PPB_SCHPO
ID PPB_SCHPO Reviewed; 532 AA.
AC O60109; Q9C427;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Alkaline phosphatase;
DE EC=3.1.3.1;
GN ORFNames=SPBC14F5.13c;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kang S.-W., Lim C.-J.;
RT "Characterization of alkaline phosphatase gene from Schizosaccharomyces
RT pombe.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
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=3.1.3.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR EMBL; AF316541; AAK07179.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19331.1; -; Genomic_DNA.
DR PIR; T39459; T39459.
DR RefSeq; NP_596739.1; NM_001022665.2.
DR AlphaFoldDB; O60109; -.
DR SMR; O60109; -.
DR BioGRID; 276470; 16.
DR STRING; 4896.SPBC14F5.13c.1; -.
DR MaxQB; O60109; -.
DR PaxDb; O60109; -.
DR EnsemblFungi; SPBC14F5.13c.1; SPBC14F5.13c.1:pep; SPBC14F5.13c.
DR GeneID; 2539926; -.
DR KEGG; spo:SPBC14F5.13c; -.
DR PomBase; SPBC14F5.13c; -.
DR VEuPathDB; FungiDB:SPBC14F5.13c; -.
DR eggNOG; KOG4126; Eukaryota.
DR HOGENOM; CLU_008539_6_0_1; -.
DR InParanoid; O60109; -.
DR OMA; NIYAYAN; -.
DR PhylomeDB; O60109; -.
DR Reactome; R-SPO-1483166; Synthesis of PA.
DR Reactome; R-SPO-6811438; Intra-Golgi traffic.
DR Reactome; R-SPO-8935690; Digestion.
DR PRO; PR:O60109; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:PomBase.
DR GO; GO:0106219; F:zinc ion sensor activity; IDA:PomBase.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; ISO:PomBase.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..532
FT /note="Alkaline phosphatase"
FT /id="PRO_0000186165"
FT TRANSMEM 27..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 513..514
FT /note="PS -> HC (in Ref. 1; AAK07179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 58666 MW; 57A84A66926D545C CRC64;
MASERDPLLP VHGEGPESPS RRNWKTWIKH GILLILVLST VIFFYFFSSH KSKGTNEKPK
FVIMMVSDGM GPGSLSMTRS FVETLNDKEG YRLPLDEHLI GSSRTRSSSS LITDSAAGAT
AFSCANKTYN GAVGVLDNEK PCGTILEAAK EAGYLTGIVV TSRVTDATPA SFSAHAANRF
MQDLIAEYQV GMGPLGRSVD LLFGGGLCSF LPKSTYRSCR SDNLDLLKYA RKKEGFQILL
NRTDFDELSN AQLPLLGLFS DYHLSYDIDY QPEVQPKLSE MVETALDVLL NATNEDTSKG
FFLLIEGSRI DMASHNNDPI AHVYEVMEYN RAFEIASAFV EKNGGSLIST SDHETGGLTV
GRQVSKKYPE YLWKPQVLSL ALHSIEYLAS AIVNHNQNTL LPYIEQFVLP AIGIPDPNPK
QIHDIYVARH NIFNLINVLS DIVSVEAQIG WTTHGHTAVD VNVYGVGEVT EHLRGNMENI
EIGQFMEIYL NVSLSDVTEK LKDAPIHGAP DRPSLVETSF SDRLVGFGAD LF
