ID RFS2_ARATH Reviewed; 773 AA. AC Q94A08; Q0WWI0; Q3EAI2; Q3EAI3; Q9SCM1; DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 2. DT 27-MAR-2024, entry version 111. DE RecName: Full=Probable galactinol--sucrose galactosyltransferase 2; DE EC=2.4.1.82; DE AltName: Full=Protein SEED IMBIBITION 2; DE AltName: Full=Raffinose synthase 2; GN Name=RFS2; Synonyms=RS2, SIP2; OrderedLocusNames=At3g57520; GN ORFNames=T8H10.120; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 435-773 (ISOFORM 1). RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP INDUCTION BY OXIDATIVE STRESS, GENE FAMILY, AND NOMENCLATURE. RX PubMed=18502973; DOI=10.1104/pp.108.122465; RA Nishizawa A., Yabuta Y., Shigeoka S.; RT "Galactinol and raffinose constitute a novel function to protect plants RT from oxidative damage."; RL Plant Physiol. 147:1251-1263(2008). CC -!- FUNCTION: Transglycosidase operating by a ping-pong reaction mechanism. CC Involved in the synthesis of raffinose, a major soluble carbohydrate in CC seeds, roots and tubers (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo- CC inositol + raffinose; Xref=Rhea:RHEA:20161, ChEBI:CHEBI:16634, CC ChEBI:CHEBI:17268, ChEBI:CHEBI:17505, ChEBI:CHEBI:17992; EC=2.4.1.82; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q94A08-1; Sequence=Displayed; CC Name=2; CC IsoId=Q94A08-2; Sequence=VSP_038414, VSP_038415; CC Name=3; CC IsoId=Q94A08-3; Sequence=VSP_038412, VSP_038413; CC -!- INDUCTION: By oxidative stress. {ECO:0000269|PubMed:18502973}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolases 36 family. CC {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; AL133248; CAB66109.1; -; Genomic_DNA. DR EMBL; CP002686; AEE79665.1; -; Genomic_DNA. DR EMBL; CP002686; AEE79667.1; -; Genomic_DNA. DR EMBL; AY050772; AAK92707.1; -; mRNA. DR EMBL; AK226370; BAE98518.1; -; mRNA. DR PIR; T46188; T46188. DR RefSeq; NP_191311.1; NM_115612.3. [Q94A08-1] DR RefSeq; NP_850715.1; NM_180384.1. [Q94A08-2] DR AlphaFoldDB; Q94A08; -. DR SMR; Q94A08; -. DR BioGRID; 10235; 2. DR STRING; 3702.Q94A08; -. DR CAZy; GH36; Glycoside Hydrolase Family 36. DR PaxDb; 3702-AT3G57520-1; -. DR ProteomicsDB; 236235; -. [Q94A08-1] DR EnsemblPlants; AT3G57520.1; AT3G57520.1; AT3G57520. [Q94A08-1] DR EnsemblPlants; AT3G57520.2; AT3G57520.2; AT3G57520. [Q94A08-2] DR GeneID; 824919; -. DR Gramene; AT3G57520.1; AT3G57520.1; AT3G57520. [Q94A08-1] DR Gramene; AT3G57520.2; AT3G57520.2; AT3G57520. [Q94A08-2] DR KEGG; ath:AT3G57520; -. DR Araport; AT3G57520; -. DR TAIR; AT3G57520; SIP2. DR eggNOG; ENOG502QPVE; Eukaryota. DR HOGENOM; CLU_007066_0_0_1; -. DR InParanoid; Q94A08; -. DR OMA; HVCPVMT; -. DR OrthoDB; 214587at2759; -. DR PhylomeDB; Q94A08; -. DR BioCyc; ARA:AT3G57520-MONOMER; -. DR BioCyc; MetaCyc:AT3G57520-MONOMER; -. DR BRENDA; 2.4.1.82; 399. DR PRO; PR:Q94A08; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q94A08; baseline and differential. DR GO; GO:0009506; C:plasmodesma; HDA:TAIR. DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IDA:TAIR. DR GO; GO:0034484; P:raffinose catabolic process; IDA:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR008811; Glycosyl_hydrolases_36. DR PANTHER; PTHR31268; -; 1. DR PANTHER; PTHR31268:SF32; GALACTINOL--SUCROSE GALACTOSYLTRANSFERASE 2-RELATED; 1. DR Pfam; PF05691; Raffinose_syn; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR Genevisible; Q94A08; AT. PE 2: Evidence at transcript level; KW Alternative splicing; Carbohydrate metabolism; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1..773 FT /note="Probable galactinol--sucrose galactosyltransferase FT 2" FT /id="PRO_0000389256" FT VAR_SEQ 552..565 FT /note="SLLKIWNMNKFTGI -> RCWLVQGNEEEPD (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_038412" FT VAR_SEQ 566..773 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_038413" FT VAR_SEQ 655..656 FT /note="EI -> DL (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_038414" FT VAR_SEQ 657..773 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_038415" FT CONFLICT 255 FT /note="Q -> R (in Ref. 3; AAK92707)" FT /evidence="ECO:0000305" SQ SEQUENCE 773 AA; 85143 MW; 0852F9E67952C8D3 CRC64; MTITSNISVQ NDNLVVQGKT ILTKIPDNII LTPVTGNGFV SGSFIGATFE QSKSLHVFPI GVLEGLRFMC CFRFKLWWMT QRMGSCGKDI PLETQFMLLE SKDEVEGNGD DAPTVYTVFL PLLEGQFRAV LQGNEKNEIE ICFESGDKAV ETSQGTHLVY VHAGTNPFEV IRQSVKAVER HMQTFHHREK KKLPSFLDWF GWCTWDAFYT DVTAEGVDEG LKSLSEGGTP PKFLIIDDGW QQIENKEKDE NCVVQEGAQF ATRLVGIKEN AKFQKSDQKD TQVSGLKSVV DNAKQRHNVK QVYAWHALAG YWGGVKPAAS GMEHYDSALA YPVQSPGVLG NQPDIVMDSL AVHGLGLVNP KKVFNFYNEL HSYLASCGID GVKVDVQNII ETLGAGLGGR VSLTRSYQQA LEASIARNFT DNGCISCMCH NTDGLYSAKQ TAIVRASDDF YPRDPASHTI HIASVAYNSL FLGEFMQPDW DMFHSLHPTA EYHAAARAVG GCAIYVSDKP GNHNFDLLRK LVLPDGSVLR AKLPGRPTRD CLFADPARDG ISLLKIWNMN KFTGIVGVFN CQGAGWCKET KKNQIHDTSP GTLTGSIRAD DADLISQVAG EDWSGDSIVY AYRSGEVVRL PKGASIPLTL KVLEYELFHI SPLKEITENI SFAPIGLVDM FNSSGAIESI DINHVTDKNP EFFDGEISSA SPALSDNRSP TALVSVSVRG CGRFGAYSSQ RPLKCAVEST ETDFTYDAEV GLVTLNLPVT REEMFRWHVE ILV //