ID AB4B_ARATH Reviewed; 1286 AA.
AC O80725;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=ABC transporter B family member 4;
DE Short=ABC transporter ABCB.4;
DE Short=AtABCB4;
DE AltName: Full=Multidrug resistance protein 4;
DE AltName: Full=P-glycoprotein 4;
GN Name=ABCB4; Synonyms=MDR4, PGP4; OrderedLocusNames=At2g47000;
GN ORFNames=F14M4.17;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 PROTEIN SEQUENCE OF 25-31; 317-333 AND 1202-1218, FUNCTION, INDUCTION,
RP INTERACTION WITH NPA, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16243904; DOI=10.1105/tpc.105.035816;
RA Terasaka K., Blakeslee J.J., Titapiwatanakun B., Peer W.A.,
RA Bandyopadhyay A., Makam S.N., Lee O.R., Richards E.L., Murphy A.S.,
RA Sato F., Yazaki K.;
RT "PGP4, an ATP binding cassette P-glycoprotein, catalyzes auxin transport in
RT Arabidopsis thaliana roots.";
RL Plant Cell 17:2922-2939(2005).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16198350; DOI=10.1016/j.febslet.2005.08.061;
RA Santelia D., Vincenzetti V., Azzarello E., Bovet L., Fukao Y., Duechtig P.,
RA Mancuso S., Martinoia E., Geisler M.;
RT "MDR-like ABC transporter AtPGP4 is involved in auxin-mediated lateral root
RT and root hair development.";
RL FEBS Lett. 579:5399-5406(2005).
RN [7]
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).
CC -!- FUNCTION: Auxin influx transporter that mediates the transport of auxin
CC in roots. Contributes to the basipetal transport in hypocotyls and root
CC tips by establishing an auxin uptake sink in the root cap. Confers
CC sensitivity to 1-N-naphthylphthalamic acid (NPA). Regulates the root
CC elongation, the initiation of lateral roots and the development of root
CC hairs. Can transport IAA, indole-3-propionic acid, NPA syringic acid,
CC vanillic acid and some auxin metabolites, but not 2,4-D and 1-
CC naphthaleneacetic acid. {ECO:0000269|PubMed:16198350,
CC ECO:0000269|PubMed:16243904}.
CC -!- SUBUNIT: Interacts with 1-naphthylphthalamic acid (NPA).
CC {ECO:0000269|PubMed:16243904}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16243904};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:16243904}. Note=Non-polar distribution in apical
CC cells. Apical (bottom) localization in mature root cells. Basal (top)
CC localization in the root elongation zone.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, especially in the root
CC elongation zone and lateral roots. In mature portion of the root,
CC expressed in the epidermis and cortex. In the root elongation zone,
CC confined to epidermis. In root tips, present in the root cap, S3
CC columella and epidermal cells. {ECO:0000269|PubMed:16198350,
CC ECO:0000269|PubMed:16243904}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at early stages of root
CC development. {ECO:0000269|PubMed:16198350}.
CC -!- INDUCTION: By auxin, and cytokinins such as kinetin. Repressed by
CC abscisic acid and cold treatment. {ECO:0000269|PubMed:16243904}.
CC -!- PTM: Phosphorylation level varies significantly during early response
CC to bacterial elicitor.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004411; AAC34225.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10785.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61709.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61712.1; -; Genomic_DNA.
DR PIR; T02187; T02187.
DR RefSeq; NP_001323911.1; NM_001337237.1.
DR RefSeq; NP_001323914.1; NM_001337236.1.
DR RefSeq; NP_182223.1; NM_130268.4.
DR AlphaFoldDB; O80725; -.
DR SMR; O80725; -.
DR BioGRID; 4649; 20.
DR STRING; 3702.O80725; -.
DR TCDB; 3.A.1.201.7; the atp-binding cassette (abc) superfamily.
DR GlyCosmos; O80725; 9 sites, No reported glycans.
DR iPTMnet; O80725; -.
DR SwissPalm; O80725; -.
DR PaxDb; 3702-AT2G47000-1; -.
DR ProteomicsDB; 244639; -.
DR EnsemblPlants; AT2G47000.1; AT2G47000.1; AT2G47000.
DR EnsemblPlants; AT2G47000.5; AT2G47000.5; AT2G47000.
DR EnsemblPlants; AT2G47000.6; AT2G47000.6; AT2G47000.
DR GeneID; 819314; -.
