AB26G_ARATH
ID AB26G_ARATH Reviewed; 685 AA.
AC Q9LK50; F4JC75;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ABC transporter G family member 26 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.26 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG26 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Putative white-brown complex homolog protein 27 {ECO:0000303|PubMed:11346655};
DE Short=AtWBC27 {ECO:0000303|PubMed:11346655};
GN Name=ABCG26 {ECO:0000303|PubMed:18299247};
GN Synonyms=WBC27 {ECO:0000303|PubMed:11346655};
GN OrderedLocusNames=At3g13220 {ECO:0000312|Araport:AT3G13220};
GN ORFNames=MJG19.19 {ECO:0000312|EMBL:BAB01414.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=20732973; DOI=10.1104/pp.110.161968;
RA Quilichini T.D., Friedmann M.C., Samuels A.L., Douglas C.J.;
RT "ATP-binding cassette transporter G26 is required for male fertility and
RT pollen exine formation in Arabidopsis.";
RL Plant Physiol. 154:678-690(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21205178; DOI=10.1111/j.1744-7909.2010.01010.x;
RA Dou X.-Y., Yang K.-Z., Zhang Y., Wang W., Liu X.-L., Chen L.-Q.,
RA Zhang X.-Q., Ye D.;
RT "WBC27, an adenosine tri-phosphate-binding cassette protein, controls
RT pollen wall formation and patterning in Arabidopsis.";
RL J. Integr. Plant Biol. 53:74-88(2011).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21696844; DOI=10.1016/j.jplph.2011.05.014;
RA Kuromori T., Ito T., Sugimoto E., Shinozaki K.;
RT "Arabidopsis mutant of AtABCG26, an ABC transporter gene, is defective in
RT pollen maturation.";
RL J. Plant Physiol. 168:2001-2005(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21223384; DOI=10.1111/j.1365-313x.2010.04412.x;
RA Choi H., Jin J.-Y., Choi S., Hwang J.-U., Kim Y.-Y., Suh M.C., Lee Y.;
RT "An ABCG/WBC-type ABC transporter is essential for transport of
RT sporopollenin precursors for exine formation in developing pollen.";
RL Plant J. 65:181-193(2011).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25415974; DOI=10.1105/tpc.114.130484;
RA Quilichini T.D., Samuels A.L., Douglas C.J.;
RT "ABCG26-mediated polyketide trafficking and hydroxycinnamoyl spermidines
RT contribute to pollen wall exine formation in Arabidopsis.";
RL Plant Cell 26:4483-4498(2014).
CC -!- FUNCTION: Mediates the transport of sporopollenin precursors (e.g.
CC polyketides) across the tapetum plasma membrane into the anther locule
CC for polymerization on developing microspore walls, thus being required
CC for male fertility and pollen exine formation and patterning prior to
CC tapetum programmed cell death. {ECO:0000269|PubMed:20732973,
CC ECO:0000269|PubMed:21205178, ECO:0000269|PubMed:21223384,
CC ECO:0000269|PubMed:21696844, ECO:0000269|PubMed:25415974}.
CC -!- SUBUNIT: Homo- or heterodimer. {ECO:0000305|PubMed:21223384}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20732973,
CC ECO:0000269|PubMed:21205178, ECO:0000269|PubMed:21223384}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20732973}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, especially in tapetum
CC within anthers. {ECO:0000269|PubMed:20732973,
CC ECO:0000269|PubMed:21205178, ECO:0000269|PubMed:21223384}.
CC -!- DEVELOPMENTAL STAGE: In developing anthers, transiently localized to
CC tapetum cells during early pollen wall formation, sporopollenin
CC biosynthesis and sporopollenin deposition.
CC {ECO:0000269|PubMed:20732973, ECO:0000269|PubMed:21205178,
CC ECO:0000269|PubMed:21223384}.
CC -!- DISRUPTION PHENOTYPE: Drastic decrease in seed production
CC (PubMed:21223384, PubMed:20732973, PubMed:21205178, PubMed:21696844).
