SLAH3_ARATH
ID SLAH3_ARATH Reviewed; 635 AA.
AC Q9FLV9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=S-type anion channel SLAH3;
DE AltName: Full=SLAC1-homolog protein 3;
GN Name=SLAH3; OrderedLocusNames=At5g24030; ORFNames=MZF18.9;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 [7]
RP FUNCTION, INTERACTION WITH KAT1, AND INDUCTION BY 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).
CC -!- FUNCTION: Slow, weak voltage-dependent S-type anion efflux channel
CC involved in maintenance of anion homeostasis (PubMed:18305482). Binds
CC to the highly selective inward-rectifying potassium channel KAT1 and
CC inhibits its activity. Functions as an essential negative regulator of
CC inward potassium channels in guard cells. Essential for the efficient
CC stomatal closure and opening in guard cells (PubMed:27002025).
CC {ECO:0000269|PubMed:18305482, ECO:0000269|PubMed:27002025}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with KAT1
CC (PubMed:27002025). {ECO:0000250, ECO:0000269|PubMed:27002025}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:18305482}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:18305482}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant, escpecially in
CC vascular systems. {ECO:0000269|PubMed:18305482}.
CC -!- INDUCTION: By drought stress in guard cells.
CC {ECO:0000269|PubMed:27002025}.
CC -!- SIMILARITY: Belongs to the SLAC1 S-type anion channel family.
CC {ECO:0000305}.
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DR EMBL; AB009056; BAB08726.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93247.1; -; Genomic_DNA.
DR EMBL; BT015364; AAU05487.1; -; mRNA.
DR EMBL; BT015721; AAU45219.1; -; mRNA.
DR RefSeq; NP_197791.1; NM_122308.5.
DR AlphaFoldDB; Q9FLV9; -.
DR SMR; Q9FLV9; -.
DR BioGRID; 17743; 3.
DR STRING; 3702.AT5G24030.1; -.
DR TCDB; 2.A.16.5.2; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR iPTMnet; Q9FLV9; -.
DR PaxDb; Q9FLV9; -.
DR PRIDE; Q9FLV9; -.
DR ProteomicsDB; 234571; -.
DR EnsemblPlants; AT5G24030.1; AT5G24030.1; AT5G24030.
DR GeneID; 832468; -.
DR Gramene; AT5G24030.1; AT5G24030.1; AT5G24030.
DR KEGG; ath:AT5G24030; -.
DR Araport; AT5G24030; -.
DR TAIR; locus:2178722; AT5G24030.
DR eggNOG; ENOG502QQKN; Eukaryota.
DR HOGENOM; CLU_017679_1_0_1; -.
DR InParanoid; Q9FLV9; -.
DR OMA; PTPLPHW; -.
DR OrthoDB; 450944at2759; -.
DR PhylomeDB; Q9FLV9; -.
DR PRO; PR:Q9FLV9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLV9; baseline and differential.
DR Genevisible; Q9FLV9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:TAIR.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:TAIR.
DR GO; GO:0006821; P:chloride transport; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP: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 Cell membrane; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..635
FT /note="S-type anion channel SLAH3"
FT /id="PRO_0000404262"
FT TOPO_DOM 1..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..299
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..358
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..419
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..541
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 102..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LD83"
SQ SEQUENCE 635 AA; 72339 MW; 3C3C59B25D860C35 CRC64;
MEEKPNYVIQ VEEELPTLLR KATTEEMVGF DNYKENGHPF PHSISRFHPS HASTTTLNGQ
ETSRSIDTME AHHHNYNETT PWTHQRKPSI SMPTSPNVLM ISDPTTSLSS ENHKNSGSTG
KSVKFLSQPM TKVSSLYIES GNGDDDRRQS HDNHHHHLHR QHQSGHHQNQ NQAANKLKDN
RYNSFKTWSG KLERQFTRKP ASVEPEAPNR NNQNLNTNEA MPVDRYYDAL EGPELETLRP
QEEIVLPNDK KWPFLLRYPI STFGMCLGVS SQAIMWKTLA TAEPTKFLHV PLWINQGLWF
ISVALILTIA TIYLLKIILF FEAVRREYYH PIRINFFFAP FISLLFLALG VPPSIITDLP
HFLWYLLMFP FICLELKIYG QWMSGGQRRL SRVANPTNHL SVVGNFVGAL LGASMGLREG
PIFFYAVGMA HYLVLFVTLY QRLPTNETLP KDLHPVFFLF VAAPSVASMA WAKVTGSFDY
GSKVCYFIAI FLYFSLAVRI NFFRGIKFSL SWWAYTFPMT GAAIATIRYA TVVKSTMTQI
MCVVLCAIAT LVVFALLVTT IIHAFVLRDL FPNDLAIAIS NRPRPKQNSQ HRWLDQLRNV
SSENIENYLK FTDSDSSQSN DVEACNGKTQ ESDSS
