AB11G_ARATH
ID AB11G_ARATH Reviewed; 703 AA.
AC Q8RXN0; Q9LMU4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ABC transporter G family member 11 {ECO:0000303|PubMed:17727615, ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.11 {ECO:0000303|PubMed:17727615, ECO:0000303|PubMed:18299247};
DE Short=AtABCG11 {ECO:0000303|PubMed:17727615, ECO:0000303|PubMed:18299247};
DE AltName: Full=Protein CUTICULAR DEFECT AND ORGAN FUSION 1 {ECO:0000303|PubMed:17971336};
DE AltName: Full=Protein DESPERADO {ECO:0000303|PubMed:17951461};
DE AltName: Full=Protein PERMEABLE LEAVES 1 {ECO:0000303|PubMed:14675439};
DE AltName: Full=White-brown complex homolog protein 11 {ECO:0000303|PubMed:11346655, ECO:0000303|PubMed:17989085};
DE Short=AtWBC11 {ECO:0000303|PubMed:11346655, ECO:0000303|PubMed:17989085};
GN Name=ABCG11 {ECO:0000303|PubMed:17727615, ECO:0000303|PubMed:18299247};
GN Synonyms=COF1 {ECO:0000303|PubMed:17971336},
GN DSO {ECO:0000303|PubMed:17951461}, PEL1 {ECO:0000303|PubMed:14675439},
GN WBC11 {ECO:0000303|PubMed:11346655, ECO:0000303|PubMed:17989085};
GN OrderedLocusNames=At1g17840 {ECO:0000312|Araport:AT1G17840};
GN ORFNames=F2H15.7 {ECO:0000312|EMBL:AAF97264.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14730060; DOI=10.1104/pp.103.027151;
RA Alvarado M.C., Zsigmond L.M., Kovacs I., Cseploe A., Koncz C.,
RA Szabados L.M.;
RT "Gene trapping with firefly luciferase in Arabidopsis. Tagging of stress-
RT responsive genes.";
RL Plant Physiol. 134:18-27(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14675439; DOI=10.1046/j.1365-313x.2003.01946.x;
RA Tanaka T., Tanaka H., Machida C., Watanabe M., Machida Y.;
RT "A new method for rapid visualization of defects in leaf cuticle reveals
RT five intrinsic patterns of surface defects in Arabidopsis.";
RL Plant J. 37:139-146(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17971336; DOI=10.1093/pcp/pcm139;
RA Ukitsu H., Kuromori T., Toyooka K., Goto Y., Matsuoka K., Sakuradani E.,
RA Shimizu S., Kamiya A., Imura Y., Yuguchi M., Wada T., Hirayama T.,
RA Shinozaki K.;
RT "Cytological and biochemical analysis of COF1, an Arabidopsis mutant of an
RT ABC transporter gene.";
RL Plant Cell Physiol. 48:1524-1533(2007).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT AND ABA, REPRESSION BY
RP CYTOKININ, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17989085; DOI=10.1093/pcp/pcm152;
RA Luo B., Xue X.-Y., Hu W.-L., Wang L.-J., Chen X.-Y.;
RT "An ABC transporter gene of Arabidopsis thaliana, AtWBC11, is involved in
RT cuticle development and prevention of organ fusion.";
RL Plant Cell Physiol. 48:1790-1802(2007).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17727615; DOI=10.1111/j.1365-313x.2007.03252.x;
RA Bird D., Beisson F., Brigham A., Shin J., Greer S., Jetter R., Kunst L.,
RA Wu X., Yephremov A., Samuels L.;
RT "Characterization of Arabidopsis ABCG11/WBC11, an ATP binding cassette
RT (ABC) transporter that is required for cuticular lipid secretion.";
RL Plant J. 52:485-498(2007).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT; ABSCISIC ACID AND
RP WOUNDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17951461; DOI=10.1104/pp.107.105676;
RA Panikashvili D., Savaldi-Goldstein S., Mandel T., Yifhar T., Franke R.B.,
RA Hoefer R., Schreiber L., Chory J., Aharoni A.;
RT "The Arabidopsis DESPERADO/AtWBC11 transporter is required for cutin and
RT wax secretion.";
RL Plant Physiol. 145:1345-1360(2007).
