MUR3_ARATH
ID MUR3_ARATH Reviewed; 619 AA.
AC Q7XJ98; Q0WWH9; Q494P2; Q9SK65; W8QNZ0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Xyloglucan galactosyltransferase MUR3 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Protein KATAMARI {ECO:0000303|PubMed:15863516};
DE AltName: Full=Protein MURUS 3 {ECO:0000303|PubMed:12837954};
DE Short=AtMUR3 {ECO:0000303|PubMed:12837954};
DE AltName: Full=Protein SHORT ROOT IN SALT MEDIUM 3 {ECO:0000303|PubMed:23571490};
GN Name=MUR3 {ECO:0000303|PubMed:12837954};
GN Synonyms=KAM1 {ECO:0000303|PubMed:15863516},
GN RSA3 {ECO:0000303|PubMed:23571490}; OrderedLocusNames=At2g20370;
GN ORFNames=F11A3.8;
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 [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ALA-290 AND
RP SER-470, AND TISSUE SPECIFICITY.
RX PubMed=12837954; DOI=10.1105/tpc.009837;
RA Madson M., Dunand C., Li X., Verma R., Vanzin G.F., Caplan J., Shoue D.A.,
RA Carpita N.C., Reiter W.-D.;
RT "The MUR3 gene of Arabidopsis encodes a xyloglucan galactosyltransferase
RT that is evolutionarily related to animal exostosins.";
RL Plant Cell 15:1662-1670(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=15020758; DOI=10.1104/pp.103.036285;
RA Li X., Cordero I., Caplan J., Moelhoej M., Reiter W.D.;
RT "Molecular analysis of 10 coding regions from Arabidopsis that are
RT homologous to the MUR3 xyloglucan galactosyltransferase.";
RL Plant Physiol. 134:940-950(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RX PubMed=15863516; DOI=10.1105/tpc.105.031930;
RA Tamura K., Shimada T., Kondo M., Nishimura M., Hara-Nishimura I.;
RT "KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required for
RT endomembrane organization in Arabidopsis.";
RL Plant Cell 17:1764-1776(2005).
RN [9]
RP MUTAGENESIS OF SER-470 AND THR-539.
RX PubMed=18657237; DOI=10.1111/j.1365-313x.2008.03636.x;
RA Tedman-Jones J.D., Lei R., Jay F., Fabro G., Li X., Reiter W.D.,
RA Brearley C., Jones J.D.;
RT "Characterization of Arabidopsis mur3 mutations that result in constitutive
RT activation of defence in petioles, but not leaves.";
RL Plant J. 56:691-703(2008).
RN [10]
RP FUNCTION, INDUCTION BY SALT STRESS, AND DISRUPTION PHENOTYPE.
RX PubMed=23571490; DOI=10.1093/mp/sst062;
RA Li W., Guan Q., Wang Z.Y., Wang Y., Zhu J.;
RT "A bi-functional xyloglucan galactosyltransferase is an indispensable salt
RT stress tolerance determinant in Arabidopsis.";
RL Mol. Plant 6:1344-1354(2013).
RN [11]
RP FUNCTION, INTERACTION WITH CSLC4 AND FUT1, AND SUBCELLULAR LOCATION.
RX PubMed=25392066; DOI=10.1093/pcp/pcu161;
RA Chou Y.H., Pogorelko G., Young Z.T., Zabotina O.A.;
RT "Protein-protein interactions among xyloglucan-synthesizing enzymes and
RT formation of Golgi-localized multiprotein complexes.";
RL Plant Cell Physiol. 56:255-267(2015).
CC -!- FUNCTION: Involved in the attachment of the Gal residue on the third
CC xylosyl unit within the XXXG core structure of xyloglucan, the
CC principal glycan that interlaces the cellulose microfibrils in plant
CC cell wall (PubMed:12837954). Associates with other xyloglucan-
CC synthesizing enzymes to form multiprotein complexes for xyloglucan
CC synthesis in the Golgi (PubMed:25392066). Interacts with actin and is
CC required for the proper endomembrane organization and for the cell
CC elongation. Not involved in the trafficking from the endoplasmic
CC reticulum to the vacuoles (PubMed:15863516). Involved in salt stress
CC tolerance. Participates in the control of the expression of genes
CC encoding for proteins involved in reactive oxygen species (ROS)
CC detoxification under salt stress. May contribute to the maintenance of
CC the proper organization of actin microfilaments during salt stress-
CC induced ROS production (PubMed:23571490). {ECO:0000269|PubMed:12837954,
CC ECO:0000269|PubMed:15863516, ECO:0000269|PubMed:23571490,
CC ECO:0000269|PubMed:25392066}.