CC Severely reduced fertility, with most siliques failing to produce seeds
CC by self-fertilization and mature anthers failing to release pollen
CC grains characterized by the absence of an exine wall on microspores,
CC due to an impaired sporopollenin deposition (PubMed:20732973,
CC PubMed:21205178, PubMed:21696844, PubMed:21223384, PubMed:25415974).
CC Aberrant structures in tapetal cells such as accumulation of numerous
CC vesicles and granules probably containing polyketides precursors in
CC tapetal cells (PubMed:21223384, PubMed:25415974). Abnormal pollen
CC grains germinating in the anther before anthesis (PubMed:21205178).
CC {ECO:0000269|PubMed:20732973, ECO:0000269|PubMed:21205178,
CC ECO:0000269|PubMed:21223384, ECO:0000269|PubMed:21696844,
CC ECO:0000269|PubMed:25415974}.
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=BAB01414.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000375; BAB01414.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75312.1; -; Genomic_DNA.
DR RefSeq; NP_187928.2; NM_112162.3.
DR AlphaFoldDB; Q9LK50; -.
DR SMR; Q9LK50; -.
DR BioGRID; 5846; 6.
DR IntAct; Q9LK50; 3.
DR STRING; 3702.AT3G13220.1; -.
DR PaxDb; Q9LK50; -.
DR PRIDE; Q9LK50; -.
DR EnsemblPlants; AT3G13220.1; AT3G13220.1; AT3G13220.
DR GeneID; 820512; -.
DR Gramene; AT3G13220.1; AT3G13220.1; AT3G13220.
DR KEGG; ath:AT3G13220; -.
DR Araport; AT3G13220; -.
DR TAIR; locus:2090009; AT3G13220.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_10_1; -.
DR InParanoid; Q9LK50; -.
DR OMA; WWKSKTG; -.
DR OrthoDB; 1022017at2759; -.
DR PRO; PR:Q9LK50; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK50; baseline and differential.
DR Genevisible; Q9LK50; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0010584; P:pollen exine formation; IMP:UniProtKB.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0030638; P:polyketide metabolic process; IMP:UniProtKB.
DR GO; GO:0080110; P:sporopollenin 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; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..685
FT /note="ABC transporter G family member 26"
FT /id="PRO_0000240698"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 65..329
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 414..623
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 685 AA; 77887 MW; 3DBF1BCC87F343EA CRC64;
MEIRRSTEEV EENHVMQITG SNGIVHNMEF MPQAYLRNQY SSEIDIDEEF VSTYPLEDAP
LPIFLKFEDV EYKVRNSHAS SANLVKTMVS KVVTHTNPDP DGYKHILKGI TGSTGPGEIL
ALMGPSGSGK TTLLKIMGGR LTDNVKGKLT YNDIPYSPSV KRRIGFVTQD DVLLPQLTVE
ETLAFAAFLR LPSSMSKEQK YAKIEMIIKE LGLERCRRTR VGGGFVKGIS GGERKRASIA
YEILVDPSLL LLDEPTSGLD STSATKLLHI LQGVAKAGRT VITTIHQPSS RMFHMFDKLL
LISEGHPAFY GKARESMEYF SSLRILPEIA MNPAEFLLDL ATGQVSDISL PDELLAAKTA
QPDSEEVLLK YLKQRYKTDL EPKEKEENHR NRKAPEHLQI AIQVKKDWTL SWWDQFLILS
RRTFRERRRD YFDKLRLVQS LGVAVVLGLL WWKSKTDTEA HLRDQVGLMF YICIFWTSSS
LFGAVYVFPF EKIYLVKERK AEMYRLSVYY VCSTLCDMVA HVLYPTFFMI IVYFMAEFNR
NIPCFLFTVL TILLIAITSQ GAGEFLGASV LSIKRAGMIA SLVLMLFLLT GGYYVQHIPK
FMQWLKYLSF MHYGFRLLLK VQYSADQLFE CGSKGGCRTL QSSSSFDTIN LNGGLQELWV
LLAMAFGYRL CAYFCLRKKI SICHL
