ACD11_ARATH
ID ACD11_ARATH Reviewed; 206 AA.
AC O64587; A0A097PRA1;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Accelerated cell death 11 {ECO:0000303|PubMed:11850411};
DE AltName: Full=Ceramide-1-phosphate transfer protein ACD11 {ECO:0000305};
DE AltName: Full=Glycolipid transfer protein domain-containing protein ACD11 {ECO:0000305};
GN Name=ACD11 {ECO:0000303|PubMed:11850411};
GN OrderedLocusNames=At2g34690 {ECO:0000312|Araport:AT2G34690};
GN ORFNames=T29F13.10 {ECO:0000312|EMBL:AAC16265.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-204.
RX PubMed=25249442; DOI=10.1038/ncomms5956;
RA Zeng L., Zhang Q., Sun R., Kong H., Zhang N., Ma H.;
RT "Resolution of deep angiosperm phylogeny using conserved nuclear genes and
RT estimates of early divergence times.";
RL Nat. Commun. 5:4956-4956(2014).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11850411; DOI=10.1101/gad.218202;
RA Brodersen P., Petersen M., Pike H.M., Olszak B., Skov S., Odum N.,
RA Jorgensen L.B., Brown R.E., Mundy J.;
RT "Knockout of Arabidopsis accelerated-cell-death11 encoding a sphingosine
RT transfer protein causes activation of programmed cell death and defense.";
RL Genes Dev. 16:490-502(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15923330; DOI=10.1104/pp.105.059303;
RA Brodersen P., Malinovsky F.G., Hematy K., Newman M.A., Mundy J.;
RT "The role of salicylic acid in the induction of cell death in Arabidopsis
RT acd11.";
RL Plant Physiol. 138:1037-1045(2005).
RN [7]
RP 3D-STRUCTURE MODELING.
RX PubMed=16309699; DOI=10.1016/j.jmb.2005.10.031;
RA Airenne T.T., Kidron H., Nymalm Y., Nylund M., West G., Mattjus P.,
RA Salminen T.A.;
RT "Structural evidence for adaptive ligand binding of glycolipid transfer
RT protein.";
RL J. Mol. Biol. 355:224-236(2006).
RN [8]
RP FUNCTION, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF ASP-60; ARG-103 AND
RP HIS-143.
RX PubMed=18657186; DOI=10.1111/j.1742-4658.2008.06584.x;
RA Petersen N.H., McKinney L.V., Pike H., Hofius D., Zakaria A., Brodersen P.,
RA Petersen M., Brown R.E., Mundy J.;
RT "Human GLTP and mutant forms of ACD11 suppress cell death in the
RT Arabidopsis acd11 mutant.";
RL FEBS J. 275:4378-4388(2008).
RN [9]
RP INTERACTION WITH BPA1; PRA1F2 AND PRA1F3, AND SUBCELLULAR LOCATION.
RX PubMed=18845362; DOI=10.1016/j.jplph.2008.08.003;
RA Petersen N.H., Joensen J., McKinney L.V., Brodersen P., Petersen M.,
RA Hofius D., Mundy J.;
RT "Identification of proteins interacting with Arabidopsis ACD11.";
RL J. Plant Physiol. 166:661-666(2009).
RN [10]
RP FUNCTION, AND LIPID-BINDING.
RX PubMed=28011644; DOI=10.1074/jbc.m116.760256;
RA Zhai X., Gao Y.G., Mishra S.K., Simanshu D.K., Boldyrev I.A., Benson L.M.,
RA Bergen H.R. III, Malinina L., Mundy J., Molotkovsky J.G., Patel D.J.,
RA Brown R.E.;
RT "Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane
RT Transfer by C1P Transfer Proteins.";
RL J. Biol. Chem. 292:2531-2541(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATES,
RP FUNCTION, MUTAGENESIS OF PHE-47; ASP-60; LYS-64; ARG-99 AND ARG-103, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24412362; DOI=10.1016/j.celrep.2013.12.023;
RA Simanshu D.K., Zhai X., Munch D., Hofius D., Markham J.E., Bielawski J.,
RA Bielawska A., Malinina L., Molotkovsky J.G., Mundy J.W., Patel D.J.,
RA Brown R.E.;
RT "Arabidopsis accelerated cell death 11, ACD11, is a ceramide-1-phosphate
RT transfer protein and intermediary regulator of phytoceramide levels.";
RL Cell Rep. 6:388-399(2014).
