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AB4B_ARATH
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   03-AUG-2022, entry version 158.
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}.
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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.AT2G47000.1; -.
DR   TCDB; 3.A.1.201.7; the atp-binding cassette (abc) superfamily.
DR   iPTMnet; O80725; -.
DR   SwissPalm; O80725; -.
DR   PaxDb; O80725; -.
DR   PRIDE; O80725; -.
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; locus:2041434; AT2G47000.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   InParanoid; O80725; -.
DR   OMA; FRLIGIR; -.
DR   OrthoDB; 186078at2759; -.
DR   PhylomeDB; O80725; -.
DR   BioCyc; ARA:AT2G47000-MON; -.
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:0016021; C:integral component of membrane; IBA:GO_Central.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
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   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 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
 
 
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