CC -!- SUBUNIT: Interacts with CSLC4 and FUT1. {ECO:0000269|PubMed:25392066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:15863516}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:15863516}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:25392066}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:25392066}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12837954}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:23571490}.
CC -!- DOMAIN: The cytoplasmic N-terminal domain interacts with actin, while
CC the lumenal C-terminal domain contributes to the activity of xyloglucan
CC galactosyltransferase. {ECO:0000269|PubMed:15863516}.
CC -!- DISRUPTION PHENOTYPE: Stunted growth. {ECO:0000269|PubMed:15863516,
CC ECO:0000269|PubMed:23571490}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY195743; AAO39815.1; -; Genomic_DNA.
DR EMBL; KJ138908; AHL38848.1; -; mRNA.
DR EMBL; AC006569; AAD21751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06999.1; -; Genomic_DNA.
DR EMBL; BT023734; AAZ23926.1; -; mRNA.
DR EMBL; AK226372; BAE98519.1; -; mRNA.
DR PIR; D84588; D84588.
DR RefSeq; NP_179627.2; NM_127596.3.
DR AlphaFoldDB; Q7XJ98; -.
DR BioGRID; 1909; 8.
DR STRING; 3702.AT2G20370.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR SwissPalm; Q7XJ98; -.
DR PaxDb; Q7XJ98; -.
DR PRIDE; Q7XJ98; -.
DR ProteomicsDB; 251380; -.
DR EnsemblPlants; AT2G20370.1; AT2G20370.1; AT2G20370.
DR GeneID; 816556; -.
DR Gramene; AT2G20370.1; AT2G20370.1; AT2G20370.
DR KEGG; ath:AT2G20370; -.
DR Araport; AT2G20370; -.
DR TAIR; locus:2039002; AT2G20370.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_2_0_1; -.
DR InParanoid; Q7XJ98; -.
DR OMA; NIENQIH; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q7XJ98; -.
DR BioCyc; ARA:AT2G20370-MON; -.
DR BioCyc; MetaCyc:AT2G20370-MON; -.
DR PRO; PR:Q7XJ98; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7XJ98; baseline and differential.
DR Genevisible; Q7XJ98; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0010256; P:endomembrane system organization; IMP:TAIR.
DR GO; GO:0042353; P:fucose biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IMP:TAIR.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Stress response; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..619
FT /note="Xyloglucan galactosyltransferase MUR3"
FT /id="PRO_0000149667"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15863516"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..619
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:15863516"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 290
FT /note="A->V: In mur3-2; altered xyloglucan, but normal
FT endomembrane organization."
FT /evidence="ECO:0000269|PubMed:12837954"
FT MUTAGEN 470
FT /note="S->L: In mur3-1; altered xyloglucan, but normal
FT endomembrane organization. In mur3-5 and cie1; stunted
FT growth; when associated with I-539."
FT /evidence="ECO:0000269|PubMed:12837954,
FT ECO:0000269|PubMed:18657237"
FT MUTAGEN 539
FT /note="T->I: In mur3-5 and cie1; stunted growth; when
FT associated with L-470."
FT /evidence="ECO:0000269|PubMed:18657237"
FT CONFLICT 87
FT /note="E -> G (in Ref. 6; BAE98519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 70744 MW; 16CB8D880CBC893D CRC64;
MFPRVSMRRR SAEVSPTEPM EKGNGKNQTN RICLLVALSL FFWALLLYFH FVVLGTSNID
KQLQLQPSYA QSQPSSVSLR VDKFPIEPHA APSKPPPKEP LVTIDKPILP PAPVANSSST
FKPPRIVESG KKQEFSFIRA LKTVDNKSDP CGGKYIYVHN LPSKFNEDML RDCKKLSLWT
NMCKFTTNAG LGPPLENVEG VFSDEGWYAT NQFAVDVIFS NRMKQYKCLT NDSSLAAAIF
VPFYAGFDIA RYLWGYNISR RDAASLELVD WLMKRPEWDI MRGKDHFLVA GRITWDFRRL
SEEETDWGNK LLFLPAAKNM SMLVVESSPW NANDFGIPYP TYFHPAKDSE VFEWQDRMRN
LERKWLFSFA GAPRPDNPKS IRGQIIDQCR NSNVGKLLEC DFGESKCHAP SSIMQMFQSS
LFCLQPQGDS YTRRSAFDSM LAGCIPVFFH PGSAYTQYTW HLPKNYTTYS VFIPEDDVRK
RNISIEERLL QIPAKQVKIM RENVINLIPR LIYADPRSEL ETQKDAFDVS VQAVIDKVTR
LRKNMIEGRT EYDYFVEENS WKYALLEEGQ REAGGHVWDP FFSKPKPGED GSSDGNGGTT
ISADAAKNSW KSEQRDKTQ