RN [11]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=20035035; DOI=10.1093/mp/ssp103;
RA Panikashvili D., Shi J.X., Bocobza S., Franke R.B., Schreiber L.,
RA Aharoni A.;
RT "The Arabidopsis DSO/ABCG11 transporter affects cutin metabolism in
RT reproductive organs and suberin in roots.";
RL Mol. Plant 3:563-575(2010).
RN [14]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH ABCG12, AND
RP SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=20870961; DOI=10.1105/tpc.110.077974;
RA McFarlane H.E., Shin J.J.H., Bird D.A., Samuels A.L.;
RT "Arabidopsis ABCG transporters, which are required for export of diverse
RT cuticular lipids, dimerize in different combinations.";
RL Plant Cell 22:3066-3075(2010).
RN [15]
RP MATERNAL IMPRINTING.
RX PubMed=21838868; DOI=10.1186/1471-2229-11-113;
RA McKeown P.C., Laouielle-Duprat S., Prins P., Wolff P., Schmid M.W.,
RA Donoghue M.T., Fort A., Duszynska D., Comte A., Lao N.T., Wennblom T.J.,
RA Smant G., Koehler C., Grossniklaus U., Spillane C.;
RT "Identification of imprinted genes subject to parent-of-origin specific
RT expression in Arabidopsis thaliana seeds.";
RL BMC Plant Biol. 11:113-113(2011).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBUNIT, AND INTERACTION WITH ABCG9 AND ABCG14.
RC STRAIN=cv. Columbia;
RX PubMed=24112720; DOI=10.1111/tpj.12334;
RA Le Hir R., Sorin C., Chakraborti D., Moritz T., Schaller H., Tellier F.,
RA Robert S., Morin H., Bako L., Bellini C.;
RT "ABCG9, ABCG11 and ABCG14 ABC transporters are required for vascular
RT development in Arabidopsis.";
RL Plant J. 76:811-824(2013).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=27247031; DOI=10.1038/nplants.2015.25;
RA Thieme C.J., Rojas-Triana M., Stecyk E., Schudoma C., Zhang W., Yang L.,
RA Minambres M., Walther D., Schulze W.X., Paz-Ares J., Scheible W.R.,
RA Kragler F.;
RT "Endogenous Arabidopsis messenger RNAs transported to distant tissues.";
RL Nat. Plants 1:15025-15025(2015).
RN [18]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=28921082; DOI=10.1007/s10265-017-0979-4;
RA Takeuchi M., Kegasa T., Watanabe A., Tamura M., Tsutsumi Y.;
RT "Expression analysis of transporter genes for screening candidate
RT monolignol transporters using Arabidopsis thaliana cell suspensions during
RT tracheary element differentiation.";
RL J. Plant Res. 131:297-305(2018).
CC -!- FUNCTION: Required for the cuticle, root suberin and pollen coat
CC development by controlling cutin and maybe wax transport to the
CC extracellular matrix (PubMed:24112720, PubMed:20035035). Involved in
CC developmental plasticity and stress responses. Together with ABCG9 and
CC ABCG14, required for vascular development by regulating lipid/sterol
CC homeostasis (PubMed:24112720). May be a transporter of lignin
CC precursors during tracheary element differentiation (PubMed:28921082).
CC {ECO:0000269|PubMed:14675439, ECO:0000269|PubMed:17727615,
CC ECO:0000269|PubMed:17951461, ECO:0000269|PubMed:17971336,
CC ECO:0000269|PubMed:17989085, ECO:0000269|PubMed:20035035,
CC ECO:0000269|PubMed:24112720, ECO:0000269|PubMed:28921082}.
CC -!- SUBUNIT: Homodimer (PubMed:24112720, PubMed:20870961). Forms
CC heterodimers with ABCG9, ABCG12 and ABCG14 in epidermal cells
CC (PubMed:24112720, PubMed:20870961). {ECO:0000269|PubMed:20870961,
CC ECO:0000269|PubMed:24112720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17727615,
CC ECO:0000269|PubMed:17951461, ECO:0000269|PubMed:17971336,
CC ECO:0000269|PubMed:17989085, ECO:0000269|PubMed:20870961,
CC ECO:0000269|PubMed:24112720}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17727615, ECO:0000269|PubMed:17951461,
CC ECO:0000269|PubMed:17971336, ECO:0000269|PubMed:17989085}.
