[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135; DOI=10.1016/0378-1119(95)00298-K; PubMed=7557398 [NCBI, ExPASy, EBI, Israel, Japan] Mullaney E.J., Daly C.B., Ehrlich K.C., Ullah A.H.J.; "The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid phosphatase."; Gene 162:117-121(1995).
[2]	PROTEIN SEQUENCE OF 23-605. STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135; DOI=10.1006/bbrc.1994.2166; PubMed=8074654 [NCBI, ExPASy, EBI, Israel, Japan] Ullah A.H.J., Mullaney E.M., Dischinger H.C. Jr.; "The complete primary structure elucidation of Aspergillus ficuum (niger), pH 6.0, optimum acid phosphatase by Edman degradation."; Biochem. Biophys. Res. Commun. 203:182-189(1994).
[3]	PROTEIN SEQUENCE OF 23-56, AND CHARACTERIZATION. STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135; PubMed=3375203 [NCBI, ExPASy, EBI, Israel, Japan] Ullah A.H.J., Cummins B.J.; "Aspergillus ficuum extracellular pH 6.0 optimum acid phosphatase: purification, N-terminal amino acid sequence, and biochemical characterization."; Prep. Biochem. 18:37-65(1988).

Comments

CATALYTIC ACTIVITY: A phosphate monoester + H₂O = an alcohol + phosphate.
COFACTOR: Copper (Potential).
ENZYME REGULATION: Competitively inhibited by phosphomycin and inorganic orthophosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6. Inactive above pH 6.7;
Temperature dependence: Optimum temperature is 63 degrees Celsius;
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Secreted.
PTM: Glycosylated; probably with N-linked high-mannose oligosaccharides.

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

U18553; AAA91632.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC2545; JC2545.

3D structure databases

ModBase

Q12546.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0003993;	Molecular function: acid phosphatase activity (inferred from electronic annotation from InterPro).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014390; Acid_Pase_Asper.
IPR003961; FN_III.
IPR004843; M-pesterase.
IPR015914; Purple_acid_Pase_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.380; Purple_acid_Pase_N; 1.

Pfam

PF00149; Metallophos; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000900; Acid_Ptase_Asper; 1.

SMART

SM00060; FN3; 1.
SMART graphical view of domain structure.

ProtoNet

Q12546.

Other

UniRef

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

Keywords

Copper; Direct protein sequencing; Glycoprotein; Hydrolase; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`CHAIN`	`23 605`	`583`	`Acid phosphatase.`	`PRO_0000023997`
`PROPEP`	`606 614`	`9`		`PRO_0000023998`
`CARBOHYD`	`110 110`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`161 161`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`242 242`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`295 295`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`333 333`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`340 340`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`352 352`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`408 408`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`429 429`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`512 512`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`523 523`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`559 559`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`578 578`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 614 AA [This is the length of the unprocessed precursor]

Molecular weight: 67211 Da [This is the MW of the unprocessed precursor]

CRC64: 7016738F63C62EBE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKGTAASALL VALSATAAQA RPVVDERFPY TGPAVPIGDW VDPTINGNGK GFPRLVEPPA 

        70         80         90        100        110        120 
VKPATANPRN NVNVISLSYI PKGMHIHYQT PFGLGQLPAV RWGKDPRNLN STAQGYSHTY 

       130        140        150        160        170        180 
DRTPSCSQVK AVTQCSQFFH EVSIDGLEPD TTYYYQIPAA NGTTQSEVLS FKTSRPAGHP 

       190        200        210        220        230        240 
GSFSVAVLND MGYTNAHGTH KQLVKAATEG TAFAWHGGDL SYADDWYSGI LACADDWPVC 

       250        260        270        280        290        300 
YNGTSSTLPG GGPLPEEYKK PLPAGEIPDQ GGPQGGDMSV LYESNWDLWQ QWLNNVTLKI 

       310        320        330        340        350        360 
PYMVLPGNHE ASCAEFDGPH NILTAYLNDD IANGTAPTDN LTYYSCPPSQ RNFTAYQHRF 

       370        380        390        400        410        420 
RMPGPETGGV GNFWYSFDYG LAHFVSIDGE TDFANSPEWN FAEDVTGNET LPSESETFIT 

       430        440        450        460        470        480 
DSGPFGNVNG SVHETKSYEQ WHWLQQDLAK VDRSKTPWVI VMSHRPMYSS AYSSYQLHVR 

       490        500        510        520        530        540 
EAFEGLLLKY GVDAYLSGHI HWYERLYPLG ANGTIDTAAI VNNNTYYAHN GKSITHIING 

       550        560        570        580        590        600 
MAGNIESHSE FSDGEGLTNI TALLDKVHYG FSKLTIFNET ALKWELIRGD DGTVGDSLTL 

       610 
LKPSHVAGGK KLHS

Q12546 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