MGP4_ARATH
ID MGP4_ARATH Reviewed; 360 AA.
AC Q9M146; Q5HZ43; Q94K03;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase MGP4 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Protein MALE GAMETOPHYTE DEFECTIVE 4 {ECO:0000303|PubMed:21288267};
DE AltName: Full=Rhamnogalacturonan xylosyltransferase MGP4 {ECO:0000305};
GN Name=MGP4 {ECO:0000303|PubMed:21288267}; OrderedLocusNames=At4g01220;
GN ORFNames=F2N1.35;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 2).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21288267; DOI=10.1111/j.1365-313x.2010.04452.x;
RA Liu X.L., Liu L., Niu Q.K., Xia C., Yang K.Z., Li R., Chen L.Q.,
RA Zhang X.Q., Zhou Y., Ye D.;
RT "Male gametophyte defective 4 encodes a rhamnogalacturonan II
RT xylosyltransferase and is important for growth of pollen tubes and roots in
RT Arabidopsis.";
RL Plant J. 65:647-660(2011).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21421394; DOI=10.1016/j.plantsci.2010.11.002;
RA Fangel J.U., Petersen B.L., Jensen N.B., Willats W.G., Bacic A.,
RA Egelund J.;
RT "A putative Arabidopsis thaliana glycosyltransferase, At4g01220, which is
RT closely related to three plant cell wall-specific xylosyltransferases, is
RT differentially expressed spatially and temporally.";
RL Plant Sci. 180:470-479(2011).
CC -!- FUNCTION: Catalyzes the transfer of D-xylose from UDP-alpha-D-xylose
CC onto L-fucose. Probably involved in the biosynthesis of
CC rhamnogalacturonan II (RG-II) through xylosylation of the internal
CC fucose moiety of the A-chain of RG-II, a structurally complex pectic
CC polysaccharide of the primary cell wall. RG-II is essential for the
CC cell wall integrity of rapidly growing tissues such as roots and pollen
CC tube growth and elongation. {ECO:0000269|PubMed:21288267}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:21288267, ECO:0000305|PubMed:21421394}; Single-pass
CC type II membrane protein {ECO:0000305|PubMed:21288267,
CC ECO:0000305|PubMed:21421394}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M146-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M146-2; Sequence=VSP_053260, VSP_053261;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21288267,
CC ECO:0000269|PubMed:21421394}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility due to impaired growth of
CC pollen tubes in the transmitting tract during fertilization.
CC {ECO:0000269|PubMed:21288267}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
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DR EMBL; AL161491; CAB80931.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81995.1; -; Genomic_DNA.
DR EMBL; AF370497; AAK43874.1; -; mRNA.
DR EMBL; CP002687; AEE81996.1; -; Genomic_DNA.
DR EMBL; BT020481; AAW38982.1; -; mRNA.
DR EMBL; BT033130; ACF28391.1; -; mRNA.
DR PIR; A85016; A85016.
DR RefSeq; NP_567211.1; NM_116352.3. [Q9M146-2]
DR RefSeq; NP_849279.1; NM_178948.3. [Q9M146-1]
DR AlphaFoldDB; Q9M146; -.
DR STRING; 3702.AT4G01220.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q9M146; -.
DR PRIDE; Q9M146; -.
DR ProteomicsDB; 239060; -. [Q9M146-1]
DR EnsemblPlants; AT4G01220.1; AT4G01220.1; AT4G01220. [Q9M146-1]
DR EnsemblPlants; AT4G01220.2; AT4G01220.2; AT4G01220. [Q9M146-2]
DR GeneID; 828028; -.
DR Gramene; AT4G01220.1; AT4G01220.1; AT4G01220. [Q9M146-1]
DR Gramene; AT4G01220.2; AT4G01220.2; AT4G01220. [Q9M146-2]
DR KEGG; ath:AT4G01220; -.
DR Araport; AT4G01220; -.
DR TAIR; locus:2124968; AT4G01220.
DR eggNOG; ENOG502QT5X; Eukaryota.
DR HOGENOM; CLU_051257_0_0_1; -.
DR InParanoid; Q9M146; -.
DR OMA; GKHDVYF; -.
DR PhylomeDB; Q9M146; -.
DR PRO; PR:Q9M146; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M146; baseline and differential.
DR Genevisible; Q9M146; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042285; F:xylosyltransferase activity; IDA:TAIR.
DR GO; GO:0048868; P:pollen tube development; IMP:TAIR.
DR GO; GO:0010306; P:rhamnogalacturonan II biosynthetic process; IMP:TAIR.
DR InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03407; Nucleotid_trans; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
FT MGP4"
FT /id="PRO_0000423716"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..360
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 191..193
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 292..299
FT /note="DMYLLSQA -> CSFFLVPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.4"
FT /id="VSP_053260"
FT VAR_SEQ 300..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.4"
FT /id="VSP_053261"
FT CONFLICT 71
FT /note="L -> H (in Ref. 3; AAK43874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41121 MW; A7E4CBAE9369D931 CRC64;
MAQQKFLHQR PIQNPFTNPF SSSPLSTSSI SNRPISLLSR NGLLLLLALL VILGVFLPWA
GSPLFPSPNK LSPSQSKWRD YSLPQAVKFV AKNGTVIVCA VSYPYLPFLN NWLISVSRQK
HQDQVLVIAE DYATLYKVNE KWPGHAVLIP PALDSQTAHK FGSQGFFNFT ARRPQHLLEI
LELGYNVMYN DVDMVWLQDP FQYLEGKHDA YFMDDMTAIK PLDHSHDLPP PGKKGRTYIC
SCMIFLRPTN GAKLLMKKWI EELETQPWSR AKKANDQPGF NWALNKTANQ VDMYLLSQAA
FPTGGLYFKN KTWVKETKGK HAIIHNNYIV GFEKKIKRFR DFNLWLVDDH ASESPLGKLE
