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Xyloglucan galactosyltransferase MUR3 (EC 2.4.1.-) (Protein KATAMARI) (Protein MURUS 3) (AtMUR3) (Protein SHORT ROOT IN SALT MEDIUM 3)

 MUR3_ARATH              Reviewed;         619 AA.
Q7XJ98; Q0WWH9; Q494P2; Q9SK65; W8QNZ0;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-OCT-2017, entry version 94.
RecName: Full=Xyloglucan galactosyltransferase MUR3 {ECO:0000305};
EC=2.4.1.- {ECO:0000305};
AltName: Full=Protein KATAMARI {ECO:0000303|PubMed:15863516};
AltName: Full=Protein MURUS 3 {ECO:0000303|PubMed:12837954};
Short=AtMUR3 {ECO:0000303|PubMed:12837954};
AltName: Full=Protein SHORT ROOT IN SALT MEDIUM 3 {ECO:0000303|PubMed:23571490};
Name=MUR3 {ECO:0000303|PubMed:12837954};
Synonyms=KAM1 {ECO:0000303|PubMed:15863516},
RSA3 {ECO:0000303|PubMed:23571490}; OrderedLocusNames=At2g20370;
ORFNames=F11A3.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ALA-290
AND SER-470, AND TISSUE SPECIFICITY.
PubMed=12837954; DOI=10.1105/tpc.009837;
Madson M., Dunand C., Li X., Verma R., Vanzin G.F., Caplan J.,
Shoue D.A., Carpita N.C., Reiter W.-D.;
"The MUR3 gene of Arabidopsis encodes a xyloglucan
galactosyltransferase that is evolutionarily related to animal
exostosins.";
Plant Cell 15:1662-1670(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=24905498; DOI=10.1111/tpj.12577;
Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
Smith-Moritz A.M., Plahar H., Chiu T.-Y.,
Gonzalez Fernandez-Nino S.M.G., Ebert B., Yang F., Christiansen K.M.,
Hansen S.F., Stonebloom S., Adams P.D., Ronald P.C., Hillson N.J.,
Hadi M.Z., Vega-Sanchez M.E., Loque D., Scheller H.V.,
Heazlewood J.L.;
"The plant glycosyltransferase clone collection for functional
genomics.";
Plant J. 79:517-529(2014).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY.
PubMed=15020758; DOI=10.1104/pp.103.036285;
Li X., Cordero I., Caplan J., Moelhoej M., Reiter W.D.;
"Molecular analysis of 10 coding regions from Arabidopsis that are
homologous to the MUR3 xyloglucan galactosyltransferase.";
Plant Physiol. 134:940-950(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
PubMed=15863516; DOI=10.1105/tpc.105.031930;
Tamura K., Shimada T., Kondo M., Nishimura M., Hara-Nishimura I.;
"KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required
for endomembrane organization in Arabidopsis.";
Plant Cell 17:1764-1776(2005).
[9]
MUTAGENESIS OF SER-470 AND THR-539.
PubMed=18657237; DOI=10.1111/j.1365-313X.2008.03636.x;
Tedman-Jones J.D., Lei R., Jay F., Fabro G., Li X., Reiter W.D.,
Brearley C., Jones J.D.;
"Characterization of Arabidopsis mur3 mutations that result in
constitutive activation of defence in petioles, but not leaves.";
Plant J. 56:691-703(2008).
[10]
FUNCTION, INDUCTION BY SALT STRESS, AND DISRUPTION PHENOTYPE.
PubMed=23571490; DOI=10.1093/mp/sst062;
Li W., Guan Q., Wang Z.Y., Wang Y., Zhu J.;
"A bi-functional xyloglucan galactosyltransferase is an indispensable
salt stress tolerance determinant in Arabidopsis.";
Mol. Plant 6:1344-1354(2013).
[11]
FUNCTION, INTERACTION WITH CSLC4 AND FUT1, AND SUBCELLULAR LOCATION.
PubMed=25392066; DOI=10.1093/pcp/pcu161;
Chou Y.H., Pogorelko G., Young Z.T., Zabotina O.A.;
"Protein-protein interactions among xyloglucan-synthesizing enzymes
and formation of Golgi-localized multiprotein complexes.";
Plant Cell Physiol. 56:255-267(2015).