CC Note=Localized in a polar manner in the epidermis side facing the
CC extracellular matrix (cuticle) and in the endosperm tissue of the
CC developing seed (PubMed:20035035). Trafficking to the plasma membrane
CC is independent of ABCG12 (PubMed:20870961).
CC {ECO:0000269|PubMed:20035035, ECO:0000269|PubMed:20870961}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC flowers, and siliques, mostly in epidermis, trichomes, vasculatures and
CC developing tissues (PubMed:14730060, PubMed:17727615, PubMed:17951461,
CC PubMed:17989085, PubMed:24112720, PubMed:20035035). Follows an
CC uniparental maternal expression in the seed, thus being the product of
CC a maternally expressed imprinted gene (PubMed:21838868). Accumulates in
CC the phloem (PubMed:24112720). Transcripts seem to be transported from
CC shoots to roots (PubMed:27247031). {ECO:0000269|PubMed:14730060,
CC ECO:0000269|PubMed:17727615, ECO:0000269|PubMed:17951461,
CC ECO:0000269|PubMed:17989085, ECO:0000269|PubMed:20035035,
CC ECO:0000269|PubMed:21838868, ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:27247031}.
CC -!- DEVELOPMENTAL STAGE: First observed in seed coat and the endosperm
CC (PubMed:20035035). Displays a polar localization in the embryo
CC protoderm (PubMed:20035035). During embryo development, expressed in
CC the radical tip. In seedlings, localized in the cotyledons, root tip,
CC and young leaves. As secondary root tips emerge, expressed in the
CC pericycle during the initial cell divisions. In leaves, mostly detected
CC in the expanding basal portion, trichomes and stomatal cells. Present
CC in rosette leaves vascular system and epidermis (PubMed:24112720). In
CC roots of mature plants, mainly expressed in lateral root primordia and
CC developing lateral roots (PubMed:24112720). Accumulates in buds and
CC open flowers, mainly in the petal epidermis and the vasculature
CC (PubMed:20035035). In the inflorescence, found in all floral organs,
CC predominantly in the anthers, styles, and young siliques, particularly
CC in young seeds (PubMed:20035035). Upon anthesis and later,
CC progressively restricted to the carpel. Also observed in phloem cells
CC of the flower stem, and in the cortical cells and interfascicular
CC fibers (PubMed:24112720). Accumulates during tracheary element
CC differentiation (PubMed:28921082). {ECO:0000269|PubMed:17727615,
CC ECO:0000269|PubMed:17951461, ECO:0000269|PubMed:20035035,
CC ECO:0000269|PubMed:24112720, ECO:0000269|PubMed:28921082}.
CC -!- INDUCTION: By light, NaCl, abscisic acid (ABA), wounding, and glucose
CC stresses. Repressed by H(2)O(2) and cytokinin.
CC {ECO:0000269|PubMed:14730060, ECO:0000269|PubMed:17951461,
CC ECO:0000269|PubMed:17989085}.
CC -!- DISRUPTION PHENOTYPE: Bushy phenotype (PubMed:24112720). Abnormal
CC cuticle and pollen grain shapes, reduced levels of wax and cutin
CC monomers, unusual lipidic cytoplasmatic inclusions in epidermal cells,
CC inter-organ postgenital fusions, and altered morphology of trichomes
CC and pavement cells (PubMed:24112720, PubMed:20035035). Altered petal
CC and silique morphology, fusion of seeds, and changes in levels of cutin
CC monomers in flowers and siliques associated with the suppression of the
CC expression of a large number of cuticle-associated genes
CC (PubMed:20035035). Altered root suberin composition, as well as root
CC expression of suberin biosynthetic genes (PubMed:20035035). Highly
CC susceptibility to salt and reduced root branching. Excess in sterol
CC (e.g. campesterol) composition (PubMed:24112720). Vascular patterning
CC defects in cotyledons and the floral stem, with a stronger phenotype in
CC plant missing also ABCG9 and ABCG14 (PubMed:24112720). Both single and
CC double mutants abcg11 abcg12 exhibit ABCG12-containing membrane
CC inclusions protruded into the vacuole and contiguous with the
CC endoplasmic reticulum (PubMed:20870961). {ECO:0000269|PubMed:14675439,
CC ECO:0000269|PubMed:17727615, ECO:0000269|PubMed:17951461,
CC ECO:0000269|PubMed:17971336, ECO:0000269|PubMed:17989085,
CC ECO:0000269|PubMed:20035035, ECO:0000269|PubMed:20870961,
CC ECO:0000269|PubMed:24112720}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97264.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC034106; AAF97264.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29642.1; -; Genomic_DNA.
