AB14G_ARATH
ID AB14G_ARATH Reviewed; 648 AA.
AC Q9C6W5; Q9C6R7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ABC transporter G family member 14 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.14 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG14 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Protein INSENSITIVE TO TEMPERATURE 211 {ECO:0000303|PubMed:28398838};
DE AltName: Full=White-brown complex homolog protein 14 {ECO:0000303|PubMed:11346655};
DE Short=AtWBC14 {ECO:0000303|PubMed:11346655};
GN Name=ABCG14 {ECO:0000303|PubMed:18299247};
GN Synonyms=INT211 {ECO:0000303|PubMed:28398838},
GN WBC14 {ECO:0000303|PubMed:11346655};
GN OrderedLocusNames=At1g31770 {ECO:0000312|Araport:AT1G31770};
GN ORFNames=F27M3.2 {ECO:0000312|EMBL:AAG60152.1},
GN F5M6.22 {ECO:0000312|EMBL:AAG50724.1};
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ABCG11.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24513716; DOI=10.1038/ncomms4274;
RA Zhang K., Novak O., Wei Z., Gou M., Zhang X., Yu Y., Yang H., Cai Y.,
RA Strnad M., Liu C.-J.;
RT "Arabidopsis ABCG14 protein controls the acropetal translocation of root-
RT synthesized cytokinins.";
RL Nat. Commun. 5:3274-3274(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24778257; DOI=10.1073/pnas.1321519111;
RA Ko D., Kang J., Kiba T., Park J., Kojima M., Do J., Kim K.Y., Kwon M.,
RA Endler A., Song W.-Y., Martinoia E., Sakakibara H., Lee Y.;
RT "Arabidopsis ABCG14 is essential for the root-to-shoot translocation of
RT cytokinin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7150-7155(2014).
RN [10]
RP REVIEW ON PHYTOHORMONE TRANSPORT.
RX PubMed=26517905; DOI=10.1042/bst20150106;
RA Borghi L., Kang J., Ko D., Lee Y., Martinoia E.;
RT "The role of ABCG-type ABC transporters in phytohormone transport.";
RL Biochem. Soc. Trans. 43:924-930(2015).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REPRESSION BY HYDROGEN PEROXIDE.
RC STRAIN=cv. Col-4;
RX PubMed=27550996; DOI=10.1104/pp.16.00415;
RA Zwack P.J., De Clercq I., Howton T.C., Hallmark H.T., Hurny A.,
RA Keshishian E.A., Parish A.M., Benkova E., Mukhtar M.S., Van Breusegem F.,
RA Rashotte A.M.;
RT "Cytokinin response factor 6 represses cytokinin-associated genes during
RT oxidative stress.";
RL Plant Physiol. 172:1249-1258(2016).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28398838; DOI=10.1094/mpmi-01-17-0011-r;
RA Wang S., Wang S., Sun Q., Yang L., Zhu Y., Yuan Y., Hua J.;
RT "A role of cytokinin transporter in Arabidopsis immunity.";
RL Mol. Plant Microbe Interact. 30:325-333(2017).
CC -!- FUNCTION: Positive regulator of plant growth which acts as an efflux
CC pump involved in the major root-to-shoot (acropetal) long-distance
CC cytokinin (CK) transport via the xylem sap (PubMed:24513716,
CC PubMed:24778257, PubMed:26517905, PubMed:28398838). Together with ABCG9
CC and ABCG11, required for vascular development by regulating
CC lipid/sterol homeostasis (PubMed:24112720). Involved in CK-dependent
CC responses to oxidative stress such as hydrogen peroxide H(2)O(2)
CC (PubMed:27550996). {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24513716, ECO:0000269|PubMed:24778257,
CC ECO:0000269|PubMed:27550996, ECO:0000269|PubMed:28398838,
CC ECO:0000303|PubMed:26517905}.
CC -!- FUNCTION: (Microbial infection) Required for SNC1-mediated defense
CC response against the virulent pathogen Pseudomonas syringae pv. tomato
CC DC3000 by promoting the accumulation of trans-zeatin (tZ)-type
CC cytokinins (CK) in the shoot. {ECO:0000269|PubMed:28398838}.
CC -!- SUBUNIT: Forms heterodimers with ABCG11. {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24513716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24778257}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Accumulates primarily in the pericycle and stelar
CC cells of roots (PubMed:24513716, PubMed:24778257). Expressed in leaves,
CC stems, flowers and siliques, and, at low levels, in roots
CC (PubMed:24112720, PubMed:24513716, PubMed:24778257). Accumulates in the
CC phloem (PubMed:24112720). {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24513716, ECO:0000269|PubMed:24778257}.
CC -!- DEVELOPMENTAL STAGE: In roots, observed in the central cylinder
CC (vascular tissues), but absent from division zones (PubMed:24112720,
CC PubMed:24513716, PubMed:24778257). Present in the vascular system of
CC the cotyledons and rosette leaves (PubMed:24112720, PubMed:24513716).
CC Also observed in phloem cells of the flower stem (PubMed:24112720).
