Protein: ABC transporter G family member 36 (ABC transporter ABCG.36) (AtABCG36) (Pleiotropic drug resistance protein 8) (AtPDR8) (Protein PENETRATION 3) (Q9XIE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with ABCG37, regulates auxin homeostasis and responses by playing a dual role in coumarine (e.g. esculin) and in the auxin precursor indole 3-butyric acid (IBA) efflux transport, thus influencing cotyledons, roots and root hairs development. Mediates the transport (export into the apoplast) of distinct indole-type metabolites in distinct biological processes; a precursor of 4-O-beta-D-glucosyl-indol-3-yl formamide (4OGlcI3F), a pathogen-inducible tryptophan-derived compound (e.g. upon Blumeria graminis conidiospore inoculation), being a probable substrate in extracellular pathogen defense. Involved in the cellular detoxification of xenobiotics by promoting the excretion of some auxinic herbicides including 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and other members of the phenoxyalkanoic acid family but not 2,4-dichlorophenoxyacetic acid (2,4-D). Mediates thymidine exudation in the rhizosphere. May be a transporter of lignin precursors during tracheary element differentiation. Key factor that controls the extent of cell death in the defense response. Necessary for both callose deposition and glucosinolate activation in response to pathogens. As a central component of nonhost resistance (NHR), required for limiting invasion by nonadapted pathogens including powdery mildews (e.g. Blumeria graminis and Erysiphe pisi), root-penetrating pathogenic fungi (e.g. Fusarium oxysporum), Phakopsora pachyrhizi and Colletotrichum gloeosporioides (anthracnose fungi), probably by sensing Ca(2+) via interactions with calmodulins (e.g. CaM7). Confers resistance to cadmium (Cd) and lead (Pb), probably as an efflux pump of Cd2+ or Cd conjugates, and possibly, of chemicals that mediate pathogen resistance. Promotes resistance to abiotic stresses (e.g. drought and salt stress) and favors general growth by preventing sodium accumulation in plants. Required for microbe-associated molecular patterns (MAMPs)- and salicylic acid (SA)-dependent hypersensitive cell death (HR), involving indole glucosinolate breakdown products (e.g. indole-3-acetonitrile), probably in a PEN2 myrosinase-dependent metabolic pathway, triggered by the recognition of effectors from incompatible pathogens including oomycetes and bacteria (e.g. AvrRpm1 and AvrRps4) and benzothiadiazole- (BTH), and leading to an induced protection against pathogens (e.g. Pseudomonas syringae pv. tomato DC3000, Golovinomyces orontii and Hyaloperonospora arabidopsidis).
Subcellular location: Cell membrane {ECO:0000269|PubMed:16415066, ECO:0000269|PubMed:16473969, ECO:0000269|PubMed:17355438, ECO:0000269|PubMed:19000165, ECO:0000269|PubMed:19648296, ECO:0000269|PubMed:20451385, ECO:0000269|PubMed:20498067, ECO:0000269|PubMed:23836668, ECO:0000269|PubMed:26315018, ECO:0000269|PubMed:27803190, ECO:0000269|PubMed:28910579, ECO:0000269|PubMed:29085068}; Multi-pass membrane protein {ECO:0000269|PubMed:16415066, ECO:0000269|PubMed:16473969, ECO:0000269|PubMed:17355438, ECO:0000269|PubMed:19000165}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:27803190, ECO:0000269|PubMed:28434950}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29085068}; Multi-pass membrane protein {ECO:0000255}. Note=Constitutively present and uniformly distributed throughout the plasma membrane in both leaves epidermal and mesophyll cells of plants in normal conditions (PubMed:23836668, PubMed:28910579). Polarized localization at the outermost side of root epidermal and cap cells, in the outer lateral membrane domain facing the environment; the trafficking and endocytic recycling between the endoplasmic reticulum, the trans-Golgi network and the plasma membrane is ACT7-, EAP3- and ALA3-dependent, but the polar localization to the outer lateral membrane domain requires EXO84B (PubMed:20451385, PubMed:20498067, PubMed:27803190, PubMed:28434950, PubMed:29085068). Incorporated transiently at the host-pathogen interface or into pathogen-induced papillae and haustorial encasement structures outside of the plasma membrane upon infection with a pathogen, in an actin-dependent manner; this translocation seems not regulated by phosphorylation (PubMed:23836668, PubMed:28434950, PubMed:28910579, PubMed:29085068). {ECO:0000269|PubMed:20451385, ECO:0000269|PubMed:20498067, ECO:0000269|PubMed:23836668, ECO:0000269|PubMed:27803190, ECO:0000269|PubMed:28434950, ECO:0000269|PubMed:28910579, ECO:0000269|PubMed:29085068}.