DR Gramene; AT2G47000.1; AT2G47000.1; AT2G47000.
DR Gramene; AT2G47000.5; AT2G47000.5; AT2G47000.
DR Gramene; AT2G47000.6; AT2G47000.6; AT2G47000.
DR KEGG; ath:AT2G47000; -.
DR Araport; AT2G47000; -.
DR TAIR; AT2G47000; ABCB4.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; O80725; -.
DR OMA; NYEYVLP; -.
DR OrthoDB; 5487044at2759; -.
DR PhylomeDB; O80725; -.
DR BioCyc; ARA:AT2G47000-MONOMER; -.
DR PRO; PR:O80725; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80725; baseline and differential.
DR Genevisible; O80725; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010328; F:auxin influx transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IDA:TAIR.
DR GO; GO:0060919; P:auxin import into cell; IDA:TAIR.
DR GO; GO:0009926; P:auxin polar transport; TAS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010540; P:basipetal auxin transport; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF11; ALPHA-FACTOR-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Auxin signaling pathway; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1286
FT /note="ABC transporter B family member 4"
FT /id="PRO_0000227915"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 764..784
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 871..891
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 63..349
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 384..620
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 720..1007
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1042..1279
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1077..1084
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15308754"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1286 AA; 139028 MW; 97D2A8AFEBA698E6 CRC64;
MASESGLNGD PNILEEVSET KRDKEEEEEV KKTEKKDEEH EKTKTVPFYK LFAFADSFDF
LLMILGTLGS IGNGLGFPLM TLLFGDLIDA FGENQTNTTD KVSKVALKFV WLGIGTFAAA
FLQLSGWMIS GERQAARIRS LYLKTILRQD IAFFDIDTNT GEVVGRMSGD TVLIQDAMGE
KVGKAIQLLA TFVGGFVIAF VRGWLLTLVM LSSIPLLVMA GALLAIVIAK TASRGQTAYA
KAATVVEQTI GSIRTVASFT GEKQAISNYN KHLVTAYKAG VIEGGSTGLG LGTLFLVVFC
SYALAVWYGG KLILDKGYTG GQVLNIIIAV LTGSMSLGQT SPCLSAFAAG QAAAYKMFET
IERRPNIDSY STNGKVLDDI KGDIELKDVY FTYPARPDEQ IFRGFSLFIS SGTTVALVGQ
SGSGKSTVVS LIERFYDPQA GDVLIDGINL KEFQLKWIRS KIGLVSQEPV LFTASIKDNI
AYGKEDATTE EIKAAAELAN ASKFVDKLPQ GLDTMVGEHG TQLSGGQKQR IAVARAILKD
PRILLLDEAT SALDAESERV VQEALDRIMV NRTTVVVAHR LSTVRNADMI AVIHQGKIVE
KGSHTELLKD PEGAYSQLIR LQEEKKSDEN AAEEQKMSSI ESFKQSSLRK SSLGRSLSKG
GSSRGNSSRH SFNMFGFPAG IDGNVVQDQE EDDTTQPKTE PKKVSIFRIA ALNKPEIPVL
ILGSISAAAN GVILPIFGIL ISSVIKAFFQ PPKKLKEDTS FWAIIFMVLG FASIIAYPAQ
TFFFAIAGCK LVQRIRSMCF EKVVHMEVGW FDEPENSSGT IGARLSADAA TIRGLVGDSL
AQTVQNLSSI LAGLIIAFLA CWQLAFVVLA MLPLIALNGF LYMKFMKGFS ADAKKMYGEA
SQVANDAVGS IRTVASFCAE DKVMNMYSKK CEGPMKNGIR QGIVSGIGFG FSFFVLFSSY
AASFYVGARL VDDGKTTFDS VFRVFFALTM AAMAISQSSS LSPDSSKADV AAASIFAIMD
RESKIDPSVE SGRVLDNVKG DIELRHVSFK YPARPDVQIF QDLCLSIRAG KTVALVGESG
SGKSTVIALL QRFYDPDSGE ITLDGVEIKS LRLKWLRQQT GLVSQEPILF NETIRANIAY
GKGGDASESE IVSSAELSNA HGFISGLQQG YDTMVGERGI QLSGGQKQRV AIARAIVKDP
KVLLLDEATS ALDAESERVV QDALDRVMVN RTTIVVAHRL STIKNADVIA VVKNGVIVEK
GKHDTLINIK DGVYASLVQL HLTAAS
//
