SLAC1_ARATH
ID SLAC1_ARATH Reviewed; 556 AA.
AC Q9LD83;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Guard cell S-type anion channel SLAC1 {ECO:0000305};
DE AltName: Full=Protein CARBON DIOXIDE INSENSITIVE 3 {ECO:0000305};
DE AltName: Full=Protein OZONE-SENSITIVE 1 {ECO:0000303|PubMed:18084014};
DE AltName: Full=Protein RADICAL-INDUCED CELL DEATH 3 {ECO:0000303|Ref.4};
DE AltName: Full=Protein SLOW ANION CHANNEL-ASSOCIATED 1 {ECO:0000303|PubMed:18305482};
GN Name=SLAC1 {ECO:0000303|PubMed:18305482};
GN Synonyms=CDI3 {ECO:0000305}, OZS1 {ECO:0000303|PubMed:18084014},
GN RCD3 {ECO:0000303|Ref.4};
GN OrderedLocusNames=At1g12480 {ECO:0000312|Araport:AT1G12480};
GN ORFNames=F5O11.23 {ECO:0000312|EMBL:AAF79652.1},
GN T12C24.3 {ECO:0000312|EMBL:AAF88102.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX DOI=10.1111/j.1365-3040.2005.01325.x;
RA Kangasjaervi J., Jaspers P., Kollist H.;
RT "Signalling and cell death in ozone-exposed plants.";
RL Plant Cell Environ. 28:1021-1036(2005).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-194, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=18305482; DOI=10.1038/nature06720;
RA Negi J., Matsuda O., Nagasawa T., Oba Y., Takahashi H., Kawai-Yamada M.,
RA Uchimiya H., Hashimoto M., Iba K.;
RT "CO2 regulator SLAC1 and its homologues are essential for anion homeostasis
RT in plant cells.";
RL Nature 452:483-486(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP SER-456, AND TISSUE SPECIFICITY.
RX PubMed=18305484; DOI=10.1038/nature06608;
RA Vahisalu T., Kollist H., Wang Y.-F., Nishimura N., Chan W.-Y., Valerio G.,
RA Lamminmaeki A., Brosche M., Moldau H., Desikan R., Schroeder J.I.,
RA Kangasjaervi J.;
RT "SLAC1 is required for plant guard cell S-type anion channel function in
RT stomatal signalling.";
RL Nature 452:487-491(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia GL1;
RX PubMed=18084014; DOI=10.1093/pcp/pcm174;
RA Saji S., Bathula S., Kubo A., Tamaoki M., Kanna M., Aono M., Nakajima N.,
RA Nakaji T., Takeda T., Asayama M., Saji H.;
RT "Disruption of a gene encoding C4-dicarboxylate transporter-like protein
RT increases ozone sensitivity through deregulation of the stomatal response
RT in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:2-10(2008).
RN [8]
RP REVIEW.
RX PubMed=19181866; DOI=10.1093/jxb/ern340;
RA Sirichandra C., Wasilewska A., Vlad F., Valon C., Leung J.;
RT "The guard cell as a single-cell model towards understanding drought
RT tolerance and abscisic acid action.";
RL J. Exp. Bot. 60:1439-1463(2009).
RN [9]
RP FUNCTION, INDUCTION, PHOSPHORYLATION, INTERACTION WITH SRK2E/OST1 AND
RP PP2CA, AND SUBCELLULAR LOCATION.
RX PubMed=19955427; DOI=10.1073/pnas.0910601106;
RA Lee S.C., Lan W., Buchanan B.B., Luan S.;
RT "A protein kinase-phosphatase pair interacts with an ion channel to
RT regulate ABA signaling in plant guard cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21419-21424(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-194, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SRK2E/OST1.
RX PubMed=19955405; DOI=10.1073/pnas.0912021106;
RA Geiger D., Scherzer S., Mumm P., Stange A., Marten I., Bauer H., Ache P.,
RA Matschi S., Liese A., Al-Rasheid K.A.S., Romeis T., Hedrich R.;
RT "Activity of guard cell anion channel SLAC1 is controlled by drought-stress
RT signaling kinase-phosphatase pair.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009).
