PROTEIN SEQUENCE OF 2-101 (ISOFORM ACYA), PROTEIN SEQUENCE OF 4-101 (ISOFORM ACYB), AND ACETYLATION OF N-TERMINUS.
TISSUE=Brain, and Testis;
PubMed=1664426 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno Y., Kanesaka Y., Fujita H., Minowa O., Shiokawa H.;
"The primary structure of two molecular species of porcine organ-common type acylphosphatase.";
J. Biochem. 110:790-794(1991).

Comments

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

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation. It is uncertain whether isoform ACYA is produced by alternative initiation or another biological event.

Name	ACYB
Isoform ID	P24540-1
This is the isoform sequence displayed in this entry.

Name	ACYA
Isoform ID	P24540-2
Note: Initiator methionine is removed. Contains an N-acetylalanine at position 2.
Features which should be applied to build the isoform sequence: VSP_026024.

TISSUE SPECIFICITY: Organ-common type isozyme is found in many different tissues.
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

3D structure databases

HSSP

P41500; 2ACY. [HSSP ENTRY / PDB]

SMR

P24540; 4-101.

ModBase

P24540.

Ontologies

GO:0003998;	Molecular function: acylphosphatase activity (inferred from electronic annotation from InterPro).
QuickGo view.

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).

ProtoNet

P24540.

Phylogenomic databases

HOVERGEN

P24540; -.

Other

UniRef

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

Keywords

Acetylation; Alternative initiation; Direct protein sequencing; Hydrolase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed; in isoform ACYB.`
`CHAIN`	`2 101`	`100`	`Acylphosphatase-1.`	`PRO_0000158537`
`DOMAIN`	`11 101`	`91`	`Acylphosphatase-like.`
`ACT_SITE`	`26 26`		`Potential.`
`ACT_SITE`	`44 44`		`Potential.`
`MOD_RES`	`2 2`		`N-acetylserine; in isoform ACYB.`
`VAR_SEQ`	`1 2`		`Missing (in isoform ACYA).`	`VSP_026024`

Sequence information

Length: 101 AA [This is the length of the unprocessed precursor]

Molecular weight: 11427 Da [This is the MW of the unprocessed precursor]

CRC64: F707C03DEE1BF18A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSMAEGDTLI SVDYEVFGKV QGVFFRKYTQ AEGKKLGLVG WVQNTDQGTV QGQLQGPTSK 

        70         80         90        100 
VRHMQEWLET RGSPKSHIDR ASFNNEKVIS KLDYSDFQIV K

P24540 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