CC -!- FUNCTION: Exhibits selective intermembrane transfer of ceramide-1-
CC phosphate (C1P) and phytoceramide-1-phosphate (PubMed:24412362,
CC PubMed:28011644). Does not transport ceramide (Cer) or GalCer,
CC suggesting a requirement for phosphate in the headgroup for
CC functionality (PubMed:24412362). Transports in vitro sphingosine, but
CC not glycosphingolipids (PubMed:11850411). Has also some in vitro
CC activity with sphingomyelin, a lipid not detected in plant tissues
CC (PubMed:18657186). The transport function may be not directly involved
CC in regulating cell death. Rather, perturbations in the function of
CC ACD11 or related components could be monitored by R-proteins, which
CC then mediate defense and programmed cell death (PCD), as proposed in
CC the guard hypothesis (Probable). C1P transfer is stimulated by
CC phosphatidylserine in C1P source vesicles (PubMed:28011644). Regulates
CC autophagy, inflammasome mediated IL1B and IL18 processing, and
CC pyroptosis, but not apoptosis (PubMed:28011644).
CC {ECO:0000269|PubMed:11850411, ECO:0000269|PubMed:18657186,
CC ECO:0000269|PubMed:24412362, ECO:0000269|PubMed:28011644,
CC ECO:0000305|PubMed:18845362}.
CC -!- SUBUNIT: Interacts with BPA1, PRA1F2 and PRA1F3 (PubMed:18845362).
CC {ECO:0000269|PubMed:18845362}.
CC -!- INTERACTION:
CC O64587; Q9LFD5: BPA1; NbExp=4; IntAct=EBI-2010923, EBI-2010933;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18845362}.
CC -!- DISRUPTION PHENOTYPE: Constitutive expression of defense-related genes
CC that accompany the hypersensitive response normally triggered by
CC avirulent pathogens. Induction of growth inhibition, premature leaf
CC chlorosis and defense-related programmed cell death (PCD) at the early
CC seedling stage, leading to a lethal phenotype before flowering
CC (PubMed:11850411, PubMed:15923330). Large increase of cell death
CC inducer phytoceramide (PubMed:24412362). {ECO:0000269|PubMed:11850411,
CC ECO:0000269|PubMed:15923330, ECO:0000269|PubMed:24412362}.
CC -!- MISCELLANEOUS: The clustered Lys-64/Arg-99/Arg-103 residues form a
CC positively charged triad ideally arranged for binding phosphate,
CC explaining the inability to bind sugar headgroups and transfer
CC glycoproteins. {ECO:0000269|PubMed:24412362}.
CC -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR EMBL; AC003096; AAC16265.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09010.1; -; Genomic_DNA.
DR EMBL; BT012177; AAS76271.1; -; mRNA.
DR EMBL; KM399929; AIU50562.1; -; mRNA.
DR PIR; T01366; T01366.
DR RefSeq; NP_181016.1; NM_129023.5.
DR PDB; 4NT1; X-ray; 1.80 A; A/B/C/D=1-206.
DR PDB; 4NT2; X-ray; 2.40 A; A=1-206.
DR PDB; 4NTG; X-ray; 2.55 A; A/B=1-206.
DR PDB; 4NTI; X-ray; 2.90 A; A/B=1-206.
DR PDB; 4NTO; X-ray; 2.15 A; A/B/C=1-206.
DR PDBsum; 4NT1; -.
DR PDBsum; 4NT2; -.
DR PDBsum; 4NTG; -.
DR PDBsum; 4NTI; -.
DR PDBsum; 4NTO; -.
DR AlphaFoldDB; O64587; -.
