[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 3-423. PubMed=2059337 [NCBI, ExPASy, EBI, Israel, Japan] Geier C., von Figura K., Pohlmann R.; "Molecular cloning of the mouse lysosomal acid phosphatase."; Biol. Chem. Hoppe-Seyler 372:301-304(1991).

Comments

CATALYTIC ACTIVITY: A phosphate monoester + H₂O = an alcohol + phosphate.
SUBCELLULAR LOCATION: Lysosome membrane; Single-pass membrane protein; Lumenal side (By similarity). Lysosome lumen (By similarity). Note=The soluble form arises by proteolytic processing of the membrane-bound form (By similarity).
PTM: The membrane-bound form is converted to the soluble form by sequential proteolytic processing. First, the C-terminal cytoplasmic tail is removed. Cleavage by a lysosomal protease releases the soluble form in the lysosome lumen (By similarity).
SIMILARITY: Belongs to the histidine acid phosphatase family.

Copyright

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

Cross-references

Sequence databases

EMBL

BC023343; AAH23343.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57199; CAA40485.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S14742; S14742.

NP_031413.1; -.

3D structure databases

HSSP

P15309; 1ND5. [HSSP ENTRY / PDB]

ModBase

P24638.

Organism-specific databases

MGI

MGI:87882; Acp2.

Gene expression databases

ArrayExpress

P24638; -.

CleanEx

MM_ACP2; -.

GermOnline

ENSMUSG00000002103; Mus musculus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0043202;	Cellular component: lysosomal lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005765;	Cellular component: lysosomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003993;	Molecular function: acid phosphatase activity (inferred from direct assay from MGI).
GO:0007040;	Biological process: lysosome organization (inferred from mutant phenotype from MGI).
GO:0001501;	Biological process: skeletal system development (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR000560; Histidine_acid_Pase.
Graphical view of domain structure.

Pfam

PF00328; Acid_phosphat_A; 1.
Pfam graphical view of domain structure.

PROSITE

PS00616; HIS_ACID_PHOSPHAT_1; 1.
PS00778; HIS_ACID_PHOSPHAT_2; 1.

ProtoNet

P24638.

Genome annotation databases

Ensembl

ENSMUSG00000002103; Mus musculus. [Contig view]

GeneID

11432; -.

KEGG

mmu:11432; -.

Phylogenomic databases

HOGENOM

P24638; -.

HOVERGEN

P24638; -.

Other

NextBio

278716; -.

SOURCE

Acp2; Mus musculus.

UniRef

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

Keywords

Glycoprotein; Hydrolase; Lysosome; Membrane; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`
`CHAIN`	`31 423`	`393`	`Lysosomal acid phosphatase.`	`PRO_0000023961`
`TOPO_DOM`	`31 381`	`351`	`Lumenal (Potential).`
`TRANSMEM`	`382 402`	`21`	`Potential.`
`TOPO_DOM`	`403 423`	`21`	`Cytoplasmic (Potential).`
`ACT_SITE`	`42 42`		`Nucleophile (By similarity).`
`ACT_SITE`	`287 287`		`Proton donor (By similarity).`
`CARBOHYD`	`92 92`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`133 133`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`167 167`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`177 177`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`191 191`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`197 197`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`267 267`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`322 322`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`331 331`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`374 374`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`159 370`		`By similarity.`
`DISULFID`	`212 310`		`By similarity.`
`DISULFID`	`345 349`		`By similarity.`
`CONFLICT`	`131 131`		`N -> S (in Ref. 2; CAA40485).`

Sequence information

Length: 423 AA [This is the length of the unprocessed precursor]

Molecular weight: 48509 Da [This is the MW of the unprocessed precursor]

CRC64: AFD7A5C90A4F2AF4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGRQTGWSQ AALLQFLLGM CLTVMPPIQA RSLRFVTLLY RHGDRSPVKT YPKDPYQEEK 

        70         80         90        100        110        120 
WPQGFGQLTK EGMLQHWELG QALRQRYHGF LNTSYHRQEV YVRSTDFDRT LMSAEANLAG 

       130        140        150        160        170        180 
LFPPNEVQHF NPNISWQPIP VHTVPITEDR LLKFPLGPCP RYEQLQNETR QTPEYQNRSI 

       190        200        210        220        230        240 
QNAQFLNMVA NETGLTNVTL ETIWNVYDTL FCEQTHGLLL PPWASPQTVQ RLSQLKDFSF 

       250        260        270        280        290        300 
LFLFGIHEQV QKARLQGGVL LAQILKNLTL MATTSQFPKL LVYSAHDTTL VALQMALNVY 

       310        320        330        340        350        360 
NGKQAPYASC HIFELYQEDN GNFSVEMYFR NDSKKAPWPL ILPGCPHRCP LQDFLRLTEP 

       370        380        390        400        410        420 
VIPKDWQKEC QLANDTADTE VIVALAVCGS ILFLLIVLLL TILFRMQAQP PGYHHVADRE 


DHA

P24638 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