DEX1_ARATH
ID DEX1_ARATH Reviewed; 896 AA.
AC F4IYM4; B3H6A9; F4IYM3; Q84TH7; Q9FV29; Q9FV30; Q9SS78;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein DEFECTIVE IN EXINE FORMATION 1 {ECO:0000303|PubMed:11743117};
DE Flags: Precursor;
GN Name=DEX1 {ECO:0000303|PubMed:11743117};
GN OrderedLocusNames=At3g09090 {ECO:0000312|Araport:AT3G09090};
GN ORFNames=MZB10.12 {ECO:0000312|EMBL:AAD56325.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11743117; DOI=10.1104/pp.010517;
RA Paxson-Sowders D.M., Dodrill C.H., Owen H.A., Makaroff C.A.;
RT "DEX1, a novel plant protein, is required for exine pattern formation
RT during pollen development in Arabidopsis.";
RL Plant Physiol. 127:1739-1749(2001).
RN [2]
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 [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] OF 6-896 (ISOFORM 1).
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] OF 6-896 (ISOFORM 1).
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.
CC -!- FUNCTION: Required for exine pattern formation during pollen
CC development, especially for primexine deposition.
CC {ECO:0000269|PubMed:11743117}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4IYM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IYM4-2; Sequence=VSP_057386;
CC Name=3;
CC IsoId=F4IYM4-3; Sequence=VSP_057387;
CC -!- TISSUE SPECIFICITY: Mostly expressed in buds, and, to a lower extent,
CC in leaves, roots and seedlings. {ECO:0000269|PubMed:11743117}.
CC -!- DISRUPTION PHENOTYPE: Male sterile. Defective pollen wall pattern
CC formation at early tetrad stage; delayed and reduced primexine
CC deposition, as well as abnormal rippling of the plasma membrane and no
CC production of spacers. Random sporopollenin deposition on the plasma
CC membrane along the microspore wall. {ECO:0000269|PubMed:11743117}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD56325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF257186; AAG31444.1; -; Genomic_DNA.
DR EMBL; AF257187; AAG31445.1; -; mRNA.
DR EMBL; AC009326; AAD56325.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74719.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74720.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74721.1; -; Genomic_DNA.
DR EMBL; BT005785; AAO64188.1; -; mRNA.
DR EMBL; AK228583; BAF00499.1; -; mRNA.
DR RefSeq; NP_001118602.1; NM_001125130.1. [F4IYM4-2]
DR RefSeq; NP_001189844.1; NM_001202915.1. [F4IYM4-3]
DR RefSeq; NP_566343.1; NM_111744.5. [F4IYM4-1]
DR AlphaFoldDB; F4IYM4; -.
DR STRING; 3702.AT3G09090.1; -.
DR PaxDb; F4IYM4; -.
DR PRIDE; F4IYM4; -.
DR ProteomicsDB; 224248; -. [F4IYM4-1]
DR EnsemblPlants; AT3G09090.1; AT3G09090.1; AT3G09090. [F4IYM4-1]
DR EnsemblPlants; AT3G09090.2; AT3G09090.2; AT3G09090. [F4IYM4-2]
DR EnsemblPlants; AT3G09090.3; AT3G09090.3; AT3G09090. [F4IYM4-3]
DR GeneID; 820063; -.
DR Gramene; AT3G09090.1; AT3G09090.1; AT3G09090. [F4IYM4-1]
DR Gramene; AT3G09090.2; AT3G09090.2; AT3G09090. [F4IYM4-2]
DR Gramene; AT3G09090.3; AT3G09090.3; AT3G09090. [F4IYM4-3]
DR KEGG; ath:AT3G09090; -.
DR Araport; AT3G09090; -.
DR TAIR; locus:2095274; AT3G09090.
DR eggNOG; ENOG502QRZ6; Eukaryota.
DR HOGENOM; CLU_007690_0_0_1; -.
DR InParanoid; F4IYM4; -.
DR OMA; TMWGDED; -.
DR OrthoDB; 180923at2759; -.
DR PRO; PR:F4IYM4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4IYM4; baseline and differential.
DR Genevisible; F4IYM4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010584; P:pollen exine formation; IMP:UniProtKB.
DR GO; GO:0010208; P:pollen wall assembly; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045232; FAM234.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR21419; PTHR21419; 1.
DR Pfam; PF01839; FG-GAP; 1.
DR SUPFAM; SSF69318; SSF69318; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell wall biogenesis/degradation;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..896
FT /note="Protein DEFECTIVE IN EXINE FORMATION 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431810"
FT TOPO_DOM 25..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 268..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 791..894
FT /note="TTTLLVPGNYQGERRITQSQIYDRPGKYRIKLPTVGVRTTGTVMVEMADKNG
FT LHFSDEFSLTFHMYYYKLLKWLLVLPMLGMFGLLVILRPQEAVPLPSFSRNT -> TLF
FT SNTDDAVGSRQLPGREEDNAEP (in isoform 2)"
FT /id="VSP_057386"
FT VAR_SEQ 875..896
FT /note="LLVILRPQEAVPLPSFSRNTDL -> GTHPHRAHQKDPGTISC (in
FT isoform 3)"
FT /id="VSP_057387"
FT CONFLICT 229
FT /note="T -> I (in Ref. 1; AAG31445)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> R (in Ref. 1; AAG31445/AAG31444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 99711 MW; 027B36C638763C83 CRC64;
MKSRARQCLL VCLLCLSLTN LSYGENKFRE RKATDDELGY PDIDEDALLN TQCPKKLELR
WQTEVTSSVY ATPLIADINS DGKLDIVVPS FVHYLEVLEG ADGDKMPGWP AFHQSNVHSS
PLLFDIDKDG VREIALATYN AEVLFFRVSG FLMSDKLEVP RRKVHKNWHV GLNPDPVDRS
HPDVHDDVLE EEAMAMKSST TQTNATTTTP NVTVSMTKEV HGANSYVSTQ EDQKRPENNQ
TEAIVKPTPE LHNSSMDAGA NNLAANATTA GSRENLNRNV TTNEVDQSKI SGDKNETVIK
LNTSTGNSSE TLGTSGNSST AETVTKSGRR LLEEDGSKES VDSHSDSKDN SEGVRMATVE
NDGGLEADAD SSFELLREND ELADEYSYDY DDYVDEKMWG DEEWVEGQHE NSEDYVNIDA
HILCTPVIAD IDKDGVQEMI VAVSYFFDPE YYDNPEHLKE LGGIDIKNYI ASSIVVFNLD
TKQVKWIKEL DLSTDKANFR AYIYSSPTVV DLDGDGYLDI LVGTSFGLFY AMDHRGNIRE
KFPLEMAEIQ GAVVAADIND DGKIELVTTD SHGNIAAWTT QGVEIWEAHL KSLVPQGPSI
GDVDGDGHTE VVVPTSSGNI YVLSGKDGSI VRPYPYRTHG RVMNQLLLVD LNKRGEKKKG
LTIVTTSFDG YLYLIDGPTS CTDVVDIGET SYSMVLADNV DGGDDLDLIV STMNGNVFCF
STPSPHHPLK AWRSSDQGRN NKANRYDREG VFVTHSTRGF RDEEGKNFWA EIEIVDKYRY
PSGSQAPYNV TTTLLVPGNY QGERRITQSQ IYDRPGKYRI KLPTVGVRTT GTVMVEMADK
NGLHFSDEFS LTFHMYYYKL LKWLLVLPML GMFGLLVILR PQEAVPLPSF SRNTDL
