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AB4C_ARATH
ID   AB4C_ARATH              Reviewed;        1516 AA.
AC   Q7DM58; O24525; Q0WVT4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=ABC transporter C family member 4;
DE            Short=ABC transporter ABCC.4;
DE            Short=AtABCC4;
DE            EC=7.6.2.2;
DE   AltName: Full=ATP-energized glutathione S-conjugate pump 4;
DE   AltName: Full=Glutathione S-conjugate-transporting ATPase 4;
DE   AltName: Full=Multidrug resistance-associated protein 4;
GN   Name=ABCC4; Synonyms=EST3, MRP4; OrderedLocusNames=At2g47800;
GN   ORFNames=F17A22.19;
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 [GENOMIC DNA], AND INDUCTION.
RX   PubMed=9671034; DOI=10.1007/s004380050779;
RA   Sanchez-Fernandez R., Ardiles-Diaz W., Van Montagu M., Inze D., May M.J.;
RT   "Cloning and expression analyses of the AtMRP4, a novel MRP-like gene from
RT   Arabidopsis thaliana.";
RL   Mol. Gen. Genet. 258:655-662(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Sanchez-Fernandez R., Rea P.A.;
RT   "AtMRP4 gene of Arabidopsis encodes a glutathione S-conjugate pump.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1272-1516, AND INDUCTION.
RX   PubMed=9271206; DOI=10.1016/s0014-5793(97)00702-3;
RA   Tommasini R., Vogt E., Schmid J., Fromentau M., Amrhein N., Martinoia E.;
RT   "Differential expression of genes coding for ABC transporters after
RT   treatment of Arabidopsis thaliana with xenobiotics.";
RL   FEBS Lett. 411:206-210(1997).
RN   [7]
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   [8]
RP   GENE FAMILY.
RX   PubMed=11855639; DOI=10.1007/s004250100661;
RA   Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA   Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT   "Multifunctionality of plant ABC transporters -- more than just
RT   detoxifiers.";
RL   Planta 214:345-355(2002).
RN   [9]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
RA   Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D.,
RA   Martinoia E., Schulz B.;
RT   "Family business: the multidrug-resistance related protein (MRP) ABC
RT   transporter genes in Arabidopsis thaliana.";
RL   Planta 216:107-119(2002).
RN   [10]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, FUNCTION,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=15225287; DOI=10.1111/j.1365-313x.2004.02125.x;
RA   Klein M., Geisler M., Suh S.J., Kolukisaoglu U.H., Azevedo L., Plaza S.,
RA   Curtis M.D., Richter A., Weder B., Schulz B., Martinoia E.;
RT   "Disruption of AtMRP4, a guard cell plasma membrane ABCC-type ABC
RT   transporter, leads to deregulation of stomatal opening and increased
RT   drought susceptibility.";
RL   Plant J. 39:219-236(2004).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA   Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA   Garin J., Bourguignon J.;
RT   "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT   cell culture.";
RL   Mol. Cell. Proteomics 6:394-412(2007).
RN   [12]
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: Involved in the regulation of stomatal aperture. May function
CC       as a high-capacity pump for folates. {ECO:0000269|PubMed:15225287}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC   -!- ACTIVITY REGULATION: Inhibited by methotrexate.
CC       {ECO:0000269|PubMed:15225287}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15225287};
CC       Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC       {ECO:0000269|PubMed:17151019}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. High expression in the guard cells.
CC       {ECO:0000269|PubMed:12430019, ECO:0000269|PubMed:15225287}.
CC   -!- INDUCTION: By salicylic acid (SA), menadione and, to a lower extent, by
CC       1-chloro-2,4-dinitrobenzene (CDNB), benoxacor, cloquintocet,
CC       fenchlorazol and fluorazol. {ECO:0000269|PubMed:12430019,
CC       ECO:0000269|PubMed:9271206, ECO:0000269|PubMed:9671034}.
CC   -!- DISRUPTION PHENOTYPE: Plants have larger stomatal aperture and
CC       increased drought susceptibility, but are not affected by the ABA
CC       signal transduction pathway. {ECO:0000269|PubMed:15225287}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR   EMBL; AJ002584; CAA05625.1; -; Genomic_DNA.
DR   EMBL; AF243509; AAF68441.1; -; mRNA.
DR   EMBL; AC005309; AAC63634.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10889.1; -; Genomic_DNA.
DR   EMBL; AK226656; BAE98764.1; -; mRNA.
DR   EMBL; U96399; AAC49797.1; -; mRNA.
DR   PIR; F84919; F84919.
DR   RefSeq; NP_182301.1; NM_130347.5.
DR   AlphaFoldDB; Q7DM58; -.
DR   SMR; Q7DM58; -.
DR   BioGRID; 4727; 1.
DR   IntAct; Q7DM58; 1.
DR   STRING; 3702.AT2G47800.1; -.
DR   iPTMnet; Q7DM58; -.
DR   PaxDb; Q7DM58; -.
DR   PRIDE; Q7DM58; -.
DR   ProteomicsDB; 244376; -.
DR   EnsemblPlants; AT2G47800.1; AT2G47800.1; AT2G47800.
DR   GeneID; 819392; -.
DR   Gramene; AT2G47800.1; AT2G47800.1; AT2G47800.
