AB5G_ORYSJ
ID AB5G_ORYSJ Reviewed; 787 AA.
AC Q8H8V7; A0A0P0VW96;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ABC transporter G family member 5 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.5 {ECO:0000303|PubMed:18299247};
DE Short=OsABCG5 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Protein REDUCED CULM NUMBER 1 {ECO:0000303|PubMed:19140940};
DE AltName: Full=White-brown complex homolog protein 5 {ECO:0000303|PubMed:22996334};
DE Short=OsWBC5 {ECO:0000303|PubMed:22996334};
GN Name=RCN1 {ECO:0000303|PubMed:19140940};
GN Synonyms=WBC5 {ECO:0000303|PubMed:22996334};
GN OrderedLocusNames=LOC_Os03g17350 {ECO:0000312|EMBL:ABF95316.1},
GN Os03g0281900 {ECO:0000312|EMBL:BAF11660.1};
GN ORFNames=OsJ_10379 {ECO:0000312|EMBL:EAZ26487.1};
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 {ECO:0000312|Proteomes:UP000059680};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-488 AND ALA-685.
RC STRAIN=cv. Akamuro, and cv. Shiokari;
RX PubMed=19140940; DOI=10.1111/j.1469-8137.2008.02724.x;
RA Yasuno N., Takamure I., Kidou S., Tokuji Y., Ureshi A.N., Funabiki A.,
RA Ashikaga K., Yamanouchi U., Yano M., Kato K.;
RT "Rice shoot branching requires an ATP-binding cassette subfamily G
RT protein.";
RL New Phytol. 182:91-101(2009).
RN [9]
RP FUNCTION, INDUCTION BY BIOTIC AND ABIOTIC STRESSES, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Shiokari;
RX PubMed=22996334; DOI=10.1007/s00438-012-0719-3;
RA Matsuda S., Funabiki A., Furukawa K., Komori N., Koike M., Tokuji Y.,
RA Takamure I., Kato K.;
RT "Genome-wide analysis and expression profiling of half-size ABC protein
RT subgroup G in rice in response to abiotic stress and phytohormone
RT treatments.";
RL Mol. Genet. Genomics 287:819-835(2012).
RN [10]
RP FUNCTION, MUTAGENESIS OF ARG-488 AND ALA-685, INDUCTION BY DEOXYGENATED
RP CONDITIONS, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Akamuro, and cv. Shiokari;
RX PubMed=25041515; DOI=10.1111/tpj.12614;
RA Shiono K., Ando M., Nishiuchi S., Takahashi H., Watanabe K., Nakamura M.,
RA Matsuo Y., Yasuno N., Yamanouchi U., Fujimoto M., Takanashi H.,
RA Ranathunge K., Franke R.B., Shitan N., Nishizawa N.K., Takamure I.,
RA Yano M., Tsutsumi N., Schreiber L., Yazaki K., Nakazono M., Kato K.;
RT "RCN1/OsABCG5, an ATP-binding cassette (ABC) transporter, is required for
RT hypodermal suberization of roots in rice (Oryza sativa).";
RL Plant J. 80:40-51(2014).
RN [11]
RP FUNCTION, MUTAGENESIS OF ALA-685, AND INDUCTION BY SALT AND OSMOTIC
RP STRESSES.
RC STRAIN=cv. Shiokari;
RX PubMed=24908511; DOI=10.1016/j.plantsci.2014.04.011;
RA Matsuda S., Nagasawa H., Yamashiro N., Yasuno N., Watanabe T., Kitazawa H.,
RA Takano S., Tokuji Y., Tani M., Takamure I., Kato K.;
RT "Rice RCN1/OsABCG5 mutation alters accumulation of essential and
RT nonessential minerals and causes a high Na/K ratio, resulting in a salt-
RT sensitive phenotype.";
RL Plant Sci. 224:103-111(2014).
CC -!- FUNCTION: Essential transporter for growth and development under
CC abiotic stress (PubMed:22996334). Mediates shoot branching by promoting
CC the outgrowth of lateral shoots (PubMed:19140940). Required for salt
CC tolerance via Na/K homeostasis, at least partly by regulating
CC SKC1/OsHKT1;5 (PubMed:24908511). Necessary for hypodermal suberization
CC of roots, which contributes to formation of the apoplastic barrier
CC (PubMed:25041515). {ECO:0000269|PubMed:19140940,
CC ECO:0000269|PubMed:24908511, ECO:0000269|PubMed:25041515,
CC ECO:0000305|PubMed:22996334}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25041515};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the crown root primordia, endodermis,
CC pericycle and stele in the root, in leaf primordia of main and axillary
CC shoots, and in the vascular cells and leaf epidermis of older leaves.
CC {ECO:0000269|PubMed:19140940}.