Interaction partners:
- Probable WRKY transcription factor 13
- ABC transporter C family member 2
- Enoyl-CoA hydratase 2, peroxisomal
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Protein LEAD-SENSITIVE 1
- Enoyl-CoA delta isomerase 2, peroxisomal
- Short-chain dehydrogenase/reductase SDRA
- ABC transporter D family member 1
- Probable protein S-acyltransferase 19
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MDYNPNLPPLGGGGVSMRRSISRSVSRASRNIEDIFSSGSRRTQSVNDDEEALKWAAIEKLPTYSRLRTTLMNAVVEDDVYGNQLMSKEVDVTKLDGEDRQKFIDMVFKVAEQDNERILTKLRNRIDRVGIKLPTVEVRYEHLTIKADCYTGNRSLPTLLNVVRNMGESALGMIGIQFAKKAQLTILKDISGVIKPGRMTLLLGPPSSGKTTLLLALAGKLDKSLQVSGDITYNGYQLDEFVPRKTSAYISQNDLHVGIMTVKETLDFSARCQGVGTRYDLLNELARREKDAGIFPEADVDLFMKASAAQGVKNSLVTDYTLKILGLDICKDTIVGDDMMRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTFQIVKCLQQIVHLNEATVLMSLLQPAPETFDLFDDIILVSEGQIVYQGPRDNILEFFESFGFKCPERKGTADFLQEVTSKKDQEQYWVNPNRPYHYIPVSEFASRYKSFHVGTKMSNELAVPFDKSRGHKAALVFDKYSVSKRELLKSCWDKEWLLMQRNAFFYVFKTVQIVIIAAITSTLFLRTEMNTRNEGDANLYIGALLFGMIINMFNGFAEMAMMVSRLPVFYKQRDLLFYPSWTFSLPTFLLGIPSSILESTAWMVVTYYSIGFAPDASRFFKQFLLVFLIQQMAASLFRLIASVCRTMMIANTGGALTLLLVFLLGGFLLPKGKIPDWWGWAYWVSPLTYAFNGLVVNEMFAPRWMNKMASSNSTIKLGTMVLNTWDVYHQKNWYWISVGALLCFTALFNILFTLALTYLNPLGKKAGLLPEEENEDADQGKDPMRRSLSTADGNRRGEVAMGRMSRDSAAEASGGAGNKKGMVLPFTPLAMSFDDVKYFVDMPGEMRDQGVTETRLQLLKGVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDVRISGFPKVQETFARISGYCEQTDIHSPQVTVRESLIFSAFLRLPKEVGKDEKMMFVDQVMELVELDSLRDSIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRAVRNTVDTGRTVVCTIHQPSIDIFEAFDELMLMKRGGQVIYAGPLGQNSHKVVEYFESFPGVSKIPEKYNPATWMLEASSLAAELKLSVDFAELYNQSALHQRNKALVKELSVPPAGASDLYFATQFSQNTWGQFKSCLWKQWWTYWRSPDYNLVRFIFTLATSLLIGTVFWQIGGNRSNAGDLTMVIGALYAAIIFVGINNCSTVQPMVAVERTVFYRERAAGMYSAMPYAISQVTCELPYVLIQTVYYSLIVYAMVGFEWKAEKFFWFVFVSYFSFLYWTYYGMMTVSLTPNQQVASIFASAFYGIFNLFSGFFIPRPKIPKWWIWYYWICPVAWTVYGLIVSQYGDVETRIQVLGGAPDLTVKQYIEDHYGFQSDFMGPVAAVLIAFTVFFAFIFAFCIRTLNFQTR