PPA4_SCHPO
ID PPA4_SCHPO Reviewed; 462 AA.
AC Q9USS6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Probable acid phosphatase SPBC4.06;
DE EC=3.1.3.2;
GN ORFNames=SPBC4.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB58405.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000250|UniProtKB:Q9NPH0};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000255}.
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DR EMBL; CU329671; CAB58405.1; -; Genomic_DNA.
DR PIR; T40420; T40420.
DR RefSeq; NP_595479.1; NM_001021390.2.
DR AlphaFoldDB; Q9USS6; -.
DR SMR; Q9USS6; -.
DR STRING; 4896.SPBC4.06.1; -.
DR MaxQB; Q9USS6; -.
DR PaxDb; Q9USS6; -.
DR EnsemblFungi; SPBC4.06.1; SPBC4.06.1:pep; SPBC4.06.
DR GeneID; 2540652; -.
DR KEGG; spo:SPBC4.06; -.
DR PomBase; SPBC4.06; -.
DR VEuPathDB; FungiDB:SPBC4.06; -.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_030431_3_1_1; -.
DR InParanoid; Q9USS6; -.
DR OMA; SWPPFTS; -.
DR PhylomeDB; Q9USS6; -.
DR Reactome; R-SPO-1483166; Synthesis of PA.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9USS6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0003993; F:acid phosphatase activity; ISM:PomBase.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:PomBase.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Mitochondrion; Reference proteome.
FT CHAIN 1..462
FT /note="Probable acid phosphatase SPBC4.06"
FT /id="PRO_0000311719"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9NPH0"
FT ACT_SITE 330
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15309"
SQ SEQUENCE 462 AA; 51976 MW; 113D45882EA0DFA9 CRC64;
MSQMSSASVK FPDSVPGVDY PKQLQLKYLQ VIFRHGERAP VKERLGSAGI PKDWKLCNNA
RRFFAQIKGE KEWSVLGFER KVESPVDTSL AAPTSDNSPS GVCIHGELTD FGRVTTRTLG
EYLRERYVKQ LKFLPDELNN YADVYMRATP MVRALESLEH VFSGLYPESK RKMGLPVIFT
RNWSDENLLP NENNCPRLVQ LYEEFAERAA KLYDPLLAGR ASEMMSQFMN GQPVRVVSSH
PRLSGLLDTI NAAIGSHVDF NPNLRDEQWL RDAETAVVEE WFGGYKVSKL MRQLGAGSLL
NDLSMRMENF VVAEKNGSPY HRLALYGAHD VTIAAILASL DAFDYRWPPF TSHLEMELFE
DTSSKSDSQN QSGDNKTTDL KLFSDESTDA SNSAIVAASN SARDMSDWYV RITYNSTPVV
MGACRGQGYK GNDTICPLSI FKDTVRALKP VEYHTMCKPV KK