-!- FUNCTION: Involved in the attachment of the Gal residue on the
third xylosyl unit within the XXXG core structure of xyloglucan,
the principal glycan that interlaces the cellulose microfibrils in
plant cell wall (PubMed:12837954). Associates with other
xyloglucan-synthesizing enzymes to form multiprotein complexes for
xyloglucan synthesis in the Golgi (PubMed:25392066). Interacts
with actin and is required for the proper endomembrane
organization and for the cell elongation. Not involved in the
trafficking from the endoplasmic reticulum to the vacuoles
(PubMed:15863516). Involved in salt stress tolerance. Participates
in the control of the expression of genes encoding for proteins
involved in reactive oxygen species (ROS) detoxification under
salt stress. May contribute to the maintenance of the proper
organization of actin microfilaments during salt stress-induced
ROS production (PubMed:23571490). {ECO:0000269|PubMed:12837954,
ECO:0000269|PubMed:15863516, ECO:0000269|PubMed:23571490,
ECO:0000269|PubMed:25392066}.
-!- SUBUNIT: Interacts with CSLC4 and FUT1.
{ECO:0000269|PubMed:25392066}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
{ECO:0000269|PubMed:15863516}; Single-pass type II membrane
protein {ECO:0000305|PubMed:15863516}. Golgi apparatus membrane
{ECO:0000269|PubMed:25392066}; Single-pass type II membrane
protein {ECO:0000305|PubMed:25392066}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12837954}.
-!- INDUCTION: By salt stress. {ECO:0000269|PubMed:23571490}.
-!- DOMAIN: The cytoplasmic N-terminal domain interacts with actin,
while the lumenal C-terminal domain contributes to the activity of
xyloglucan galactosyltransferase. {ECO:0000269|PubMed:15863516}.
-!- DISRUPTION PHENOTYPE: Stunted growth.
{ECO:0000269|PubMed:15863516, ECO:0000269|PubMed:23571490}.
-!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD21751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY195743; AAO39815.1; -; Genomic_DNA.
EMBL; KJ138908; AHL38848.1; -; mRNA.
EMBL; AC006569; AAD21751.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC06999.1; -; Genomic_DNA.
EMBL; BT023734; AAZ23926.1; -; mRNA.
EMBL; AK226372; BAE98519.1; -; mRNA.
PIR; D84588; D84588.
RefSeq; NP_179627.2; NM_127596.3.
UniGene; At.39706; -.
BioGrid; 1909; 8.
STRING; 3702.AT2G20370.1; -.
CAZy; GT47; Glycosyltransferase Family 47.
SwissPalm; Q7XJ98; -.
PaxDb; Q7XJ98; -.
EnsemblPlants; AT2G20370.1; AT2G20370.1; AT2G20370.
GeneID; 816556; -.
Gramene; AT2G20370.1; AT2G20370.1; AT2G20370.
KEGG; ath:AT2G20370; -.
Araport; AT2G20370; -.
TAIR; locus:2039002; AT2G20370.
eggNOG; KOG1021; Eukaryota.
eggNOG; ENOG410XTFH; LUCA.
HOGENOM; HOG000239726; -.
InParanoid; Q7XJ98; -.
KO; K20888; -.
OMA; PEWDIMR; -.
OrthoDB; EOG093606IH; -.
PhylomeDB; Q7XJ98; -.
BioCyc; ARA:AT2G20370-MONOMER; -.
BioCyc; MetaCyc:AT2G20370-MONOMER; -.
PRO; PR:Q7XJ98; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; Q7XJ98; AT.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0030173; C:integral component of Golgi membrane; IDA:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IDA:TAIR.
GO; GO:0010256; P:endomembrane system organization; IMP:TAIR.
GO; GO:0042353; P:fucose biosynthetic process; IMP:TAIR.
GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:TAIR.
GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
GO; GO:0009969; P:xyloglucan biosynthetic process; IMP:TAIR.
InterPro; IPR004263; Exostosin.
Pfam; PF03016; Exostosin; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
Membrane; Reference proteome; Signal-anchor; Stress response;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 619 Xyloglucan galactosyltransferase MUR3.
/FTId=PRO_0000149667.
TOPO_DOM 1 33 Cytoplasmic.
{ECO:0000305|PubMed:15863516}.
TRANSMEM 34 54 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 55 619 Lumenal. {ECO:0000305|PubMed:15863516}.
COMPBIAS 85 124 Pro-rich.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 465 465 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 290 290 A->V: In mur3-2; altered xyloglucan, but
normal endomembrane organization.
{ECO:0000269|PubMed:12837954}.
MUTAGEN 470 470 S->L: In mur3-1; altered xyloglucan, but
normal endomembrane organization. In
mur3-5 and cie1; stunted growth; when
associated with I-539.
{ECO:0000269|PubMed:12837954,
ECO:0000269|PubMed:18657237}.
MUTAGEN 539 539 T->I: In mur3-5 and cie1; stunted growth;
when associated with L-470.
{ECO:0000269|PubMed:18657237}.
CONFLICT 87 87 E -> G (in Ref. 6; BAE98519).
{ECO:0000305}.
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


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