ACP5
entrez
54
canonical
uniprot
P13686
canonical
ensembl
ENSG00000102575
resolver
ensp
ENSP00000218758
resolver
ensp
ENSP00000392374
resolver
ensp
ENSP00000464831
resolver
ensp
ENSP00000465127
resolver
ensp
ENSP00000465498
resolver
ensp
ENSP00000468685
resolver
ensp
ENSP00000468767
resolver
ensp
ENSP00000496973
resolver
ensp
ENSP00000497140
resolver
ensp
ENSP00000512173
resolver
ensp
ENSP00000512191
resolver
ensp
ENSP00000559725
resolver
ensp
ENSP00000614522
resolver
enst
ENST00000218758
resolver
enst
ENST00000412435
resolver
enst
ENST00000589792
resolver
enst
ENST00000590832
resolver
enst
ENST00000591319
resolver
enst
ENST00000592659
resolver
enst
ENST00000592828
resolver
enst
ENST00000648477
resolver
enst
ENST00000649386
resolver
enst
ENST00000695791
resolver
enst
ENST00000695811
resolver
enst
ENST00000889666
resolver
genesymbol
ACP5
resolver
hgnc
HGNC:124
resolver
uniprot
A8K3V2
resolver
uniprot
Q2TAB1
resolver
uniprot
Q6IAS6
resolver
uniprot
Q9UCJ5
resolver
uniprot
Q9UCJ6
resolver
uniprot
Q9UCJ7
resolver
uniprot_entry
PPA5_HUMAN
resolver
uniprot_sec
A8K3V2
resolver
uniprot_sec
Q2TAB1
resolver
uniprot_sec
Q6IAS6
resolver
uniprot_sec
Q9UCJ5
resolver
uniprot_sec
Q9UCJ6
resolver
uniprot_sec
Q9UCJ7
resolver
activity_regulation
ACTIVITY REGULATION: Not inhibited by L(+)-tartrate (PubMed:2775236). Synthesized as a single chain proenzyme, with low enzymatic activity. Proteolytic cleavage converts ACP5 into a more active form (PubMed:15950921). {ECO:0000269|PubMed:15950921, ECO:0000269|PubMed:2775236}.
uniprot
proteins
amino_acid_sequence
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQIAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASGKSLFKTRLPRRARP
uniprot
proteins
disease_involvement
DISEASE: Spondyloenchondrodysplasia with immune dysregulation (SPENCDI) [MIM:607944]: A disease characterized by vertebral and metaphyseal dysplasia, spasticity with cerebral calcifications, and strong predisposition to autoimmune diseases. The skeletal dysplasia is characterized by radiolucent and irregular spondylar and metaphyseal lesions that represent islands of chondroid tissue within bone. {ECO:0000269|PubMed:21217752, ECO:0000269|PubMed:21217755}. Note=The disease is caused by variants affecting the gene represented in this entry. ACP5 inactivating mutations result in a functional excess of phosphorylated osteopontin causing deregulation of osteopontin signaling and consequential autoimmune disease.
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:1477968, PubMed:2775236). 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) (By similarity). 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 (By similarity). Promotes osteoclast migration by dephosphorylating SPP1, which binds osteoclasts to the bone matrix (By similarity). 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 (By similarity). 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:P29288, ECO:0000250|UniProtKB:Q05117, ECO:0000269|PubMed:1477968, ECO:0000269|PubMed:2775236}.
uniprot
proteins
mass_dalton
36599
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:15950921}.
uniprot
proteins
protein_family
Metallophosphoesterase superfamily
uniprot
proteins
protein_family
Purple acid phosphatase family
uniprot
proteins
pubmed
11828464
uniprot
proteins
pubmed
11983200
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1477968
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15950921
uniprot
proteins
pubmed
15993892
uniprot
proteins
pubmed
1872798
uniprot
proteins
pubmed
21217752
uniprot
proteins
pubmed
21217755
uniprot
proteins
pubmed
2334436
uniprot
proteins
pubmed
2338077
uniprot
proteins
pubmed
2610679
uniprot
proteins
pubmed
2775236
uniprot
proteins
pubmed
2909539
uniprot
proteins
pubmed
8359686
uniprot
proteins
sequence_length
325
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q05117}. Secreted {ECO:0000269|PubMed:11983200}. Note=The uncleaved form (isoform 5a) is secreted by macrophage and dendritic cell. The cleaved form (isoform 5b) is secreted by osteoclasts. {ECO:0000269|PubMed:11983200}.
uniprot
proteins