EDA30_ARATH
ID EDA30_ARATH Reviewed; 656 AA.
AC F4J2C8; Q0WS93; Q9SRV8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 30 {ECO:0000303|PubMed:15634699};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase 22 {ECO:0000305};
DE Short=O-FucT-22 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
DE AltName: Full=Protein TUBE GROWTH DEFECTIVE 1 {ECO:0000303|PubMed:19237690};
GN Name=EDA30 {ECO:0000303|PubMed:15634699};
GN Synonyms=OFUT22 {ECO:0000305}, TGD1 {ECO:0000303|PubMed:19237690};
GN OrderedLocusNames=At3g03810 {ECO:0000312|Araport:AT3G03810};
GN ORFNames=F20H23.17 {ECO:0000312|EMBL:AAF00637.1};
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 [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].
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19237690; DOI=10.1534/genetics.108.090852;
RA Boavida L.C., Shuai B., Yu H.J., Pagnussat G.C., Sundaresan V.,
RA McCormick S.;
RT "A collection of Ds insertional mutants associated with defects in male
RT gametophyte development and function in Arabidopsis thaliana.";
RL Genetics 181:1369-1385(2009).
RN [6]
RP GENE FAMILY, AND 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 [7]
RP GENE FAMILY.
RX PubMed=22916179; DOI=10.1371/journal.pone.0042914;
RA Neumetzler L., Humphrey T., Lumba S., Snyder S., Yeats T.H., Usadel B.,
RA Vasilevski A., Patel J., Rose J.K., Persson S., Bonetta D.;
RT "The FRIABLE1 gene product affects cell adhesion in Arabidopsis.";
RL PLoS ONE 7:E42914-E42914(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.
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 -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Embryo sac development arrest. Unfused polar
CC nuclei (PubMed:15634699). Pollen tube growth defective
CC (PubMed:19237690). {ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:19237690}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF00637.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; AC009540; AAF00637.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE73996.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63558.1; -; Genomic_DNA.
DR EMBL; AK228044; BAF00006.1; -; mRNA.
DR RefSeq; NP_001325638.1; NM_001337489.1.
DR RefSeq; NP_187031.2; NM_111252.5.
DR AlphaFoldDB; F4J2C8; -.
DR STRING; 3702.AT3G03810.1; -.
DR PaxDb; F4J2C8; -.
DR PRIDE; F4J2C8; -.
DR ProteomicsDB; 247060; -.
DR EnsemblPlants; AT3G03810.1; AT3G03810.1; AT3G03810.
DR EnsemblPlants; AT3G03810.2; AT3G03810.2; AT3G03810.
DR GeneID; 821131; -.
DR Gramene; AT3G03810.1; AT3G03810.1; AT3G03810.
DR Gramene; AT3G03810.2; AT3G03810.2; AT3G03810.
DR KEGG; ath:AT3G03810; -.
DR Araport; AT3G03810; -.
DR TAIR; locus:2079404; AT3G03810.
DR eggNOG; ENOG502QQP9; Eukaryota.
DR HOGENOM; CLU_020836_0_0_1; -.
DR InParanoid; F4J2C8; -.
DR OMA; PEYYVTE; -.
DR OrthoDB; 253235at2759; -.
DR PRO; PR:F4J2C8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J2C8; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010197; P:polar nucleus fusion; IMP:TAIR.
DR GO; GO:0048868; P:pollen tube development; IMP:TAIR.
DR CDD; cd11299; O-FucT_plant; 1.
DR InterPro; IPR024709; FucosylTrfase_pln.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR Pfam; PF10250; O-FucT; 1.
DR PIRSF; PIRSF009360; UCP009360; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..656
FT /note="Protein EMBRYO SAC DEVELOPMENT ARREST 30"
FT /id="PRO_0000442084"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT REGION 381..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 221
FT /note="L -> M (in Ref. 3; BAF00006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 75038 MW; 8293CC6CC7D5C918 CRC64;
MVFKSRIKWI ALFVLILSMG SLVVHLSMTK SSGVQLAYSA RDNLWQDFDS LLGAQDFRNK
HLWRPVKSLE TLQPYANPRN SYPAPSSKNN GFIYAKIFGG FDKIRSSICD LVTISRLLNA
TLVIPELQES LRSKGISNKF KSFSYLYDEE QFIAFLKNDV IVMKTLPESL KAARKRNEFP
LFKPKNSASP KFYLEDVLPK LKKANVIGLI VSDGGCLQSA LPASMPELQR LRCRVAFHAL
QLRPEIQVLA KEMVDRLRKS GQPFLAYHPG LVREKLAYHG CAELFQDIHS ELIQYRRAQM
IKQRFILEEL IVDSRLRRDN GLCPLMPEEV GILLKALGYS QKAIIYLAGS EIFGGQRVLI
PLRAMFPNLV DRTSLCSTEE LSELVGPETP LPENTYKMPP RKSDKQLKEE WNKAGPRPRP
LPPPPDRPIY QHEKEGWYGW LTENDTEPSP SPMDLRNQAH RLLWDALDFA VSVEADVFFP
GFNNDGSGWP DFSSLVMGQR LYERPSSRTY RLDRKVIQEL FNITREDMYH PNRNWTLRVR
KHLNSSLGES GLIRQSMLSK PRSFLSHPLP ECSCRTSALE DSRQIQSDDG RFLYGGEDEC
PKWIKSAGVE KSKTDDGDQP DYDHDLLAEQ SETEEEFAKS KVASAFDQDE EWDPND
