AB9G_ARATH
ID AB9G_ARATH Reviewed; 638 AA.
AC Q9SZR9; F4JIV3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ABC transporter G family member 9 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.9 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG9 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Probable white-brown complex homolog protein 9 {ECO:0000303|PubMed:11346655};
DE Short=AtWBC9 {ECO:0000303|PubMed:11346655};
GN Name=ABCG9 {ECO:0000303|PubMed:18299247};
GN Synonyms=WBC9 {ECO:0000303|PubMed:11346655};
GN OrderedLocusNames=At4g27420 {ECO:0000312|Araport:AT4G27420};
GN ORFNames=F27G19.20 {ECO:0000312|EMBL:CAB43874.1};
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=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 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 SUBUNIT, INTERACTION WITH ABCG11, AND SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24474628; DOI=10.1105/tpc.113.118935;
RA Choi H., Ohyama K., Kim Y.-Y., Jin J.-Y., Lee S.B., Yamaoka Y.,
RA Muranaka T., Suh M.C., Fujioka S., Lee Y.;
RT "The role of Arabidopsis ABCG9 and ABCG31 ATP binding cassette transporters
RT in pollen fitness and the deposition of steryl glycosides on the pollen
RT coat.";
RL Plant Cell 26:310-324(2014).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27634427; DOI=10.1104/pp.16.00967;
RA Zhao B., Shi H., Wang W., Liu X., Gao H., Wang X., Zhang Y., Yang M.,
RA Li R., Guo Y.;
RT "Secretory COPII protein SEC31B is required for pollen wall development.";
RL Plant Physiol. 172:1625-1642(2016).
CC -!- FUNCTION: Together with ABCG31, involved in pollen coat deposition of
CC steryl glycosides required for pollen fitness (PubMed:24474628).
CC Together with ABCG11 and ABCG14, required for vascular development by
CC regulating lipid/sterol homeostasis (PubMed:24112720).
CC {ECO:0000269|PubMed:24112720, ECO:0000269|PubMed:24474628}.
CC -!- SUBUNIT: Homodimer (PubMed:24112720). Forms heterodimers with ABCG11
CC (PubMed:24112720). {ECO:0000269|PubMed:24112720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24474628, ECO:0000269|PubMed:27634427}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Present in flowers and siliques, at lower levels in
CC leaves and stems, but barely in roots (PubMed:24474628,
CC PubMed:24112720). Accumulates in the phloem (PubMed:24112720). Highly
CC expressed in the tapetum of anthers (PubMed:24474628, PubMed:27634427).
CC {ECO:0000269|PubMed:24112720, ECO:0000269|PubMed:24474628,
CC ECO:0000269|PubMed:27634427}.
CC -!- DEVELOPMENTAL STAGE: In roots, observed in the central cylinder
CC (PubMed:24112720). Restricted to the petiole main vein
CC (PubMed:24112720). Present in rosette leaves vascular system
CC (PubMed:24112720). Expressed transiently during flower develoment in
CC the anthers and developing siliques, mostly in the tapetal cell layer
CC during pollen maturation (PubMed:24474628). Also observed in phloem
CC cells of the flower stem (PubMed:24112720).
CC {ECO:0000269|PubMed:24112720, ECO:0000269|PubMed:24474628}.
CC -!- DISRUPTION PHENOTYPE: Pollen grains of the double mutant abcg9 abcg31
CC shrivel up and collapse upon exposure to dry air, and exhibit an
CC immature coat containing reduced levels of steryl glycosides, thus
CC leading to a low viability (PubMed:24474628). Defective in sterol (e.g.
CC 24-methylene cholesterol) composition (PubMed:24112720). Vascular
CC patterning defects in cotyledons and the floral stem, with a stronger
CC phenotype in plant missing also ABCG11 and ABCG14 (PubMed:24112720).
CC {ECO:0000269|PubMed:24112720, ECO:0000269|PubMed:24474628}.
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=CAB43874.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81392.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL078467; CAB43874.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81392.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85338.1; -; Genomic_DNA.
DR PIR; T08934; T08934.
DR RefSeq; NP_194472.3; NM_118876.4.
DR AlphaFoldDB; Q9SZR9; -.
DR SMR; Q9SZR9; -.
DR BioGRID; 14137; 7.
DR IntAct; Q9SZR9; 5.
DR STRING; 3702.AT4G27420.1; -.
DR PaxDb; Q9SZR9; -.
DR PRIDE; Q9SZR9; -.
DR ProteomicsDB; 244498; -.
DR EnsemblPlants; AT4G27420.1; AT4G27420.1; AT4G27420.
DR GeneID; 828850; -.
DR Gramene; AT4G27420.1; AT4G27420.1; AT4G27420.
DR KEGG; ath:AT4G27420; -.
DR Araport; AT4G27420; -.
DR TAIR; locus:2124029; AT4G27420.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_10_1; -.
DR InParanoid; Q9SZR9; -.
DR OMA; ECVNGDY; -.
DR OrthoDB; 1022017at2759; -.
DR PRO; PR:Q9SZR9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZR9; baseline and differential.
DR Genevisible; Q9SZR9; AT.
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:0070505; C:pollen coat; IMP: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; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:1901656; P:glycoside transport; IMP:UniProtKB.
DR GO; GO:0010208; P:pollen wall assembly; IMP:UniProtKB.
DR GO; GO:0010222; P:stem vascular tissue pattern formation; IGI:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..638
FT /note="ABC transporter G family member 9"
FT /id="PRO_0000240681"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 37..292
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 369..575
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT BINDING 84..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 638 AA; 70753 MW; 9ADE750F1A5E517B CRC64;
MDNQEVSMDV ETPIAKTNDD RSLPFSIFKK ANNPVTLKFE NLVYTVKLKD SQGCFGKNDK
TEERTILKGL TGIVKPGEIL AMLGPSGSGK TSLLTALGGR VGEGKGKLTG NISYNNKPLS
KAVKRTTGFV TQDDALYPNL TVTETLVFTA LLRLPNSFKK QEKIKQAKAV MTELGLDRCK
DTIIGGPFLR GVSGGERKRV SIGQEILINP SLLFLDEPTS GLDSTTAQRI VSILWELARG
GRTVVTTIHQ PSSRLFYMFD KLLLLSEGNP VYFGLGSNAM DYFASVGYSP LVERINPSDF
LLDIANGVGS DESQRPEAMK AALVAFYKTN LLDSVINEVK GQDDLCNKPR ESSRVATNTY
GDWPTTWWQQ FCVLLKRGLK QRRHDSFSGM KVAQIFIVSF LCGLLWWQTK ISRLQDQIGL
LFFISSFWAF FPLFQQIFTF PQERAMLQKE RSSGMYRLSP YFLSRVVGDL PMELILPTCF
LVITYWMAGL NHNLANFFVT LLVLLVHVLV SGGLGLALGA LVMDQKSATT LGSVIMLTFL
LAGGYYVQHV PVFISWIKYV SIGYYTYKLL ILGQYTANEL YPCGDNGKLR CHVGDFEGIK
HIGFNSGLVS ALALTAMLVV YRVIAYIALT RIGKTKSG
