GDE1_SCHPO
ID GDE1_SCHPO Reviewed; 1076 AA.
AC Q9C104; P78784;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Glycerophosphocholine phosphodiesterase gde1;
DE EC=3.1.4.2 {ECO:0000250|UniProtKB:Q02979};
DE AltName: Full=Glycerophosphodiester phosphodiesterase gde1;
GN Name=gde1; ORFNames=SPAPB1E7.05;
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 [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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 662-1076.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-523; SER-851;
RP SER-852 AND SER-853, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Glycerophosphocholine glycerophosphodiesterase responsible
CC for the hydrolysis of intracellular glycerophosphocholine into
CC glycerol-phosphate and choline. The choline is used for phosphatidyl-
CC choline synthesis. Required for utilization of glycerophosphocholine as
CC phosphate source. {ECO:0000250|UniProtKB:Q02979}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:16061, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:57597; EC=3.1.4.2;
CC Evidence={ECO:0000250|UniProtKB:Q02979};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16062;
CC Evidence={ECO:0000250|UniProtKB:Q02979};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the GDE1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAC36922.1; -; Genomic_DNA.
DR EMBL; D89133; BAA13795.1; -; mRNA.
DR PIR; T42379; T42379.
DR RefSeq; NP_594131.1; NM_001019555.2.
DR AlphaFoldDB; Q9C104; -.
DR SMR; Q9C104; -.
DR BioGRID; 280091; 4.
DR STRING; 4896.SPAPB1E7.05.1; -.
DR iPTMnet; Q9C104; -.
DR MaxQB; Q9C104; -.
DR PaxDb; Q9C104; -.
DR PRIDE; Q9C104; -.
DR EnsemblFungi; SPAPB1E7.05.1; SPAPB1E7.05.1:pep; SPAPB1E7.05.
DR GeneID; 2543677; -.
DR KEGG; spo:SPAPB1E7.05; -.
DR PomBase; SPAPB1E7.05; gde1.
DR VEuPathDB; FungiDB:SPAPB1E7.05; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_005444_1_0_1; -.
DR InParanoid; Q9C104; -.
DR OMA; HSTQLDT; -.
DR PhylomeDB; Q9C104; -.
DR PRO; PR:Q9C104; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; ISO:PomBase.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:PomBase.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR033506; Gde1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF1; PTHR22958:SF1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF03009; GDPD; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1076
FT /note="Glycerophosphocholine phosphodiesterase gde1"
FT /id="PRO_0000067250"
FT DOMAIN 1..96
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REPEAT 298..327
FT /note="ANK 1"
FT REPEAT 332..362
FT /note="ANK 2"
FT REPEAT 366..395
FT /note="ANK 3"
FT REPEAT 400..429
FT /note="ANK 4"
FT DOMAIN 747..1066
FT /note="GP-PDE"
FT REGION 524..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 669
FT /note="A -> E (in Ref. 2; BAA13795)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="E -> G (in Ref. 2; BAA13795)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="F -> S (in Ref. 2; BAA13795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1076 AA; 118129 MW; 3129E2F5036FD301 CRC64;
MLENDLQKVV NLFNTRIVQL DNYVTRLSTE KSPNTEITQA LSSSYEAEEK AKQLKELDFR
LQQLSSFCEW NKLAFEKLAA NMDKHLGTER LVTFYEQKVC KLDFANSSKI YESMIALKAL
NSSQNDSEVK DKLEKLSIHH PLKKDLLAFI QLDIAAEVVT ACINAPDSVL VDILAASIIA
GAKACMREVI GRIGLRSECL ASALRRAINN LCGPDEGVLY FLEVLKQICS VVYVDSYHSN
RLLSRILLVE RNSKGQSVMH SVAKLGWAGL CSKFCEIVSS IPDSEPLNWM LPCWRDVMHD
TPLTLAIKGN HVEALHALLS AQDKETTSTK PGPVPPLVLT CCVGDYDLIV EELILAGFNP
NEVDASSNTA LHTAVRYNRP ECVKMLLKLG ANPSARDFLN SWTPLMLASA TGLSEIVSIL
VASGASVDEV DSSGWTAMEQ AVVRGYLHLA DKLRTQVALS DKPVNLHTLY IKASSSEMRS
RKRAMDLQLS RSVVIIRISD LAGRIRVSLQ GDDAVYVSGR SPSFAASRPS SVDFMSQSTD
SLSKNDTTAS NGSMTPSSSQ NNSVIIDIPR SHFDNAGEVC LENLAEPDEI ADDSIHLHYD
AAQENSPQPV NGSSPPYELV FVTRNTEEAT ITIDLLANRS HKILGRTVCC LTSLVSDLGN
HMQSLKPLAP LPLLSSKTLK PIAHVNADVL ISKVTVDDRF SSNDGISTPA LSLEAVSNVS
RTALEDAERS LHKSATTTSE SGKSNGVAVI GHRGLGKNQP DRLSLQLGEN TLQSFIKAAD
LGASYVELDV QMTKDMVPVV YHDFIVNETG TDAQVHSLTL EQFLGASHSP SEEIKDDASD
IQQKRRPRAY SSSFTPSGSQ VNFGEFAEEN ARLKPKVYKG NALGHTICAP FTTLKDVLKE
VPQSVGLNVE FKYPMLSEAE EEKLLPIAYD YNFYVDTILS IIKKYGGKRK YIFSSFNPDI
CILLSLKSTN PVLFLTEGGT AYRTDVRAAS LRQALKFASQ WSFLGIVSAC EPLIMCPRLI
KAVKQLGLSC YTYGVLNNDV DNVRRQVRFG VDAVIVDNVL AIRRALNQYD ESLESD
