(data stored in ACNUC13479 zone)

SWISSPROT: 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   07-JUN-2017, entry version 104.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, PATHWAY,
RP   AND 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
RT   impaired in 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.,
RA   Gonzalez Fernandez-Nino S.M.G., Ebert B., Yang F., Christiansen K.M.,
RA   Hansen S.F., Stonebloom S., Adams P.D., Ronald P.C., Hillson N.J.,
RA   Hadi M.Z., Vega-Sanchez M.E., Loque D., Scheller H.V.,
RA   Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional
RT   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RP   BY 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.,
RA   Wieslander A., Maler L.;
RT   "Lipid interacting regions in phosphate stress glycosyltransferase
RT   atDGD2 from Arabidopsis thaliana.";
RL   Biochemistry 50:4451-4466(2011).
CC   -!- FUNCTION: Catalyzes the transfer of the sulfoquinovose moiety from
CC       UDP-sulfoquinovose to diacylglycerol during sulfolipid
CC       biosynthesis. Sulfolipid contributes to maintaining a negatively
CC       charged lipid-water interface, a requirement for proper function
CC       of photosynthetic membranes. Sulfolipid may also function as a
CC       substitute of anionic phospholipids under phosphate-limited growth
CC       conditions. {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};
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   UniGene; At.47995; -.
DR   ProteinModelPortal; Q8S4F6; -.
DR   SMR; Q8S4F6; -.
DR   STRING; 3702.AT5G01220.1; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; Q8S4F6; -.
DR   PaxDb; Q8S4F6; -.
DR   ProMEX; Q8S4F6; -.
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   eggNOG; COG0438; LUCA.
DR   HOGENOM; HOG000077285; -.
DR   KO; K06119; -.
DR   OMA; WQRGVDT; -.
DR   OrthoDB; EOG093608Q9; -.
DR   PhylomeDB; Q8S4F6; -.
DR   BioCyc; MetaCyc:MONOMER-1202; -.
DR   PRO; PR:Q8S4F6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q8S4F6; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA: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:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
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;
DR   PRODOM; Q8S4F6.
DR   SWISS-2DPAGE; Q8S4F6.
KW   Chloroplast; Complete proteome; Glycosyltransferase;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein;
KW   Plastid; Reference proteome; Transferase; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT       1     83       Chloroplast. {ECO:0000255}.
FT   CHAIN        84    510       Sulfoquinovosyl transferase SQD2.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000432457.
FT   TRANSMEM    198    218       Helical. {ECO:0000255}.
FT   COMPBIAS     24     27       Poly-Ser. {ECO:0000255}.
FT   MOD_RES      88     88       Phosphoserine.
FT                                {ECO:0000244|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
//

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