CC Accumulates also in the mature anthers of open flowers and in siliques
CC (PubMed:24513716). {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24513716, ECO:0000269|PubMed:24778257}.
CC -!- INDUCTION: Repressed by hydrogen peroxide H(2)O(2) in a CRF6-dependent
CC manner. {ECO:0000269|PubMed:27550996}.
CC -!- DISRUPTION PHENOTYPE: Weak growth, small inflorescences and rosettes,
CC slender stems, and short and retarded primary root growth leading to
CC dwarf plants (PubMed:24513716, PubMed:24778257, PubMed:28398838).
CC Impaired translocation of trans-zeatin (tZ)-type cytokinins (CK) from
CC roots to shoots (acropetal), thereby affecting the plant growth and
CC development and leading to a reduced cytokinin content in xylem sap
CC (PubMed:24513716, PubMed:24778257). Defective in sterol (e.g. 24-
CC methylene cholesterol and sitosterol) composition (PubMed:24112720).
CC Vascular patterning defects in cotyledons and the floral stem, with a
CC stronger phenotype in plant missing also ABCG9 and ABCG11
CC (PubMed:24112720). Altered responses to oxidative stress (e.g. hydrogen
CC peroxide H(2)O(2)) (PubMed:27550996). Suppression of the SNC1-mediated
CC defense response due to a deficiency of tZ-type CK in the shoot
CC (PubMed:28398838). {ECO:0000269|PubMed:24112720,
CC ECO:0000269|PubMed:24513716, ECO:0000269|PubMed:24778257,
CC ECO:0000269|PubMed:27550996, ECO:0000269|PubMed:28398838}.
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=AAG50724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC074360; AAG60152.1; -; Genomic_DNA.
DR EMBL; AC079041; AAG50724.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31390.1; -; Genomic_DNA.
DR EMBL; AK117530; BAC42192.1; -; mRNA.
DR EMBL; AY088793; AAM67104.1; -; mRNA.
DR PIR; C86441; C86441.
DR RefSeq; NP_564383.1; NM_102911.3.
DR AlphaFoldDB; Q9C6W5; -.
DR SMR; Q9C6W5; -.
DR BioGRID; 25298; 1.
DR STRING; 3702.AT1G31770.1; -.
DR TCDB; 3.A.1.204.29; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q9C6W5; -.
DR PRIDE; Q9C6W5; -.
DR ProteomicsDB; 244559; -.
DR EnsemblPlants; AT1G31770.1; AT1G31770.1; AT1G31770.
DR GeneID; 840064; -.
DR Gramene; AT1G31770.1; AT1G31770.1; AT1G31770.
DR KEGG; ath:AT1G31770; -.
DR Araport; AT1G31770; -.
DR TAIR; locus:2028656; AT1G31770.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_10_1; -.
DR InParanoid; Q9C6W5; -.
DR OMA; WCARMSS; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q9C6W5; -.
DR PRO; PR:Q9C6W5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6W5; baseline and differential.
DR Genevisible; Q9C6W5; 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: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; IDA:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0010184; P:cytokinin transport; IMP:UniProtKB.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0140115; P:export across plasma membrane; IDA:UniProtKB.
DR GO; GO:0140352; P:export from cell; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; 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; Cytokinin signaling pathway;
KW Developmental protein; Glycoprotein; Membrane; Nucleotide-binding;
KW Plant defense; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..648
FT /note="ABC transporter G family member 14"
FT /id="PRO_0000240686"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..304
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 384..590
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 648 AA; 72619 MW; D52A2D2434A5BB9D CRC64;
MPQNCIAPRP EEDGGVMVQG LPDMSDTQSK SVLAFPTITS QPGLQMSMYP ITLKFEEVVY
KVKIEQTSQC MGSWKSKEKT ILNGITGMVC PGEFLAMLGP SGSGKTTLLS ALGGRLSKTF
SGKVMYNGQP FSGCIKRRTG FVAQDDVLYP HLTVWETLFF TALLRLPSSL TRDEKAEHVD
RVIAELGLNR CTNSMIGGPL FRGISGGEKK RVSIGQEMLI NPSLLLLDEP TSGLDSTTAH
RIVTTIKRLA SGGRTVVTTI HQPSSRIYHM FDKVVLLSEG SPIYYGAASS AVEYFSSLGF
STSLTVNPAD LLLDLANGIP PDTQKETSEQ EQKTVKETLV SAYEKNISTK LKAELCNAES
HSYEYTKAAA KNLKSEQWCT TWWYQFTVLL QRGVRERRFE SFNKLRIFQV ISVAFLGGLL
WWHTPKSHIQ DRTALLFFFS VFWGFYPLYN AVFTFPQEKR MLIKERSSGM YRLSSYFMAR
NVGDLPLELA LPTAFVFIIY WMGGLKPDPT TFILSLLVVL YSVLVAQGLG LAFGALLMNI
KQATTLASVT TLVFLIAGGY YVQQIPPFIV WLKYLSYSYY CYKLLLGIQY TDDDYYECSK
GVWCRVGDFP AIKSMGLNNL WIDVFVMGVM LVGYRLMAYM ALHRVKLR