DR   KEGG; ath:AT2G47800; -.
DR   Araport; AT2G47800; -.
DR   TAIR; locus:2043268; AT2G47800.
DR   eggNOG; KOG0054; Eukaryota.
DR   HOGENOM; CLU_000604_27_1_1; -.
DR   InParanoid; Q7DM58; -.
DR   OMA; ICMATPV; -.
DR   OrthoDB; 138195at2759; -.
DR   PhylomeDB; Q7DM58; -.
DR   BioCyc; ARA:AT2G47800-MON; -.
DR   PRO; PR:Q7DM58; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q7DM58; baseline and differential.
DR   Genevisible; Q7DM58; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:TAIR.
DR   GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR   GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR   CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR   Gene3D; 1.20.1560.10; -; 2.
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; IPR044746; ABCC_6TM_D1.
DR   InterPro; IPR044726; ABCC_6TM_D2.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..1516
FT                   /note="ABC transporter C family member 4"
FT                   /id="PRO_0000226075"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        953..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        992..1012
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1067..1087
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1089..1109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1186..1206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1211..1231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          326..607
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          641..864
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          957..1237
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1274..1508
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          879..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..903
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         676..683
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1308..1315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        1234
FT                   /note="F -> L (in Ref. 5; BAE98764)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1295
FT                   /note="T -> I (in Ref. 5; BAE98764)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1516 AA;  169080 MW;  047751628C58431E CRC64;
     MWLLSSSPWL SELSCSYSAV VEHTSSVPVP IQWLRFVLLS PCPQRALFSA VDFIFLLCFA
     LHKLFSSPSS SSEINGHAEI RKPLIGIRGR TPTRTTAWFK TTVAVTVLLS FCSVVLCVLA
     FTGKRRTQRP WNLIDPLFWL IHAVTHLVIA VLVLHQKRFA ALNHPLSLRI YWISSFVLTS
     LFAVTGIFHF LSDAATSLRA EDVASFFSFP LTAFLLIASV RGITGLVTAE TNSPTKPSDA
     VSVEKSDNVS LYASASVFSK TFWLWMNPLL SKGYKSPLTL EQVPTLSPEH KAERLALLFE
     SSWPKPSENS SHPIRTTLLR CFWKEILFTA ILAIVRLGVM YVGPVLIQSF VDFTSGKRSS
     PWQGYYLVLI LLVAKFVEVL TTHQFNFDSQ KLGMLIRSTL ITALYKKGLK LTGSARQNHG
     VGQIVNYMAV DAQQLSDMML QLHAIWLMPL QVTVALVLLY GSLGASVITA VIGLTGVFVF
     ILLGTQRNNG YQFSLMGNRD SRMKATNEML NYMRVIKFQA WENHFNKRIL KFRDMEFGWL
     SKFLYSIAGN IIVLWSTPVL ISALTFATAL ALGVKLDAGT VFTTTTIFKI LQEPIRTFPQ
     SMISLSQAMI SLGRLDSYMM SKELSEDAVE RALGCDGNTA VEVRDGSFSW DDEDNEPALS
     DINFKVKKGE LTAIVGTVGS GKSSLLASVL GEMHRISGQV RVCGSTGYVA QTSWIENGTV
     QDNILFGLPM VREKYNKVLN VCSLEKDLQM MEFGDKTEIG ERGINLSGGQ KQRIQLARAV
     YQECDVYLLD DVFSAVDAHT GSDIFKKCVR GALKGKTVLL VTHQVDFLHN VDCILVMRDG
     KIVESGKYDE LVSSGLDFGE LVAAHETSME LVEAGADSAA VATSPRTPTS PHASSPRTSM
     ESPHLSDLND EHIKSFLGSH IVEDGSKLIK EEERETGQVS LGVYKQYCTE AYGWWGIVLV
     LFFSLTWQGS LMASDYWLAY ETSAKNAISF DASVFILGYV IIALVSIVLV SIRSYYVTHL
     GLKTAQIFFR QILNSILHAP MSFFDTTPSG RILSRASTDQ TNVDILIPFM LGLVVSMYTT
     LLSIFIVTCQ YAWPTAFFVI PLGWLNIWYR NYYLASSREL TRMDSITKAP IIHHFSESIA
     GVMTIRSFRK QELFRQENVK RVNDNLRMDF HNNGSNEWLG FRLELVGSWV LCISALFMVL
     LPSNVIRPEN VGLSLSYGLS LNSVLFFAIY MSCFVENKMV SVERIKQFTD IPSESEWERK
     ETLPPSNWPF HGNVHLEDLK VRYRPNTPLV LKGITLDIKG GEKVGVVGRT GSGKSTLIQV
     LFRLVEPSGG KIIIDGIDIS TLGLHDLRSR FGIIPQEPVL FEGTVRSNID PTEQYSDEEI
     WKSLERCQLK DVVATKPEKL DSLVVDNGEN WSVGQRQLLC LGRVMLKRSR LLFLDEATAS
     VDSQTDAVIQ KIIREDFASC TIISIAHRIP TVMDGDRVLV IDAGKAKEFD SPARLLERPS
     LFAALVQEYA LRSAGI
 
 
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