RN [11]
RP SUBUNIT, MEMBRANE TOPOLOGY, GATING SITE, AND MUTAGENESIS OF GLY-194;
RP PHE-450 AND SER-456.
RX DOI=10.1038/nature09487;
RA Chen Y.-H., Hu L., Punta M., Bruni R., Hillerish B., Kloss B., Rost B.,
RA Love J., Siegelbaum S.A., Hendrickson W.A.;
RT "Homologue structure of the SLAC1 anion channel for closing stomata in
RT leaves.";
RL Nature 467:1074-1080(2010).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-59; SER-86; SER-113;
RP SER-120 AND SER-146, PHOSPHORYLATION BY SRK2E/OST1, MUTAGENESIS OF SER-120
RP AND SER-146, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=20128877; DOI=10.1111/j.1365-313x.2010.04159.x;
RA Vahisalu T., Puzorjova I., Brosche M., Valk E., Lepiku M., Moldau H.,
RA Pechter P., Wang Y.-S., Lindgren O., Salojaervi J., Loog M.,
RA Kangasjaervi J., Kollist H.;
RT "Ozone-triggered rapid stomatal response involves the production of
RT reactive oxygen species, and is controlled by SLAC1 and OST1.";
RL Plant J. 62:442-453(2010).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20345603; DOI=10.1111/j.1365-313x.2010.04213.x;
RA Ache P., Bauer H., Kollist H., Al-Rasheid K.A.S., Lautner S., Hartung W.,
RA Hedrich R.;
RT "Stomatal action directly feeds back on leaf turgor: new insights into the
RT regulation of the plant water status from non-invasive pressure probe
RT measurements.";
RL Plant J. 62:1072-1082(2010).
RN [14]
RP INTERACTION WITH CPK6; CPK21 AND CPK23, AND PHOSPHORYLATION BY CPK21 AND
RP CPK23.
RX PubMed=20385816; DOI=10.1073/pnas.0912030107;
RA Geiger D., Scherzer S., Mumm P., Marten I., Ache P., Matschi S., Liese A.,
RA Wellmann C., Al-Rasheid K.A.S., Grill E., Romeis T., Hedrich R.;
RT "Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with
RT distinct Ca2+ affinities.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010).
RN [15]
RP INTERACTION WITH GHR1, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=22730405; DOI=10.1105/tpc.112.100107;
RA Hua D., Wang C., He J., Liao H., Duan Y., Zhu Z., Guo Y., Chen Z., Gong Z.;
RT "A plasma membrane receptor kinase, GHR1, mediates abscisic acid- and
RT hydrogen peroxide-regulated stomatal movement in Arabidopsis.";
RL Plant Cell 24:2546-2561(2012).
RN [16]
RP FUNCTION, INTERACTION WITH KAT1; KAT2; KAT3/KC1 AND AKT2, AND INDUCTION BY
RP DROUGHT STRESS.
RX PubMed=27002025; DOI=10.1105/tpc.16.01050;
RA Zhang A., Ren H.M., Tan Y.Q., Qi G.N., Yao F.Y., Wu G.L., Yang L.W.,
RA Hussain J., Sun S.J., Wang Y.F.;
RT "S-type anion channels SLAC1 and SLAH3 function as essential negative
RT regulators of inward K+ channels and stomatal opening in Arabidopsis.";
RL Plant Cell 28:949-955(2016).
RN [17]
RP ACTIVITY REGULATION, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=27694184; DOI=10.1105/tpc.16.00131;
RA Horak H., Sierla M., Toldsepp K., Wang C., Wang Y.-S., Nuhkat M., Valk E.,
RA Pechter P., Merilo E., Salojaervi J., Overmyer K., Loog M., Brosche M.,
RA Schroeder J.I., Kangasjaervi J., Kollist H.;
RT "A dominant mutation in the HT1 kinase uncovers roles of MAP kinases and
RT GHR1 in CO2-induced stomatal closure.";
RL Plant Cell 28:2493-2509(2016).
