AB4C_MAIZE
ID AB4C_MAIZE Reviewed; 1510 AA.
AC A7KVC2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ABC transporter C family MRP4 {ECO:0000305};
DE EC=7.-.-.- {ECO:0000305};
DE AltName: Full=Multidrug resistance-associated protein 4 {ECO:0000305};
DE Short=ZmMRP4 {ECO:0000303|PubMed:17676037};
DE AltName: Full=Protein LOW PHYTIC ACID 1 {ECO:0000303|PubMed:17676037};
GN Name=MRP4 {ECO:0000303|PubMed:17676037};
GN Synonyms=LPA1 {ECO:0000303|PubMed:17676037};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. B73;
RX PubMed=17676037; DOI=10.1038/nbt1322;
RA Shi J., Wang H., Schellin K., Li B., Faller M., Stoop J.M., Meeley R.B.,
RA Ertl D.S., Ranch J.P., Glassman K.;
RT "Embryo-specific silencing of a transporter reduces phytic acid content of
RT maize and soybean seeds.";
RL Nat. Biotechnol. 25:930-937(2007).
CC -!- FUNCTION: ABC transporter that may affect phytic acid transport and
CC compartmentalization. May function directly or indirectly in removing
CC phytic acid from the cytosol or in vesicle trafficking. Required for
CC phytic acid accumulation in developing seeds. Phytic acid is the
CC primary storage form of phosphorus in cereal grains and other plant
CC seeds. {ECO:0000269|PubMed:17676037}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stalks, tassels, silks,
CC developing seeds and developing embryos. {ECO:0000269|PubMed:17676037}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction in seed phytic acid, and strong
CC increase of inorganic phosphate and myo-inositol levels in seeds.
CC {ECO:0000269|PubMed:17676037}.
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; EF586878; ABS81429.1; -; mRNA.
DR RefSeq; NP_001106060.1; NM_001112590.1.
DR AlphaFoldDB; A7KVC2; -.
DR SMR; A7KVC2; -.
DR STRING; 4577.GRMZM5G820122_P01; -.
DR TCDB; 3.A.1.208.42; the atp-binding cassette (abc) superfamily.
DR PaxDb; A7KVC2; -.
DR PRIDE; A7KVC2; -.
DR EnsemblPlants; Zm00001eb003490_T001; Zm00001eb003490_P001; Zm00001eb003490.
DR GeneID; 100125659; -.
DR Gramene; Zm00001eb003490_T001; Zm00001eb003490_P001; Zm00001eb003490.
DR KEGG; zma:100125659; -.
DR eggNOG; KOG0054; Eukaryota.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; A7KVC2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0055085; P:transmembrane transport; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1510
FT /note="ABC transporter C family MRP4"
FT /id="PRO_0000431885"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 945..965
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TRANSMEM 1060..1082
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TRANSMEM 1086..1108
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255"
FT TRANSMEM 1154..1174
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255"
FT TRANSMEM 1179..1199
FT /note="Helical; Name=18"
FT /evidence="ECO:0000255"
FT DOMAIN 320..595
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 629..852
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 950..1220
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1267..1501
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 889..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 664..671
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1301..1308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1510 AA; 166790 MW; 1CDA695DE219CA53 CRC64;
MPPSFPSLPL PEAVAATAHA ALLALAALLL LLRAARALAS RCASCLKAPR RRGGPAVVVG
DGAGGALAAA TAGAWHRAVL ASCAYALLSQ VAVLSYEVAV AGSRVSARAL LLPAVQAVSW
AALLALALQA RAVGWARFPA LVRLWWVVSF ALCVVIAYDD SRRLIGQGAR AVDYAHMVAN
FASVPALGFL CLVGVMGSTG LELEFTEDGN GLHEPLLLGR QRREAEEELG CLRVTPYADA
GILSLATLSW LSPLLSVGAQ RPLELADIPL LAHKDRAKSC YKAMSAHYER QRLEYPGREP
SLTWAILKSF WREAAVNGTF AAVNTIVSYV GPYLISYFVD YLSGNIAFPH EGYILASIFF
VAKLLETLTA RQWYLGVDIM GIHVKSGLTA MVYRKGLRLS NASRQSHTSG EIVNYMAVDV
QRVGDYAWYF HDIWMLPLQI ILALAILYKN VGIAMVSTLV ATVLSIAASV PVAKLQEHYQ
DKLMASKDER MRKTSECLKN MRILKLQAWE DRYRLQLEEM RNVECRWLRW ALYSQAAVTF
VFWSSPIFVA VITFGTCILL GGQLTAGGVL SALATFRILQ EPLRNFPDLI SMMAQTRVSL
DRLSHFLQQE ELPDDATINV PQSSTDKAVD IKDGAFSWNP YTLTPTLSDI HLSVVRGMRV
AVCGVIGSGK SSLLSSILGE IPKLCGHVRI SGTAAYVPQT AWIQSGNIEE NILFGSQMDR
QRYKRVIAAC CLKKDLELLQ YGDQTVIGDR GINLSGGQKQ RVQLARALYQ DADIYLLDDP
FSAVDAHTGS ELFKEYILTA LATKTVIYVT HQVEFLPAAD LILVLKDGHI TQAGKYDDLL
QAGTDFNALV SAHKEAIETM DIFEDSDSDT VSSIPNKRLT PSISNIDNLK NKMCENGQPS
NTRGIKEKKK KEERKKKRTV QEEERERGKV SSKVYLSYMG EAYKGTLIPL IILAQTMFQV
LQIASNWWMA WANPQTEGDA PKTDSVVLLV VYMSLAFGSS LFVFMRSLLV ATFGLAAAQK
LFIKMLRCVF RAPMSFFDTT PSGRILNRVS VDQSVVDLDI AFRLGGFAST TIQLLGIVAV
MSKVTWQVLI LIVPMAVACM WMQRYYIASS RELTRILSVQ KSPVIHLFSE SIAGAATIRG
FGQEKRFMKR NLYLLDCFAR PLFSSLAAIE WLCLRMELLS TFVFAFCMAI LVSFPPGTIE
PSMAGLAVTY GLNLNARMSR WILSFCKLEN RIISVERIYQ YCRLPSEAPL IIENCRPPSS
WPQNGNIELI DLKVRYKDDL PLVLHGVSCM FPGGKKIGIV GRTGSGKSTL IQALFRLIEP
TGGKIIIDNI DISAIGLHDL RSRLSIIPQD PTLFEGTIRM NLDPLEECTD QEIWEALEKC
QLGEVIRSKE EKLDSPVLEN GDNWSVGQRQ LIALGRALLK QAKILVLDEA TASVDTATDN
LIQKIIRSEF KDCTVCTIAH RIPTVIDSDL VLVLSDGKIA EFDTPQRLLE DKSSMFIQLV
SEYSTRSSCI
