ACP3
entrez
55
canonical
uniprot
P15309
canonical
ensembl
ENSG00000014257
resolver
ensp
ENSP00000323036
resolver
ensp
ENSP00000337471
resolver
ensp
ENSP00000417744
resolver
ensp
ENSP00000709382
resolver
genesymbol
ACP3
resolver
genesymbol_syn
ACPP
resolver
hgnc
HGNC:125
resolver
uniprot
D3DNC6
resolver
uniprot
Q5FBY0
resolver
uniprot
Q96KY0
resolver
uniprot
Q96QK9
resolver
uniprot
Q96QM0
resolver
uniprot_entry
PPAP_HUMAN
resolver
uniprot_sec
D3DNC6
resolver
uniprot_sec
Q5FBY0
resolver
uniprot_sec
Q96KY0
resolver
uniprot_sec
Q96QK9
resolver
uniprot_sec
Q96QM0
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatase activity inhibited by L(+)-tartrate, and by its derivative, alpha-benzylaminobenzylphosphonic acid (PubMed:1989985, PubMed:8132635, PubMed:9584846). Inhibited by phenylglyoxal, forming a covalent adduct with Arg-86 (PubMed:1989985). {ECO:0000269|PubMed:1989985, ECO:0000269|PubMed:8132635, ECO:0000269|PubMed:9584846}.
uniprot
proteins
amino_acid_sequence
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD
uniprot
proteins
ec_number
3.1.3.2
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
ec_number
3.1.3.5
uniprot
proteins
function
FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins (PubMed:10506173, PubMed:15280042, PubMed:20498373, PubMed:9584846, PubMed:8132635). Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (PubMed:10506173, PubMed:15280042). {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:15280042, ECO:0000269|PubMed:20498373, ECO:0000269|PubMed:8132635, ECO:0000269|PubMed:9584846}.; FUNCTION: [Isoform 2]: Tyrosine phosphatase that acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling (PubMed:20498373). In addition to its tyrosine phosphatase activity has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor (By similarity). {ECO:0000250|UniProtKB:Q8CE08, ECO:0000269|PubMed:20498373}.; FUNCTION: [PAPf39]: (Microbial infection) Forms amyloid beta-sheet fibrils in semen. These fibrils, termed SEVI (semen-derived enhancer of viral infection) capture HIV virions, attach them to target cells and enhance infection (PubMed:18083097, PubMed:19451623, PubMed:19897482). SEVI amyloid fibrils are degraded by polyphenol epigallocatechin-3-gallate (EGCG), a constituent of green tea (PubMed:19451623). Assembly of SEVI amyloid fibrils and their amplification of HIV infection is inhibited by WW61, a non-natural hexapeptide inhibitor (Trp-His-Lys-chAla-Trp-hydroxyTic) (PubMed:21677644). The target cell attachment and enhancement of HIV infection is also inhibited by surfen (PubMed:19897482). Also similarly boosts XMRV (xenotropic murine leukemia virus-related virus) infection (PubMed:19403677). {ECO:0000269|PubMed:18083097, ECO:0000269|PubMed:19403677, ECO:0000269|PubMed:19451623, ECO:0000269|PubMed:19897482, ECO:0000269|PubMed:21677644}.
uniprot
proteins
mass_dalton
44566
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="R->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:8132635"; MUTAGEN 44; /note="H->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:8132635"; MUTAGEN 47; /note="R->A: Reduces catalytic efficiency by 90,000-fold with p-nitrophenyl phosphate as substrate at pH 5.0."; /evidence="ECO:0000269|PubMed:8132635"; MUTAGEN 86; /note="R->A: Has a minor effect on activity, reducing catalytic efficiency by 1.6-fold with p-nitrophenyl phosphate as substrate at pH 5.0."; /evidence="ECO:0000269|PubMed:8132635"; MUTAGEN 111; /note="R->A: Reduces catalytic efficiency by 16,000-fold with p-nitrophenyl phosphate as substrate at pH 5.0. Shows no activity with phenyl phosphate."; /evidence="ECO:0000269|PubMed:8132635"; MUTAGEN 206; /note="W->F: Greatly reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate."; /evidence="ECO:0000269|PubMed:9584846"; MUTAGEN 206; /note="W->L: Reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate."; /evidence="ECO:0000269|PubMed:9584846"; MUTAGEN 289; /note="H->A: Reduces catalytic efficiency by 400-fold with p-nitrophenyl phosphate as substrate at pH 5.0."; /evidence="ECO:0000269|PubMed:8132635"; MUTAGEN 290; /note="D->A: Reduces catalytic efficiency by 100-fold with p-nitrophenyl phosphate as substrate at pH 5.0. Shows higher activity with p-nitrophenyl phosphate than with phenyl phosphate."; /evidence="ECO:0000269|PubMed:8132635
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. High mannose content, partially sialylated and fucosylated biantennary complex. Also fucosylated with partially sialylated triantennary complex oligosaccharides. {ECO:0000269|PubMed:10639192, ECO:0000269|PubMed:12525165, ECO:0000269|PubMed:38341922}.; PTM: Proteolytically cleaved in seminal fluid to produce several peptides. Peptide PAPf39, the most prominent, forms amyloid beta-sheet fibrils, SEVI (semen-derived enhancer of viral infection). {ECO:0000269|PubMed:18083097}.
uniprot
proteins
protein_family
Histidine acid phosphatase family
uniprot
proteins
pubmed
10506173
uniprot
proteins
pubmed
10639192
uniprot
proteins
pubmed
12525165
uniprot
proteins
pubmed
1375464
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15280042
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17638863
uniprot
proteins
pubmed
17897319
uniprot
proteins
pubmed
18083097
uniprot
proteins
pubmed
19403677
uniprot
proteins
pubmed
19451623
uniprot
proteins
pubmed
19897482
uniprot
proteins
pubmed
1989985
uniprot
proteins
pubmed
19995078
uniprot
proteins
pubmed
20498373
uniprot
proteins
pubmed
21487525
uniprot
proteins
pubmed
21677644
uniprot
proteins
pubmed
2395659
uniprot
proteins
pubmed
2712834
uniprot
proteins
pubmed
2842184
uniprot
proteins
pubmed
3674882
uniprot
proteins
pubmed
38341922
uniprot
proteins
pubmed
7951074
uniprot
proteins
pubmed
8132635
uniprot
proteins
pubmed
9584846
uniprot
proteins
pubmed
9804805
uniprot
proteins
sequence_length
386
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000305|PubMed:17638863}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:20498373}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:20498373}. Cytoplasm, cytosol {ECO:0000269|PubMed:20498373}. Note=Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell membrane and in intracellular vesicles (PubMed:17638863). Colocalizes with LAMP2 on the lysosome membrane (PubMed:17897319). {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319}.
uniprot
proteins
transmembrane_region
TRANSMEM P15309-2:382..404; /note="Helical"; /evidence="ECO:0000303|PubMed:17638863
uniprot
proteins