SFR2_ORYSJ
ID SFR2_ORYSJ Reviewed; 647 AA.
AC Q8L6H7; F4MGF3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Beta-glucosidase-like SFR2, chloroplastic {ECO:0000303|PubMed:15258268};
DE EC=2.4.1.184 {ECO:0000250|UniProtKB:Q93Y07};
DE AltName: Full=Beta-glucosidase 36 {ECO:0000303|PubMed:17196101};
DE Short=Os11bglu36 {ECO:0000303|PubMed:17196101};
DE AltName: Full=Protein SENSITIVE TO FREEZING 2 {ECO:0000303|PubMed:15258268};
DE Short=OsSFR2 {ECO:0000303|PubMed:15258268};
GN Name=SFR2 {ECO:0000303|PubMed:15258268};
GN Synonyms=BGLU36 {ECO:0000303|PubMed:17196101};
GN OrderedLocusNames=Os11g0683500 {ECO:0000312|EMBL:BAF28826.1},
GN LOC_Os11g45710 {ECO:0000312|EMBL:ABA95293.1};
GN ORFNames=OsJ_34793 {ECO:0000312|EMBL:EAZ19256.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15258268; DOI=10.1105/tpc.104.024018;
RA Thorlby G., Fourrier N., Warren G.;
RT "The SENSITIVE TO FREEZING2 gene, required for freezing tolerance in
RT Arabidopsis thaliana, encodes a beta-glucosidase.";
RL Plant Cell 16:2192-2203(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17196101; DOI=10.1186/1471-2229-6-33;
RA Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A.,
RA Ketudat Cairns J.R.;
RT "Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglu12
RT beta-glucosidase.";
RL BMC Plant Biol. 6:33-33(2006).
RN [8]
RP FUNCTION.
RX PubMed=18466306; DOI=10.1111/j.1365-313x.2008.03549.x;
RA Fourrier N., Bedard J., Lopez-Juez E., Barbrook A., Bowyer J., Jarvis P.,
RA Warren G., Thorlby G.;
RT "A role for SENSITIVE TO FREEZING2 in protecting chloroplasts against
RT freeze-induced damage in Arabidopsis.";
RL Plant J. 55:734-745(2008).
CC -!- FUNCTION: Galactosyltransferase synthesizing digalactosyldiacylglycerol
CC from monogalactosyldiacylglycerol in the absence of UDP-galactose (By
CC similarity). Potentially involved in freezing tolerance
CC (PubMed:18466306). {ECO:0000250|UniProtKB:Q93Y07,
CC ECO:0000269|PubMed:18466306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol = a 1,2-
CC diacyl-3-O-[beta-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol +
CC a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:15921, ChEBI:CHEBI:17615,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:87082; EC=2.4.1.184;
CC Evidence={ECO:0000250|UniProtKB:Q93Y07};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250|UniProtKB:Q93Y07}.
CC -!- MISCELLANEOUS: Rice SFR2 is able to rescue freezing tolerance phenotype
CC in Arabidopsis sfr2 mutant. {ECO:0000269|PubMed:18466306}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AJ491323; CAD36515.1; -; mRNA.
DR EMBL; DP000010; ABA95293.1; -; Genomic_DNA.
DR EMBL; DP000010; ABA95294.1; -; Genomic_DNA.
DR EMBL; DP000010; ABA95295.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF28826.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT15259.1; -; Genomic_DNA.
DR EMBL; CM000148; EAZ19256.1; -; Genomic_DNA.
DR RefSeq; XP_015617860.1; XM_015762374.1.
DR RefSeq; XP_015617862.1; XM_015762376.1.
DR RefSeq; XP_015617863.1; XM_015762377.1.
DR RefSeq; XP_015617864.1; XM_015762378.1.
DR RefSeq; XP_015617865.1; XM_015762379.1.
DR RefSeq; XP_015617866.1; XM_015762380.1.
DR RefSeq; XP_015617867.1; XM_015762381.1.
DR RefSeq; XP_015617868.1; XM_015762382.1.
DR RefSeq; XP_015617869.1; XM_015762383.1.
DR RefSeq; XP_015617870.1; XM_015762384.1.
DR RefSeq; XP_015617871.1; XM_015762385.1.
DR RefSeq; XP_015617872.1; XM_015762386.1.
DR RefSeq; XP_015617873.1; XM_015762387.1.
DR AlphaFoldDB; Q8L6H7; -.
DR SMR; Q8L6H7; -.
DR STRING; 4530.OS11T0683500-02; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q8L6H7; -.
DR PRIDE; Q8L6H7; -.
DR EnsemblPlants; Os11t0683500-02; Os11t0683500-02; Os11g0683500.
DR GeneID; 4351127; -.
DR Gramene; Os11t0683500-02; Os11t0683500-02; Os11g0683500.
DR KEGG; osa:4351127; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_11_0_1; -.
DR InParanoid; Q8L6H7; -.
DR OMA; DYIHEKS; -.
DR OrthoDB; 408001at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR ExpressionAtlas; Q8L6H7; baseline and differential.
DR Genevisible; Q8L6H7; OS.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102996; F:beta,beta digalactosyldiacylglycerol galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IEA:UniProt.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProt.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0046480; F:galactolipid galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 2.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Glycoprotein; Glycosidase; Glycosyltransferase; Hydrolase;
KW Membrane; Plastid; Plastid outer membrane; Reference proteome; Transferase.
FT CHAIN 1..647
FT /note="Beta-glucosidase-like SFR2, chloroplastic"
FT /id="PRO_0000390355"
FT REGION 116..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 303
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 466
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 511..512
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 647 AA; 73271 MW; 2724E1636C15C0A0 CRC64;
MPLPAFVAAA ARLAVLVAAA ATAANAASYA RYRRRHLRRI PSPIDESADP LADFRAFPSS
DADDSEEDNF FFGLATAPAH VEDRLEDAWL QFATETSCDD NGNVRDQRPV DALMASAAGD
GGSQQSWRST GGENIGDREQ RKPLRVAMEA MLRGFEILAE SGESAGGDNC SHNVAAWHNV
PCPQERLRFW SDPDAELKLA KETGISVFRM GVDWARLMPE EPTEELKSSV NFAALERYRW
IIQRVREYGM KVMLTLFHHS LPPWAGKYGG WKMEKTVTYF MDFVRLVVDR VSNLVDYWVI
FNEPHVFVML TYCAGAWPGG DPNAIEVATS TLPTGVYNQA LHWMAIAHSE AYDYIHSKSK
NERKPIVGVA HHVSFTRPYG LFDVAAVALA NSLTLFPYVD SICDKLDFIG INYYGQEVIS
GPGLKLVDND EYSESGRGVY PDGLFRILIQ FNERYKRLNI PFVITENGVS DETDLIRKPY
ILEHLLATYA AIIMGVRVLG YLFWTTSDNW EWADGYGPKF GLVAVDRANN LARKPRPSYF
LFSRVVTTGK ITRQDRMSAW RELQQAAVQK KTRPFFRAVD KHGRMYAGGL DRPIQRPFIL
RDWRFGHYKM EGLQDPLSCF IRCIFAPFSR QKKIHYIEDD VISYSIN