RN [18]
RP INTERACTION WITH GHR1.
RC STRAIN=cv. Columbia, and cv. Columbia GL1;
RX PubMed=30361234; DOI=10.1105/tpc.18.00441;
RA Sierla M., Horak H., Overmyer K., Waszczak C., Yarmolinsky D.,
RA Maierhofer T., Vainonen J.P., Denessiouk K., Salojaervi J., Laanemets K.,
RA Toldsepp K., Vahisalu T., Gauthier A., Puukko T., Paulin L., Auvinen P.,
RA Geiger D., Hedrich R., Kollist H., Kangasjaervi J.;
RT "The receptor-like pseudokinase GHR1 is required for stomatal closure.";
RL Plant Cell 30:2813-2837(2018).
RN [19]
RP FUNCTION.
RX PubMed=29463779; DOI=10.1126/scisignal.aam9514;
RA Devireddy A.R., Zandalinas S.I., Gomez-Cadenas A., Blumwald E., Mittler R.;
RT "Coordinating the overall stomatal response of plants: Rapid leaf-to-leaf
RT communication during light stress.";
RL Sci. Signal. 11:0-0(2018).
CC -!- FUNCTION: Slow, weak voltage-dependent S-type anion efflux channel
CC involved in maintenance of anion homeostasis. Cl(-) efflux through
CC SLAC1 causes membrane depolarization, which activates outward-
CC rectifying K1 channels, leading to KCl and water efflux to reduce
CC turgor further and cause stomatal closure, that reduces water loss and
CC promotes leaf turgor. Essential for stomatal closure in response to
CC CO(2), abscisic acid (ABA), ozone O(3), light/dark transitions,
CC humidity change, calcium ions, hydrogen peroxide H(2)O(2), reactive
CC oxygen species (ROS), and nitric oxide. Binds to the highly selective
CC inward-rectifying potassium channels KAT1 and AKT2, and inhibits their
CC activities. Functions as an essential negative regulator of inward
CC potassium channels in guard cells. Essential for the efficient stomatal
CC closure and opening in guard cells (PubMed:27002025). Involved in the
CC local and/or systemic stomatal responses (e.g. stomatal closure) to
CC light stress (PubMed:29463779). {ECO:0000269|PubMed:18084014,
CC ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:18305484,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:20128877, ECO:0000269|PubMed:20345603,
CC ECO:0000269|PubMed:27002025, ECO:0000269|PubMed:29463779,
CC ECO:0000269|Ref.4}.
CC -!- ACTIVITY REGULATION: Activated by GHR1-mediated phosphorylation which
CC is negatively regulated by ABI2 but not ABI1 (PubMed:22730405).
CC Activation by SRK2E/OST1 and GHR1 is repressed by HT1
CC (PubMed:27694184). {ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:27694184}.
CC -!- SUBUNIT: Homotrimer. Interacts with SRK2E, CPK6, CPK21, CPK23 and
CC PP2CA. The channel is inactivated upon PP2CA and ABI1 binding.
CC Interacts with KAT1, KAT2, KAT3/KC1 and AKT2 (PubMed:27002025).
CC Interacts with GHR1 (PubMed:22730405, PubMed:30361234).
CC {ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:20385816, ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:27002025, ECO:0000269|PubMed:30361234,
CC ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC Q9LD83; Q9ZSA2: CPK21; NbExp=2; IntAct=EBI-11174918, EBI-8519603;
CC Q9LD83; Q9M101: CPK23; NbExp=4; IntAct=EBI-11174918, EBI-15847592;
CC Q9LD83; Q940H6: SRK2E; NbExp=8; IntAct=EBI-11174918, EBI-782514;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305482,
CC ECO:0000269|PubMed:18305484, ECO:0000269|PubMed:19955405,
CC ECO:0000269|PubMed:19955427}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:18305484,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in guard cells. Also
CC detected in the vascular strands close to the leaf margins.
CC {ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:18305484,
CC ECO:0000269|PubMed:19955405}.
CC -!- INDUCTION: By drought stress in guard cells.
CC {ECO:0000269|PubMed:27002025}.
