ID A0A1P8AWC0_ARATH Unreviewed; 1101 AA.
AC A0A1P8AWC0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=glycerophosphodiester phosphodiesterase {ECO:0000256|ARBA:ARBA00012247};
DE EC=3.1.4.46 {ECO:0000256|ARBA:ARBA00012247};
GN Name=SNC4 {ECO:0000313|EMBL:ANM60958.1, ECO:0000313|TAIR:AT1G66980};
GN Synonyms=GDPDL2 {ECO:0000313|EMBL:ANM60958.1};
GN OrderedLocusNames=At1g66980 {ECO:0000313|Araport:AT1G66980,
GN ECO:0000313|EMBL:ANM60958.1};
GN ORFNames=F1O19.6 {ECO:0000313|EMBL:ANM60958.1}, F1O19_6
GN {ECO:0000313|EMBL:ANM60958.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM60958.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:ANM60958.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC Evidence={ECO:0000256|ARBA:ARBA00029315};
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DR EMBL; CP002684; ANM60958.1; -; Genomic_DNA.
DR RefSeq; NP_001323205.1; NM_001334265.1.
DR AlphaFoldDB; A0A1P8AWC0; -.
DR SMR; A0A1P8AWC0; -.
DR EnsemblPlants; AT1G66980.4; AT1G66980.4; AT1G66980.
DR GeneID; 843016; -.
DR Gramene; AT1G66980.4; AT1G66980.4; AT1G66980.
DR Araport; AT1G66980; -.
DR TAIR; AT1G66980; SNC4.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A1P8AWC0; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08603; GDPD_SHV3_repeat_1; 1.
DR CDD; cd08604; GDPD_SHV3_repeat_2; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43620:SF47; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE GDPDL1-RELATED; 1.
DR PANTHER; PTHR43620; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51704; GP_PDE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8AWC0,
KW ECO:0007829|ProteomicsDB:A0A1P8AWC0};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..1101
FT /note="glycerophosphodiester phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010228114"
FT TRANSMEM 735..756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..336
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT DOMAIN 352..653
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT DOMAIN 788..1077
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 816
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1101 AA; 122169 MW; A97A45DF7B54D6EC CRC64;
MNSQQSTRTK QMLQQSSTHL LCGVVLLQLF AAQVDAQRST SPWQTLSDSS LAAYQFAMVV
SVADVVLWCD VQLTKDGHGI CFPDLNLANA SNSEEVYPNR QKSYPVNGVT TKGWFPIDFS
LTELQKVLFS LIRGILSRSG KFDENGYSIS TVQNVATQMK PALFWLNVQH DEFYEQHNLS
MSSFLLSTSR TVSIDFISSP EVNFFRKIAG GFGNNGPSFV FQFMGKEDFE PTTNRTYGSI
LSNLSFVKTF ASGILVPKSY ILPLDDKQYL LPHTSLVQDA HKAGLKLYAS GFANDVDIAY
NYSWDPVSEY LSFVDNGNFS VDGMLSDFPL TASASVDCFS HIGRNATKQV DFLVISKNGA
SGEYPGCTKL AYEKAIKDGS DVIDCPVQMS SDGIPFCSSS IDLVNSTTVG QTHLRNRSII
VPEISSVAGI FTFSLTWHEI QSLTPAISNP FRENGMSRNP NERNSGNLIS LYEFLNLAKN
STSLSGILIS LENVVYLREK KGLDVVKVVL NRLTETGYIV GTLKVMIQST TRLVLVDFKN
QSTYKTVYKI KETIGNITDS AIEDIKKFAN AVVINKASVF PNSDSFLTGQ TTNVLERLQK
FQLPVYVELF QNEFVSQPFD FFADETVEIN AYIFGAGING TITEFPYTAA RYKRNRCLGR
EEVPPYMLPV NPGGVLTLIS TSSLPPAQDP NPIFTHDDVT EPPLPPVIAK SPTSTLGTPS
TIAKPLRNFL KVIRIVSWSV AGVVLFLVLL TLVFCFHRKR ETRLRQQKLK ALIPLEHYTY
AQVKRITKSF AEVVGRGGFG IVYKGTLSDG RVVAVKVLKD TKGNGEDFIN EVATMSRTSH
LNIVSLLGFC SEGSKRAIIY EFLENGSLDK FILGKTSVNM DWTALYRIAL GVAHGLEYLH
HSCKTRIVHF DIKPQNVLLD DSFCPKVSDF GLAKLCEKKE SILSMLDTRG TIGYIAPEMI
SRVYGNVSHK SDVYSYGMLV LEIIGARNKE KANQACASNT SSMYFPEWVY RDLESCKSGR
HIEDGINSEE DELAKKMTLV GLWCIQPSPV DRPAMNRVVE MMEGSLEALE VPPRPVLQQI
PISNLHESSI LSEDVSVYTE G
//
