Acp5
entrez
25732
canonical
uniprot
P29288
canonical
ensembl
ENSRNOG00000046261
resolver
ensp
ENSRNOP00000066364
resolver
ensp
ENSRNOP00000074001
resolver
enst
ENSRNOT00000092200
resolver
genesymbol
Acp5
resolver
uniprot
A0A0G2K6Z6
resolver
uniprot_entry
A0A0G2K6Z6_RAT
resolver
uniprot_entry
PPA5_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Not inhibited by L(+)-tartrate (By similarity). Synthesized as a single chain proenzyme, with low enzymatic activity. Proteolytic cleavage converts ACP5 into a more active form (PubMed:10493912, PubMed:15929988). {ECO:0000250|UniProtKB:P13686, ECO:0000269|PubMed:10493912, ECO:0000269|PubMed:15929988}.
uniprot
proteins
amino_acid_sequence
MDTWMVLLGLQILLLPLLAHCTAPASTLRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQIMGADFIMSLGDNFYFTGVHDANDKRFQETFEDVFSDRALRNIPWYVLAGNHDHLGNVSAQIAYSKISKRWNFPSPYYRLRFKVPRSNITVAIFMLDTVMLCGNSDDFVSQQPEMPRDLGVARTQLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLAAYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSVRHQRKVPNGYLRFHYGSEDSLGGFTYVEIGSKEMSITYVEASGKSLFKTSLPRRPRP
uniprot
proteins
ec_number
3.1.3.2
uniprot
proteins
function
FUNCTION: Functions as a binuclear Fe(III)-Fe(II) acid phosphatase that hydrolyzes phosphate esters to alcohols and phosphate under acidic conditions (PubMed:11560512, PubMed:15929988, PubMed:19854170, PubMed:8195113). Dephosphorylates a broad range of substrates, including adenosine 5'-diphosphate (ADP), adenosine 5'-triphosphate (ATP), as well as larger phosphoproteins such as osteopontin (SPP1), a highly phosphorylated bone matrix protein, bone sialoprotein (IBSP) and synthetic compounds such as para-nitrophenyl phosphate (p-NPP) (PubMed:11560512, PubMed:15929988, PubMed:19854170, PubMed:8195113). Through the dephosphorylation of bone matrix proteins, plays a crucial role in normal cartilage mineralization during skeletal development and in maintaining and remodeling bone integrity in adults (PubMed:19854170, PubMed:8195113). Promotes osteoclast migration by dephosphorylating SPP1, which binds osteoclasts to the bone matrix (PubMed:19854170). Also involved in immune regulation and macrophage function, contributes to the breakdown of internalized pathogens within lysosomes (By similarity). Regulates immune cell recruitment during infection, partly via interaction with SPP1 (By similarity). The uncleaved form (isoform 5a) functions primarily in immune regulation rather than bone resorption. May contribute to the removal of mannose-6-phosphate (Man6P) from lysosomal proteins after their delivery to lysosomes, acting in concert with ACP2 (By similarity). {ECO:0000250|UniProtKB:Q05117, ECO:0000269|PubMed:11560512, ECO:0000269|PubMed:15929988, ECO:0000269|PubMed:19854170, ECO:0000269|PubMed:8195113}.
uniprot
proteins
mass_dalton
36726
uniprot
proteins
mutagenesis
MUTAGEN 166; /note="S->A: Increases acid phosphatase activity."; /evidence="ECO:0000269|PubMed:15929988"; MUTAGEN 167; /note="D->A,N,Q: Limited proteolysis. Increases acid phosphatase activity."; /evidence="ECO:0000269|PubMed:11560512"; MUTAGEN 172; /note="Q->A: Does not affect acid phosphatase activity."; /evidence="ECO:0000269|PubMed:15929988"; MUTAGEN 173; /note="Q->A: Increases acid phosphatase activity."; /evidence="ECO:0000269|PubMed:15929988
uniprot
proteins
post_translational_modification
PTM: Produced as a low-activity single-chain proenzyme and becomes activated through proteolytic cleavage of a surface loop by lysosomal, intracellular, or secreted proteases. This cleavage generates two subunits of approximately 16-17 kDa and 20-23 kDa that remain connected by disulfide bonds, forming the active catalytic form (isoform 5b). {ECO:0000269|PubMed:15929988}.
uniprot
proteins
pubmed
10388567
uniprot
proteins
pubmed
10438611
uniprot
proteins
pubmed
10493912
uniprot
proteins
pubmed
11560512
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15929988
uniprot
proteins
pubmed
1722212
uniprot
proteins
pubmed
1830446
uniprot
proteins
pubmed
19854170
uniprot
proteins
pubmed
8195113
uniprot
proteins
sequence_length
327
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q05117}. Secreted {ECO:0000250|UniProtKB:P13686}. Note=The uncleaved form (isoform 5a) is secreted by macrophage and dendritic cell. The cleaved form (isoform 5b) is secreted by osteoclasts. {ECO:0000250|UniProtKB:P13686}.
uniprot
proteins