CC -!- PTM: Phosphorylation by SRK2E, especially on Ser-120, activates the
CC channel. Also phosphorylated and activated by CPK21 and CPK23. Abscisic
CC acid (ABA) promotes phosphorylation. This phosphorylation is inhibited
CC by ABI1. Phosphorylated and activated by GHR1; this phosphorylation is
CC repressed by ABI2 but not ABI1 (PubMed:22730405). Phosphorylated by HT1
CC on N-terminus but not C-terminus (PubMed:27694184).
CC {ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:20128877,
CC ECO:0000269|PubMed:20385816, ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:27694184}.
CC -!- DISRUPTION PHENOTYPE: Constitutively higher stomatal conductance with
CC over-accumulation of the osmoregulatory anions in guard cell. Impaired
CC slow (S-type) anion channel currents that are activated by cytosolic
CC calcium ions and abscisic acid (ABA) (normally leading to a decrease in
CC stomatal conductance). Higher sensitivity to ozone. Increased water
CC loss associated with a constitutive stomatal opening phenotype. Reduced
CC circadian leaf turgor changes. {ECO:0000269|PubMed:18084014,
CC ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:18305484,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:20128877,
CC ECO:0000269|PubMed:20345603, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the SLAC1 S-type anion channel family.
CC {ECO:0000305}.
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DR EMBL; AC025416; AAF79652.1; -; Genomic_DNA.
DR EMBL; AC025417; AAF88102.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28888.1; -; Genomic_DNA.
DR EMBL; AF424557; AAL11551.1; -; mRNA.
DR EMBL; BT002640; AAO11556.1; -; mRNA.
DR RefSeq; NP_563909.1; NM_101120.3.
DR PDB; 7WNQ; EM; 2.70 A; A/B/C=1-556.
DR PDBsum; 7WNQ; -.
DR AlphaFoldDB; Q9LD83; -.
DR SMR; Q9LD83; -.
DR BioGRID; 23045; 6.
DR DIP; DIP-49025N; -.
DR IntAct; Q9LD83; 8.
DR STRING; 3702.AT1G12480.1; -.
DR TCDB; 2.A.16.5.1; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR iPTMnet; Q9LD83; -.
DR PaxDb; Q9LD83; -.
DR PRIDE; Q9LD83; -.
DR ProteomicsDB; 232621; -.
DR EnsemblPlants; AT1G12480.1; AT1G12480.1; AT1G12480.
DR GeneID; 837805; -.
DR Gramene; AT1G12480.1; AT1G12480.1; AT1G12480.
DR KEGG; ath:AT1G12480; -.
DR Araport; AT1G12480; -.
DR TAIR; locus:2034700; AT1G12480.
DR eggNOG; ENOG502QQKN; Eukaryota.
DR HOGENOM; CLU_017679_3_0_1; -.
DR InParanoid; Q9LD83; -.
DR OMA; WCVFMAP; -.
DR OrthoDB; 450944at2759; -.
DR PhylomeDB; Q9LD83; -.
DR PRO; PR:Q9LD83; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LD83; baseline and differential.
DR Genevisible; Q9LD83; AT.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008509; F:anion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006820; P:anion transport; IMP:TAIR.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:TAIR.
DR GO; GO:0015698; P:inorganic anion transport; IDA:UniProtKB.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:TAIR.
DR GO; GO:0015711; P:organic anion transport; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0010037; P:response to carbon dioxide; IMP:TAIR.
DR GO; GO:0009270; P:response to humidity; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR GO; GO:0010193; P:response to ozone; IMP:TAIR.
DR GO; GO:0090332; P:stomatal closure; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR Gene3D; 1.50.10.150; -; 1.
DR InterPro; IPR030183; SLAC/SLAH.
DR InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR PANTHER; PTHR31269; PTHR31269; 1.
