YND1_SCHPO
ID YND1_SCHPO Reviewed; 572 AA.
AC Q9USP2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Golgi apyrase {ECO:0000303|PubMed:12686557};
DE EC=3.6.1.5;
DE AltName: Full=ATP-diphosphatase {ECO:0000250|UniProtKB:P40009};
DE AltName: Full=ATP-diphosphohydrolase {ECO:0000250|UniProtKB:P40009};
DE AltName: Full=Adenosine diphosphatase {ECO:0000250|UniProtKB:P40009};
DE Short=ADPase {ECO:0000250|UniProtKB:P40009};
DE AltName: Full=Golgi nucleoside diphosphatase {ECO:0000250|UniProtKB:P40009};
GN Name=ynd1 {ECO:0000312|EMBL:CAB57847.1}; ORFNames=SPCC11E10.05c;
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:CAB57847.1}
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 FUNCTION, ENZYME ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=12686557; DOI=10.1074/jbc.m300892200;
RA D'Alessio C., Trombetta E.S., Parodi A.J.;
RT "Nucleoside diphosphatase and glycosyltransferase activities can localize
RT to different subcellular compartments in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 278:22379-22387(2003).
RN [3] {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 -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC nucleoside tri- and di-phosphates. Required for Golgi glycosylation and
CC cell wall integrity. Involved in N-mannosylation of proteins in Golgi.
CC {ECO:0000250|UniProtKB:P40009, ECO:0000269|PubMed:12686557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC Evidence={ECO:0000269|PubMed:12686557};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12686557};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12686557};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12686557};
CC Note=Divalent metal cations. Ca(2+), Mg(2+) or Mn(2+).
CC {ECO:0000269|PubMed:12686557};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:12686557}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:12686557,
CC ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000255}.
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DR EMBL; CU329672; CAB57847.1; -; Genomic_DNA.
DR PIR; T40856; T40856.
DR RefSeq; NP_588201.1; NM_001023191.2.
DR AlphaFoldDB; Q9USP2; -.
DR SMR; Q9USP2; -.
DR BioGRID; 275324; 12.
DR STRING; 4896.SPCC11E10.05c.1; -.
DR iPTMnet; Q9USP2; -.
DR MaxQB; Q9USP2; -.
DR PaxDb; Q9USP2; -.
DR PRIDE; Q9USP2; -.
DR EnsemblFungi; SPCC11E10.05c.1; SPCC11E10.05c.1:pep; SPCC11E10.05c.
DR GeneID; 2538741; -.
DR KEGG; spo:SPCC11E10.05c; -.
DR PomBase; SPCC11E10.05c; ynd1.
DR VEuPathDB; FungiDB:SPCC11E10.05c; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_3_1_1; -.
DR InParanoid; Q9USP2; -.
DR OMA; QDEIGPP; -.
DR PhylomeDB; Q9USP2; -.
DR Reactome; R-SPO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9USP2; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; IDA:PomBase.
DR GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:PomBase.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISO:PomBase.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:PomBase.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006256; P:UDP catabolic process; IBA:GO_Central.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Golgi apparatus; Hydrolase; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..572
FT /note="Golgi apyrase"
FT /id="PRO_0000347282"
FT TOPO_DOM 1..470
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40009, ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40009, ECO:0000255"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 572 AA; 64680 MW; 8E039FBFA0D3B482 CRC64;
MVRKYGIFID AGSSGSRLLI YSWDYDTDSS LSDKVKKLPL IETGIGDGGK WSLKVQPGIS
SFANNPKHVG KKHLKELLDF AAHAIPKDVH KETPVFLSAT AGMRLLGVDA QNKILSHACR
YIKKNYDFDI PNCSNSIRVI DGKAEGMYGW LATNYLLKTL EEKDTSTVGF LDMGGASVQI
AFELPPSQLK NYKDSISTVH IGLQNGQQLE YPLFVTTWLG FGANEAYRRY LGLLIESENG
KVGNTLSDPC SLRGRTYDID GIEFAGTGDL KQCLKLTYNL LNKDKPCSMD PCNFDGISIP
PVDFANTEFV GVSEFWYTTN DVFDMGGSYH FPNFYKKVDE YCGTEWETML SRLYNKELTP
STDENKLEKL CFKASWALNV LHEGFDVPKS NTSSNDAKDG LSVIPAYHSP FTSLEKIERT
EVSWTLGQVL LYASNQQLLA KPEYANYYMD PYGKLIASPS KHWMRLFPNK LFFILSFIFC
LFFLFSLVLF GYDPKRRQRF KKFLLRLQRR KAPYIMSANG SYEDIADFSD DLEMSSPSKW
HGPPIRTTSS HVLADRLSFT ASRERTPRSP FP
