MSR1_ARATH
ID MSR1_ARATH Reviewed; 422 AA.
AC Q9LU40; Q8LA51;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein MANNAN SYNTHESIS-RELATED 1 {ECO:0000303|PubMed:22966747};
DE Short=AtMSR1 {ECO:0000303|PubMed:22966747};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase 25 {ECO:0000305};
DE Short=O-FucT-25 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31429.1};
GN Name=MSR1 {ECO:0000303|PubMed:22966747, ECO:0000312|EMBL:ARJ31429.1};
GN Synonyms=OFUT25 {ECO:0000305};
GN OrderedLocusNames=At3g21190 {ECO:0000312|Araport:AT3G21190};
GN ORFNames=MXL8.4 {ECO:0000312|EMBL:BAB01710.1};
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].
RC STRAIN=cv. Columbia;
RA Zeng W., Gluza P., Heazlewood J.;
RT "Arabidopsis glycosyltransferases: an update.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP REVIEW.
RX PubMed=22629278; DOI=10.3389/fpls.2012.00059;
RA Hansen S.F., Harholt J., Oikawa A., Scheller H.V.;
RT "Plant glycosyltransferases beyond CAZy: a perspective on DUF families.";
RL Front. Plant Sci. 3:59-59(2012).
RN [8]
RP GENE FAMILY.
RX PubMed=23272088; DOI=10.1371/journal.pone.0051129;
RA Voxeur A., Andre A., Breton C., Lerouge P.;
RT "Identification of putative rhamnogalacturonan-II specific
RT glycosyltransferases in Arabidopsis using a combination of bioinformatics
RT approaches.";
RL PLoS ONE 7:E51129-E51129(2012).
RN [9]
RP GENE FAMILY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22966747; DOI=10.1111/tpj.12019;
RA Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT "Identification of an additional protein involved in mannan biosynthesis.";
RL Plant J. 73:105-117(2013).
RN [10]
RP WEB RESOURCE.
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).
CC -!- FUNCTION: Glycosyltransferase involved in mannan biosynthesis.
CC {ECO:0000269|PubMed:22966747}.
CC -!- PATHWAY: Glycan biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22966747}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22966747}.
CC -!- DISRUPTION PHENOTYPE: Decreased of mannosyl levels due to a reduction
CC of glucomannan content. {ECO:0000269|PubMed:22966747}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; KY906065; ARJ31429.1; -; mRNA.
DR EMBL; AB023045; BAB01710.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76474.1; -; Genomic_DNA.
DR EMBL; BT005762; AAO64166.1; -; mRNA.
DR EMBL; BT006084; AAP04069.1; -; mRNA.
DR EMBL; AK228514; BAF00437.1; -; mRNA.
DR EMBL; AY088029; AAM65575.1; -; mRNA.
DR RefSeq; NP_566677.1; NM_113014.4.
DR AlphaFoldDB; Q9LU40; -.
DR STRING; 3702.AT3G21190.1; -.
DR PaxDb; Q9LU40; -.
DR PRIDE; Q9LU40; -.
DR ProteomicsDB; 250791; -.
DR EnsemblPlants; AT3G21190.1; AT3G21190.1; AT3G21190.
DR GeneID; 821672; -.
DR Gramene; AT3G21190.1; AT3G21190.1; AT3G21190.
DR KEGG; ath:AT3G21190; -.
DR Araport; AT3G21190; -.
DR TAIR; locus:2094731; AT3G21190.
DR eggNOG; ENOG502QUE8; Eukaryota.
DR HOGENOM; CLU_018420_3_0_1; -.
DR InParanoid; Q9LU40; -.
DR OMA; IRVASYF; -.
DR OrthoDB; 695946at2759; -.
DR PhylomeDB; Q9LU40; -.
DR PRO; PR:Q9LU40; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU40; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0051753; F:mannan synthase activity; IMP:UniProtKB.
DR GO; GO:0052325; P:cell wall pectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010412; P:mannan metabolic process; IMP:UniProtKB.
DR GO; GO:0097502; P:mannosylation; IMP:UniProtKB.
DR CDD; cd11299; O-FucT_plant; 1.
DR InterPro; IPR024709; FucosylTrfase_pln.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR PANTHER; PTHR31288; PTHR31288; 1.
DR Pfam; PF10250; O-FucT; 1.
DR PIRSF; PIRSF009360; UCP009360; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Fucose metabolism; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..422
FT /note="Protein MANNAN SYNTHESIS-RELATED 1"
FT /id="PRO_0000442087"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 27..422
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 263..265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CONFLICT 214
FT /note="S -> A (in Ref. 6; AAM65575)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> I (in Ref. 6; AAM65575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46799 MW; 9B060067EDA54806 CRC64;
MGVDLRQVVA GILTITMFVM LGQMLHRDYF DSLQEKAQGD AQDIEFEGSK VSVKDGLVGT
VEGSKGLWME DNTDLTPCWP TLLSDDAVSS KGYVTFSLTN GPEYHISQIT DAVMVAKHLG
ATLVLPDIRG SKPGDERNFE DIYDADKLIK SLENVVKVVK KLPEEVSLRN MAIVKVPTRV
TEDYIKEHID PIFKSKGNIR VASYFPSVNL RKSSQDGETD PVACLAMFGS LELQPEVNAV
AESMVERLRT HSRKSGGRFI AVDLRIDILE KKNCHTTGVV GSKTCYNAQE IALFLRKLGF
ASDTTIYLTQ PRWDSSLNIL KDIFPKTFTK EAIMPASKRS KYLESVSSEY ENVIDFYISS
RSDVFVPAIS GLFYANTVGK RIALGKPQVL VPAEISETSG LATDFISPYI SKKNHLAYSC
FC
