SQD2_ARATH
ID SQD2_ARATH Reviewed; 510 AA.
AC Q8S4F6; Q941K9; Q9LFB4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sulfoquinovosyl transferase SQD2 {ECO:0000303|PubMed:11960029};
DE EC=2.4.1.- {ECO:0000305|PubMed:11960029};
DE AltName: Full=Protein SULFOQUINOVOSYLDIACYLGLYCEROL 2 {ECO:0000303|PubMed:11960029};
DE AltName: Full=Sulfolipid synthase SQD2 {ECO:0000305|PubMed:11960029};
DE AltName: Full=UDP-sulfoquinovose: diacylglycerol alpha-sulfoquinovosyltransferase SQD2 {ECO:0000305};
DE Flags: Precursor;
GN Name=SQD2 {ECO:0000303|PubMed:11960029};
GN OrderedLocusNames=At5g01220 {ECO:0000312|Araport:AT5G01220};
GN ORFNames=F7J8.200 {ECO:0000312|EMBL:CAB69850.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND
RP INDUCTION BY PHOSPHATE DEPLETION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11960029; DOI=10.1073/pnas.082696499;
RA Yu B., Xu C., Benning C.;
RT "Arabidopsis disrupted in SQD2 encoding sulfolipid synthase is impaired in
RT phosphate-limited growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5732-5737(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21506606; DOI=10.1021/bi200162f;
RA Szpryngiel S., Ge C., Iakovleva I., Georgiev A., Lind J., Wieslander A.,
RA Maler L.;
RT "Lipid interacting regions in phosphate stress glycosyltransferase atDGD2
RT from Arabidopsis thaliana.";
RL Biochemistry 50:4451-4466(2011).
CC -!- FUNCTION: Catalyzes the transfer of the sulfoquinovose moiety from UDP-
CC sulfoquinovose to diacylglycerol during sulfolipid biosynthesis.
CC Sulfolipid contributes to maintaining a negatively charged lipid-water
CC interface, a requirement for proper function of photosynthetic
CC membranes. Sulfolipid may also function as a substitute of anionic
CC phospholipids under phosphate-limited growth conditions.
CC {ECO:0000269|PubMed:11960029}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000269|PubMed:11960029}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255,
CC ECO:0000269|PubMed:21506606}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: By phosphate depletion. {ECO:0000269|PubMed:11960029}.
CC -!- DISRUPTION PHENOTYPE: Lack of sulfolipid leading to reduced growth
CC under phosphate-limited growth conditions.
CC {ECO:0000269|PubMed:11960029}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB69850.1; Type=Erroneous gene model prediction; Evidence={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; AF454354; AAM18913.1; -; mRNA.
DR EMBL; KJ138712; AHL38652.1; -; mRNA.
DR EMBL; AL137189; CAB69850.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90311.1; -; Genomic_DNA.
DR EMBL; AY045961; AAK76635.1; -; mRNA.
DR EMBL; BT005796; AAO64198.1; -; mRNA.
DR PIR; T45962; T45962.
DR RefSeq; NP_568085.2; NM_120200.4.
DR AlphaFoldDB; Q8S4F6; -.
DR SMR; Q8S4F6; -.
DR STRING; 3702.AT5G01220.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q8S4F6; -.
DR PaxDb; Q8S4F6; -.
DR PRIDE; Q8S4F6; -.
DR ProMEX; Q8S4F6; -.
DR ProteomicsDB; 226855; -.
DR EnsemblPlants; AT5G01220.1; AT5G01220.1; AT5G01220.
DR GeneID; 831888; -.
DR Gramene; AT5G01220.1; AT5G01220.1; AT5G01220.
DR KEGG; ath:AT5G01220; -.
DR Araport; AT5G01220; -.
DR TAIR; locus:2150059; AT5G01220.
DR eggNOG; KOG1111; Eukaryota.
DR HOGENOM; CLU_009583_20_0_1; -.
DR InParanoid; Q8S4F6; -.
DR OMA; SGYMRDE; -.
DR OrthoDB; 482876at2759; -.
DR PhylomeDB; Q8S4F6; -.
DR BioCyc; MetaCyc:MON-1202; -.
DR PRO; PR:Q8S4F6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S4F6; baseline and differential.
DR Genevisible; Q8S4F6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0046510; F:UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:TAIR.
DR GO; GO:0046506; P:sulfolipid biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phosphoprotein; Plastid; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..83
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 84..510
FT /note="Sulfoquinovosyl transferase SQD2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432457"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 510 AA; 56630 MW; 20E57D318D6BED68 CRC64;
MTTLSSINLS IPPHLLPSTT NTCSSSSATS CSPPRSSSFV LHSPLSFGHR RLPISKKSKL
RFCGVITKEA VSGSNDMTIT QVREDDESEI DAPLLDPESL SKPRRIALFV EPSPFAYVSG
YKNRFQNFIR YLREMGDEVI VVTTHEGVPE EFYGARVIGS RSFPCPYYQK VPLSLALSPR
IISEIARFKP DIIHASSPGV MVFGALAIAK MLSVPIVMSY HTHVPVYIPR YTFSWLVKPM
WSIIRFLHRA ADLTLVPSAA IGKDLIAAGA TAANQLRLWN KGVDSESFNP RFRSQEMRIR
LSNGEPEKPL VIHVGRIGVE KSLELLKSVM DKLPEARIAF IGDGPYKEDL EKLFTGMPAV
FTGTLQGDEL SQAYASGDVF VMPSESETLG LVVLEAMSSG LPVVAARAGG IPDIIPEDQE
GKTGFLFNPG DVEDCVTKLR TLLHDRETRE IIGKAAREET EKYDWRAATT KIRNEQYSAA
IWFWRKKKVH VLGPINWLIK RLFPVPEGNV
