, Japan] Pastore A., Saudek V., Ramponi G., Williams R.J.P.; "Three-dimensional structure of acylphosphatase. Refinement and structure analysis."; J. Mol. Biol. 224:427-440(1992).

Comments

FUNCTION: Its physiological role is not yet clear.
CATALYTIC ACTIVITY: An acylphosphate + H₂O = a carboxylate + phosphate.
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

A01015; QPHO.

3D structure databases

PDB

1APS; NMR; -; A=1-99.

[ExPASy / RCSB / EBI]

PDBsum

1APS; -.

ModBase

P00818.

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).

Other

Phylogenomic databases

HOVERGEN

P00818; -.

Other

LinkHub

P00818; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; 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_0000158541`
`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.`
`STRAND`	`7 15`	`9`
`HELIX`	`26 34`	`9`
`STRAND`	`37 41`	`5`
`STRAND`	`47 55`	`9`
`HELIX`	`56 64`	`9`
`STRAND`	`65 68`	`4`
`STRAND`	`72 74`	`3`
`STRAND`	`79 89`	`11`
`STRAND`	`92 98`	`7`

Sequence information

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

Molecular weight: 11148 Da [This is the MW of the unprocessed precursor]

CRC64: 911DAF1820A53790 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTARPLKSV DYEVFGRVQG VCFRMYAEDE ARKIGVVGWV KNTSKGTVTG QVQGPEEKVN 

        70         80         90 
SMKSWLSKVG SPSSRIDRTN FSNEKTISKL EYSNFSVRY

P00818 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