AB13C_ORYSJ
ID AB13C_ORYSJ Reviewed; 1505 AA.
AC Q10RX7; A0A0P0VSW0;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ABC transporter C family member 13 {ECO:0000303|PubMed:18299247};
DE Short=OsABCC13 {ECO:0000303|PubMed:18299247};
DE EC=7.-.-.- {ECO:0000305};
DE AltName: Full=Multidrug resistance-associated protein 13 {ECO:0000303|PubMed:16375897};
DE Short=OsMRP13 {ECO:0000303|PubMed:16375897};
DE AltName: Full=OsMRP5 {ECO:0000303|PubMed:19370321};
DE AltName: Full=Protein LOW PHYTIC ACID 2 {ECO:0000303|PubMed:19370321};
GN Name=ABCC13 {ECO:0000303|PubMed:18299247};
GN Synonyms=LPA2 {ECO:0000303|PubMed:19370321};
GN OrderedLocusNames=Os03g0142800 {ECO:0000312|EMBL:BAF10848.1},
GN LOC_Os03g04920 {ECO:0000312|EMBL:ABF93919.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16375897; DOI=10.1016/j.febslet.2005.11.056;
RA Klein M., Burla B., Martinoia E.;
RT "The multidrug resistance-associated protein (MRP/ABCC) subfamily of ATP-
RT binding cassette transporters in plants.";
RL FEBS Lett. 580:1112-1122(2006).
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19370321; DOI=10.1007/s00122-009-1018-1;
RA Xu X.H., Zhao H.J., Liu Q.L., Frank T., Engel K.H., An G., Shu Q.Y.;
RT "Mutations of the multi-drug resistance-associated protein ABC transporter
RT gene 5 result in reduction of phytic acid in rice seeds.";
RL Theor. Appl. Genet. 119:75-83(2009).
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:19370321}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf sheaths, leaf blades and
CC developing seeds. {ECO:0000269|PubMed:19370321}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction in seed phytic acid, and strong
CC increase of inorganic phosphate and myo-inositol levels in seeds.
CC Seedling lethality when homozygous. {ECO:0000269|PubMed:19370321}.
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; DP000009; ABF93919.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10848.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82235.1; -; Genomic_DNA.
DR RefSeq; XP_015630971.1; XM_015775485.1.
DR AlphaFoldDB; Q10RX7; -.
DR SMR; Q10RX7; -.
DR STRING; 4530.OS03T0142800-01; -.
DR TCDB; 3.A.1.208.34; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q10RX7; -.
DR PRIDE; Q10RX7; -.
DR EnsemblPlants; Os03t0142800-01; Os03t0142800-01; Os03g0142800.
DR GeneID; 4331585; -.
DR Gramene; Os03t0142800-01; Os03t0142800-01; Os03g0142800.
DR KEGG; osa:4331585; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q10RX7; -.
DR OMA; FVKFFGW; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q10RX7; baseline and differential.
DR Genevisible; Q10RX7; OS.
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..1505
FT /note="ABC transporter C family member 13"
FT /id="PRO_0000431886"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..68
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TRANSMEM 1055..1077
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TRANSMEM 1081..1103
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255"
FT TRANSMEM 1149..1169
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255"
FT TRANSMEM 1174..1194
FT /note="Helical; Name=18"
FT /evidence="ECO:0000255"
FT DOMAIN 314..589
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 623..846
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 945..1215
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1262..1496
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 881..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 658..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1296..1303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1505 AA; 166149 MW; 037D36E9F71112DB CRC64;
MPHFPNLPLP EAAAAAAHAA LLALALLLLL LRSARALASR CASCLKTAPR RAAAVDGGLA
AASSVGAWYR AALACCGYAL LAQVAALSYE VAVAGSHVAV EALLLPAVQA LAWAALLALA
MQARAVGWGR FPVLVRVWWV VSFVLCVGIA YDDTRHLMGD DDDDEVDYAH MVANFASAPA
LGFLCLVGVM GSTGVELEFT DDDSSVHEPL LLGGQRRDAD EEPGCLRVTP YGDAGIVSLA
TLSWLSPLLS VGAQRPLELA DIPLMAHKDR AKSCYKAMSS HYERQRMERP GSEPSLAWAI
LKSFWREAAI NGAFAAVNTI VSYVGPYLIS YFVDYLSGKI EFPHEGYILA SVFFVAKLLE
TLTARQWYLG VDVMGIHVKS GLTAMVYRKG LRLSNSSRQS HTSGEIVNYM AVDVQRVGDY
AWYFHDIWML PLQIILALAI LYKNVGIAMV STLVATVLSI AASVPVAKLQ EHYQDKLMAS
KDERMRKTSE CLKNMRILKL QAWEDRYRLK LEEMRNVECK WLRWALYSQA AVTFVFWSSP
IFVAVITFGT CILLGGELTA GGVLSALATF RILQEPLRNF PDLISMIAQT RVSLDRLSHF
LQQEELPDDA TITVPHGSTD KAININDATF SWNPSSPTPT LSGINLSVVR GMRVAVCGVI
GSGKSSLLSS ILGEIPKLCG QVRISGSAAY VPQTAWIQSG NIEENILFGS PMDKQRYKRV
IEACSLKKDL QLLQYGDQTI IGDRGINLSG GQKQRVQLAR ALYQDADIYL LDDPFSAVDA
HTGSELFREY ILTALASKTV IYVTHQIEFL PAADLILVLK DGHITQAGKY DDLLQAGTDF
NALVCAHKEA IETMEFSEDS DEDTVSSVPI KRLTPSVSNI DNLKNKVSNN EKPSSTRGIK
EKKKKPEERK KKRSVQEEER ERGRVSLQVY LSYMGEAYKG TLIPLIILAQ TMFQVLQIAS
NWWMAWANPQ TEGDAPKTDS VVLLVVYMSL AFGSSLFVFV RSLLVATFGL ATAQKLFVKM
LRCVFRAPMS FFDTTPSGRI LNRVSVDQSV VDLDIAFRLG GFASTTIQLL GIVAVMSKVT
WQVLILIVPM AVACMWMQRY YIASSRELTR ILSVQKSPVI HLFSESIAGA ATIRGFGQEK
RFMKRNLYLL DCFARPLFSS LAAIEWLCLR MELLSTFVFA FCMAILVSFP PGTIEPSMAG
LAVTYGLNLN ARMSRWILSF CKLENRIISV ERIYQYCKLP SEAPLIIENS RPSSSWPENG
NIELVDLKVR YKDDLPLVLH GISCIFPGGK KIGIVGRTGS GKSTLIQALF RLIEPTGGKV
IIDDVDISRI GLHDLRSRLS IIPQDPTLFE GTIRMNLDPL EECTDQEIWE ALEKCQLGEV
IRSKDEKLDS PVLENGDNWS VGQRQLIALG RALLKQAKIL VLDEATASVD TATDNLIQKI
IRSEFKDCTV CTIAHRIPTV IDSDLVLVLS DGKIAEFDTP QRLLEDKSSM FMQLVSEYST
RSSCI
