PROTEIN SEQUENCE OF 2-103.
TISSUE=Skeletal muscle;
DOI=10.1111/j.1432-1033.1983.tb07825.x; PubMed=6317387 [NCBI, ExPASy, EBI, Israel, Japan]
Camici G., Manao G., Cappugi G., Berti A., Stefani M., Liguri G., Ramponi G.;
"The primary structure of turkey muscle acylphosphatase.";
Eur. J. Biochem. 137:269-277(1983).

Comments

FUNCTION: Its physiological role is not yet clear.
CATALYTIC ACTIVITY: An acylphosphate + H₂O = a carboxylate + phosphate.
SUBUNIT: Monomer (TU1) or homodimer (TU3) in absence of reducing factors; 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	A01018; QPTK.
3D structure databases
HSSP	P00818; 1APS. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR	P00821; 11-103.
ModBase	P00821.
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	P00821.
ProtoNet	P00821.
Phylogenomic databases
HOVERGEN	P00821; -.
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`	`2 103`	`102`	`Acylphosphatase-2.`	`PRO_0000158549`
`DOMAIN`	`13 103`	`91`	`Acylphosphatase-like.`
`ACT_SITE`	`28 28`		`Potential.`
`ACT_SITE`	`46 46`		`Potential.`
`MOD_RES`	`2 2`		`N-acetylserine.`
`MOD_RES`	`26 26`		`S-glutathionyl cysteine; alternate.`
`DISULFID`	`26 26`		`Interchain; alternate.`

Sequence information

Length: 103 AA [This is the length of the unprocessed precursor]

Molecular weight: 11448 Da [This is the MW of the unprocessed precursor]

CRC64: 23D12EB987EC37C8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSALTKASGA LKSVDYEVFG RVQGVCFRMY TEEEARKLGV VGWVKNTRQG TVTGQVQGPE 

        70         80         90        100 
DKVNAMKSWL SKVGSPSSRI DRTNFSNEKE ISKLDFSGFS TRY

P00821 in FASTA format

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View entry in raw text format (no links)
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	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