AB32G_ORYSJ
ID AB32G_ORYSJ Reviewed; 1451 AA.
AC Q8LQX2;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ABC transporter G family member 32 {ECO:0000303|PubMed:18299247};
DE Short=OsABCG32 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Pleiotropic drug resistance protein 16 {ECO:0000303|PubMed:16506311};
DE Short=OsPDR16 {ECO:0000303|PubMed:16506311};
GN Name=ABCG32 {ECO:0000303|PubMed:18299247};
GN Synonyms=PDR16 {ECO:0000303|PubMed:16506311},
GN PDR5 {ECO:0000312|EMBL:AAQ01165.1};
GN OrderedLocusNames=Os01g0342700 {ECO:0000312|EMBL:BAF04869.1},
GN LOC_Os01g24010; ORFNames=B1045F02.15 {ECO:0000312|EMBL:BAB93292.1};
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 [MRNA].
RA Yao Q., Peng R., Xiong A.;
RT "Isolation and characterization of a rice ATPase gene.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16506311; DOI=10.1016/j.febslet.2005.12.043;
RA Crouzet J., Trombik T., Fraysse A.S., Boutry M.;
RT "Organization and function of the plant pleiotropic drug resistance ABC
RT transporter family.";
RL FEBS Lett. 580:1123-1130(2006).
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: May be a general defense protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; AY332479; AAQ01165.1; -; mRNA.
DR EMBL; AP003329; BAB93292.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04869.1; -; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015622300.1; XM_015766814.1.
DR AlphaFoldDB; Q8LQX2; -.
DR SMR; Q8LQX2; -.
DR STRING; 4530.OS01T0342750-01; -.
DR PaxDb; Q8LQX2; -.
DR PRIDE; Q8LQX2; -.
DR GeneID; 4326812; -.
DR KEGG; osa:4326812; -.
DR eggNOG; KOG0065; Eukaryota.
DR InParanoid; Q8LQX2; -.
DR OrthoDB; 324553at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013581; PDR_assoc.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF08370; PDR_assoc; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1451
FT /note="ABC transporter G family member 32"
FT /id="PRO_0000433451"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1197..1217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1237..1257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1312..1332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1373..1393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1423..1443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 162..435
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 513..725
FT /note="ABC transmembrane type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
FT DOMAIN 853..1105
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1178..1392
FT /note="ABC transmembrane type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
FT REGION 809..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 898..905
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1451 AA; 163894 MW; 6EC60CE354C7B664 CRC64;
MAREIHKIAS LRRESSLWRR GDDGVYFSRS STGASSSRFR DEEDDEEALR WAALERLPTR
DRVRRGILLQ AAEGNGEKVE VDVGRMGARE SRALIARLIR AADDDHALFL LKLKDRMDRV
GIDYPTIEVR FEKLEVEAEV HVGNRGLPTL LNSIINTVQA IGNALHISPT RKQPMTVLHD
VSGIIKPRRM TLLLGPPGSG KTTLLLALAG KLEDNLKVSG KVTYNGHGMD EFVPQRTAAY
ISQHDLHIGE MTVRETLAFS ARCQGVGSRY DMLTELSRRE KAENIKPDQD IDVYMKASAI
GGQESSVVTE YILKILGLDI CADTVVGNDM LRGVSGGQRK RVTTGEMLVG PARALFMDEI
STGLDSSTTY QIVNSIGQTI RILGGTAVIS LLQPAPETYN LFDDIILLSD GQIVYQGARE
HVLEFFELMG FRCPQRKGVA DFLQEVTSKK DQEQYWYRND IPYSFVPVKQ FADAFRSFHV
GQSIQNELSE PFDRSRSHPA SLATSKFGVS WMALLKANID RELLLMKRNS FVYIFKAANL
TLTAFLVMTT FLRTKMRHDT TYGTIYMGAL YFALDTIMFN GFAELGMTVM KLPVFFKQRD
LLFFPAWTYT IPSWILQIPV TFFEVGVYVF TTYYVVGFDP NVSRFFKQYL LLVALNQMSS
SLFRFIAGIG RDMVVSQTFG PLSLLAFTAL GGFILARPDV KKWWIWGYWI SPLSYAQNAI
STNEFLGRSW NKSFPGQNDT VGISILKSRG IFTEAKWYWI GFGALIGYTL LFNLLYTVAL
SFLKPLGDSY PSVPEDALKE KRANQTGEIL DSCEEKKSRK KEQSQSVNQK HWNNTAESSQ
IRQGILPFAQ LSLSFNDIKY SVDMPEAMTA QGVTEERLLL LKGVSGSFRP GVLTALMGVS
GAGKTTLMDV LAGRKTGGYI EGDITISGYP KKQETFARIS GYCEQNDIHS PHVTVYESLV
FSAWMRLPSE VDSETRKMFI EEVMELVELT SLRGALVGLP GVNGLSTEQR KRLTVAVELV
ANPSIIFMDE PTSGLDARAA AIVMRTVRKT VDTGRTVVCT IHQPSIDIFE AFDELFLMKR
GGEEIYVGPL GQNSSKLIEY FEGIEGISKI KDGYNPATWM LEVTSTTQEE MLGIDFSEIY
KRSELYQRNK ELIQDLSTPT PGSTDLHFPT QYSRSFFTQC IACLWKHKLS YWRNPSYTAV
RLLFTIIIAL LFGTMFWDLG RKTKKEQDLF NAVGSMYAAV LYIGIQNSGC VQPVVVVERT
VFYRERAAGM YSGFPYAFGQ VAIELPYILV QTLVYGVLVY SMIGFEWTVA KFIWYLFFMY
FTLLYFTFFG MMAVGLTPNE SIAAIISPAI YNAWNLFSGY LIPRPKIPVW WRWYCWICPV
AWTLYGLVAS QFGNIQTKLD GKDQTVAQFI TEYYGFHHDL LWLVAVVHVV FTVMFAFLFS
FAIMKFNFQR R