DR EMBL; AY080792; AAL87274.1; -; mRNA.
DR EMBL; AY150457; AAN12898.1; -; mRNA.
DR PIR; E86313; E86313.
DR RefSeq; NP_173226.2; NM_101647.5.
DR AlphaFoldDB; Q8RXN0; -.
DR SMR; Q8RXN0; -.
DR BioGRID; 23602; 18.
DR IntAct; Q8RXN0; 13.
DR STRING; 3702.AT1G17840.1; -.
DR TCDB; 3.A.1.204.8; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q8RXN0; -.
DR PaxDb; Q8RXN0; -.
DR PRIDE; Q8RXN0; -.
DR ProteomicsDB; 244576; -.
DR EnsemblPlants; AT1G17840.1; AT1G17840.1; AT1G17840.
DR GeneID; 838363; -.
DR Gramene; AT1G17840.1; AT1G17840.1; AT1G17840.
DR KEGG; ath:AT1G17840; -.
DR Araport; AT1G17840; -.
DR TAIR; locus:2030898; AT1G17840.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_7_1; -.
DR InParanoid; Q8RXN0; -.
DR OMA; FISGTMC; -.
DR OrthoDB; 806939at2759; -.
DR PhylomeDB; Q8RXN0; -.
DR PRO; PR:Q8RXN0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RXN0; baseline and differential.
DR Genevisible; Q8RXN0; AT.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0080051; P:cutin transport; IMP:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
DR GO; GO:0010222; P:stem vascular tissue pattern formation; IGI:TAIR.
DR GO; GO:0010345; P:suberin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..703
FT /note="ABC transporter G family member 11"
FT /id="PRO_0000240683"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 50..293
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 382..594
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 703 AA; 78413 MW; 8D85EE940AC39003 CRC64;
MEIEASRQQT TVPVSVGGGN FPVGGLSPLS EAIWREKAPT EFVGDVSARL TWQDLTVMVT
MGDGETQNVL EGLTGYAEPG SLTALMGPSG SGKSTMLDAL ASRLAANAFL SGTVLLNGRK
TKLSFGTAAY VTQDDNLIGT LTVRETIWYS ARVRLPDKML RSEKRALVER TIIEMGLQDC
ADTVIGNWHL RGISGGEKRR VSIALEILMR PRLLFLDEPT SGLDSASAFF VTQTLRALSR
DGRTVIASIH QPSSEVFELF DRLYLLSGGK TVYFGQASDA YEFFAQAGFP CPALRNPSDH
FLRCINSDFD KVRATLKGSM KLRFEASDDP LEKITTAEAI RLLVDYYHTS DYYYTAKAKV
EEISQFKGTI LDSGGSQASF LLQTYTLTKR SFINMSRDFG YYWLRLLIYI LVTVCIGTIY
LNVGTSYSAI LARGSCASFV FGFVTFMSIG GFPSFVEDMK VFQRERLNGH YGVAAFVIAN
TLSATPFLIM ITFISGTICY FMVGLHPGFT HYLFFVLCLY ASVTVVESLM MAIASIVPNF
LMGIIIGAGI QGIFMLVSGF FRLPNDIPKP FWRYPMSYIS FHFWALQGQY QNDLRGLTFD
SQGSAFKIPG EYVLENVFQI DLHRSKWINL SVILSMIIIY RIIFFIMIKT NEDVTPWVRG
YIARRRMKQK NGTQNTTVAP DGLTQSPSLR NYIATRTDGA RRW