DR SMR; O64587; -.
DR IntAct; O64587; 4.
DR STRING; 3702.AT2G34690.1; -.
DR PaxDb; O64587; -.
DR PRIDE; O64587; -.
DR ProteomicsDB; 244382; -.
DR DNASU; 818034; -.
DR EnsemblPlants; AT2G34690.1; AT2G34690.1; AT2G34690.
DR GeneID; 818034; -.
DR Gramene; AT2G34690.1; AT2G34690.1; AT2G34690.
DR KEGG; ath:AT2G34690; -.
DR Araport; AT2G34690; -.
DR TAIR; locus:2061529; AT2G34690.
DR eggNOG; KOG4189; Eukaryota.
DR HOGENOM; CLU_082630_0_0_1; -.
DR InParanoid; O64587; -.
DR OMA; YKFFQLM; -.
DR OrthoDB; 1423493at2759; -.
DR PhylomeDB; O64587; -.
DR PRO; PR:O64587; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64587; baseline and differential.
DR Genevisible; O64587; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1902387; F:ceramide 1-phosphate binding; IBA:GO_Central.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; IBA:GO_Central.
DR GO; GO:0140338; F:sphingomyelin transfer activity; IDA:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR GO; GO:0009751; P:response to salicylic acid; IMP:TAIR.
DR Gene3D; 1.10.3520.10; -; 1.
DR InterPro; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR Pfam; PF08718; GLTP; 1.
DR SUPFAM; SSF110004; SSF110004; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid transport; Lipid-binding;
KW Reference proteome; Transport.
FT CHAIN 1..206
FT /note="Accelerated cell death 11"
FT /id="PRO_0000432642"
FT BINDING 60
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000269|PubMed:24412362"
FT BINDING 64
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000269|PubMed:24412362"
FT BINDING 99
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000269|PubMed:24412362"
FT BINDING 103
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000269|PubMed:24412362"
FT BINDING 143
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 47
FT /note="F->Q: Decreased activity."
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 60
FT /note="D->A: Loss of 85% of activity."
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 60
FT /note="D->N: Loss of 70% of activity."
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 60
FT /note="D->V: Loss of lipid transfer, but no effect on PCD
FT suppression."
FT /evidence="ECO:0000269|PubMed:18657186"
FT MUTAGEN 64
FT /note="K->A: Severe reduction in C1P transfer."
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 99
FT /note="R->A,E: Severe reduction in C1P transfer."
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 103
FT /note="R->A: Severe reduction in C1P transfer."
FT /evidence="ECO:0000269|PubMed:24412362"
FT MUTAGEN 103
FT /note="R->W: No gain of galacosylceramide transfer and no
FT effect on PCD suppression."
FT /evidence="ECO:0000269|PubMed:18657186"
FT MUTAGEN 143
FT /note="H->L: Loss of lipid transfer, but no effect on PCD
FT suppression."
FT /evidence="ECO:0000269|PubMed:18657186"
FT CONFLICT 30
FT /note="Missing (in Ref. 4; AIU50562)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="Missing (in Ref. 4; AIU50562)"
FT /evidence="ECO:0000305"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:4NT1"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4NT1"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:4NTO"
FT HELIX 97..120
FT /evidence="ECO:0007829|PDB:4NT1"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:4NT1"
FT HELIX 172..198
FT /evidence="ECO:0007829|PDB:4NT1"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4NT1"
SQ SEQUENCE 206 AA; 22680 MW; 430928C6A134FB4A CRC64;
MADSEADKPL RKISAAFKKL AIIVNSPNPE VPVTQFSHAC SLVSPLFGCL GIAFKFAEMD
YVAKVDDLVR ASSSISTLVV MMDKDIEADC VRKAGSHTRN LLRVKRGLDM VKVLFEQIIA
SEGDNSLKDP ATKSYAQVFA PHHGWAIRKA VSLGMYALPT RAHLLNMLKE DEAAAKIHMQ
SYVNSSAPLI TYLDNLFLSK QLGIDW