CC -!- INDUCTION: Strongly up-regulated in roots after exposure to salt and
CC osmotic stresses (PubMed:24908511). Induced in roots by
CC benzylaminopurine (BAP), abscisic acid (ABA) and salicylic acid (SA)
CC (PubMed:22996334). Accumulates in shoots upon heat (e.g. 42 degrees
CC Celsius) (PubMed:22996334). Repressed in roots by NaCl, jasmonic acid
CC (JA), gibberellic acid (GA) and auxin (IAA) (PubMed:22996334).
CC Accumulates in most hypodermal and some endodermal roots cells under
CC stagnant deoxygenated conditions leading to hypoxia (PubMed:25041515).
CC {ECO:0000269|PubMed:22996334, ECO:0000269|PubMed:24908511,
CC ECO:0000269|PubMed:25041515}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK072135; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC084405; AAN64474.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF95316.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11660.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83580.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ26487.1; -; Genomic_DNA.
DR EMBL; AK072135; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015628264.1; XM_015772778.1.
DR AlphaFoldDB; Q8H8V7; -.
DR SMR; Q8H8V7; -.
DR STRING; 4530.OS03T0281900-01; -.
DR PaxDb; Q8H8V7; -.
DR PRIDE; Q8H8V7; -.
DR EnsemblPlants; Os03t0281900-01; Os03t0281900-01; Os03g0281900.
DR GeneID; 4332449; -.
DR Gramene; Os03t0281900-01; Os03t0281900-01; Os03g0281900.
DR KEGG; osa:4332449; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_8_1; -.
DR InParanoid; Q8H8V7; -.
DR OMA; ANIGYAC; -.
DR OrthoDB; 1022017at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q8H8V7; OS.
DR GO; GO:0048226; C:Casparian strip; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0048225; C:suberin network; IMP:UniProtKB.
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:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:UniProtKB.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0055078; P:sodium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010345; P:suberin biosynthetic process; IEP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Membrane;
KW Nucleotide-binding; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..787
FT /note="ABC transporter G family member 5"
FT /id="PRO_0000430947"
FT TRANSMEM 500..520
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..745
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT DOMAIN 121..382
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 484..691
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 488
FT /note="R->C: In rcn1-1; altered shoot branching due to
FT impaired outgrowth of tiller buds leading to reduced culm
FT number. Short roots lacking suberized hypodermis in
FT waterlogged soil."
FT /evidence="ECO:0000269|PubMed:19140940,
FT ECO:0000269|PubMed:25041515"
FT MUTAGEN 685
FT /note="A->P: In rcn1-2; altered shoot branching due to
FT impaired outgrowth of tiller buds leading to reduced culm
FT number. Short roots lacking suberized hypodermis in
FT waterlogged soil. Disturbed accumulation of essential and
FT nonessential minerals leading to a high Na/K ratio, thus
FT resulting in a salt-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:19140940,
FT ECO:0000269|PubMed:24908511, ECO:0000269|PubMed:25041515"
FT CONFLICT 503
FT /note="I -> T (in Ref. 6; AK072135)"
SQ SEQUENCE 787 AA; 86968 MW; AE4EBA639F533559 CRC64;
MSRFVDKLPL FDRRPSPMEE AEGLPRSGYL GQLHHHQYYQ PHSNMLPLEQ SPPTSTKHTS
VTLAQLLKRV NDARSGSSTP ISSPRYTIEL GGSKPESVSS ESDDHHSDDG GSEGQPRALV
LKFTDLTYSV KQRRKGSCLP FRRAAADEPE LPAMRTLLDG ISGEARDGEI MAVLGASGSG
KSTLIDALAN RIAKESLHGS VTINGESIDS NLLKVISAYV RQEDLLYPML TVEETLMFAA
EFRLPRSLPT REKKKRVKEL IDQLGLKRAA NTIIGDEGHR GVSGGERRRV SIGVDIIHNP
IMLFLDEPTS GLDSTSAFMV VTVLKAIAQS GSVVVMSIHQ PSYRILGLLD RLLFLSRGKT
VYYGPPSELP PFFLDFGKPI PDNENPTEFA LDLIKEMETE TEGTKRLAEH NAAWQLKHHG
EGRGYGGKPG MSLKEAISAS ISRGKLVSGA TDGTVSVAAS DHSAPPPSSS SVSKFVNPFW
IEMGVLTRRA FINTKRTPEV FIIRLAAVLV TGFILATIFW RLDESPKGVQ ERLGFFAIAM
STMYYTCSDA LPVFLSERYI FLRETAYNAY RRSSYVLSHT IVGFPSLVVL SFAFALTTFF
SVGLAGGVNG FFYFVAIVLA SFWAGSGFAT FLSGVVTHVM LGFPVVLSTL AYFLLFSGFF
INRDRIPRYW LWFHYISLVK YPYEAVMQNE FGDPTRCFVR GVQMFDNTPL AALPAAVKVR
VLQSMSASLG VNIGTGTCIT TGPDFLKQQA ITDFGKWECL WITVAWGFLF RILFYISLLL
GSRNKRR