DR Pfam; PF03595; SLAC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Cell membrane; Coiled coil;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..556
FT /note="Guard cell S-type anion channel SLAC1"
FT /id="PRO_0000404259"
FT TOPO_DOM 1..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..295
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..352
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..418
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 441..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..479
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..36
FT /evidence="ECO:0000255"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 450
FT /note="Important for channel gating"
FT MOD_RES 59
FT /note="Phosphoserine; by SRK2E"
FT /evidence="ECO:0000269|PubMed:20128877"
FT MOD_RES 86
FT /note="Phosphoserine; by SRK2E"
FT /evidence="ECO:0000269|PubMed:20128877"
FT MOD_RES 113
FT /note="Phosphoserine; by SRK2E"
FT /evidence="ECO:0000269|PubMed:20128877"
FT MOD_RES 120
FT /note="Phosphoserine; by SRK2E"
FT /evidence="ECO:0000269|PubMed:20128877"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20128877"
FT MUTAGEN 38
FT /note="S->F: In slac1-6; normal ozone-triggered rapid
FT transient decrease (RTD) in stomatal conductance."
FT MUTAGEN 120
FT /note="S->F: In slac1-7; impaired ozonetriggered rapid
FT transient decrease (RTD) in stomatal conductance."
FT /evidence="ECO:0000269|PubMed:20128877"
FT MUTAGEN 146
FT /note="S->F: In slac1-8; impaired ozone-triggered rapid
FT transient decrease (RTD) in stomatal conductance."
FT /evidence="ECO:0000269|PubMed:20128877"
FT MUTAGEN 194
FT /note="G->D: In slac1-2; impaired anion transport activity,
FT strong insensitivity to abscisic acid (ABA), altered CO(2)-
FT dependent leaf temperature change and stomatal closure,
FT reduced sensitivity to darkness, and defective regulation
FT of transpiration in response to drought stress. Impaired
FT anion transport activity; when associated with A-450."
FT /evidence="ECO:0000269|PubMed:18305482,
FT ECO:0000269|PubMed:19955405, ECO:0000269|Ref.11"
FT MUTAGEN 450
FT /note="F->A: Enhanced and constitutive anion transport
FT activity. Impaired anion transport activity; when
FT associated with D-194."
FT /evidence="ECO:0000269|Ref.11"
FT MUTAGEN 450
FT /note="F->G,T: Enhanced and constitutive anion transport
FT activity."
FT /evidence="ECO:0000269|Ref.11"
FT MUTAGEN 450
FT /note="F->L,V: Impaired anion transport activity."
FT /evidence="ECO:0000269|Ref.11"
FT MUTAGEN 456
FT /note="S->F: In slac1-1; reduced slow (S-type) anion
FT channel currents, and increased water loss due to impaired
FT stomatal closure."
FT /evidence="ECO:0000269|PubMed:18305484, ECO:0000269|Ref.11"
SQ SEQUENCE 556 AA; 63235 MW; E2E310F026EE0C01 CRC64;
MERKQSNAHS TFADINEVED EAEQELQQQE NNNNKRFSGN RGPNRGKQRP FRGFSRQVSL
ETGFSVLNRE SRERDDKKSL PRSGRSFGGF ESGGIINGGD GRKTDFSMFR TKSTLSKQKS
LLPSIIRERD IENSLRTEDG ETKDDSINEN VSAGRYFAAL RGPELDEVKD NEDILLPKEE
QWPFLLRFPI GCFGICLGLS SQAVLWLALA KSPATNFLHI TPLINLVVWL FSLVVLVSVS
FTYILKCIFY FEAVKREYFH PVRVNFFFAP WVVCMFLAIS VPPMFSPNRK YLHPAIWCVF
MGPYFFLELK IYGQWLSGGK RRLCKVANPS SHLSVVGNFV GAILASKVGW DEVAKFLWAV
GFAHYLVVFV TLYQRLPTSE ALPKELHPVY SMFIAAPSAA SIAWNTIYGQ FDGCSRTCFF
IALFLYISLV ARINFFTGFK FSVAWWSYTF PMTTASVATI KYAEAVPGYP SRALALTLSF
ISTAMVCVLF VSTLLHAFVW QTLFPNDLAI AITKRKLTRE KKPFKRAYDL KRWTKQALAK
KISAEKDFEA EEESHH
