SLAH1_ARATH
ID SLAH1_ARATH Reviewed; 385 AA.
AC Q5E930; O04592; Q84WB2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=S-type anion channel SLAH1;
DE AltName: Full=SLAC1-homolog protein 1;
GN Name=SLAH1; OrderedLocusNames=At1g62280; ORFNames=F19K23.20;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
CC -!- FUNCTION: Slow, weak voltage-dependent S-type anion efflux channel
CC involved in maintenance of anion homeostasis.
CC {ECO:0000269|PubMed:18305482}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305482};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18305482}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular systems of root.
CC {ECO:0000269|PubMed:18305482}.
CC -!- SIMILARITY: Belongs to the SLAC1 S-type anion channel family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC000375; AAB60772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33945.1; -; Genomic_DNA.
DR EMBL; BT004052; AAO42083.1; -; mRNA.
DR EMBL; BT021090; AAX12860.1; -; mRNA.
DR PIR; D96649; D96649.
DR RefSeq; NP_176418.2; NM_104908.4.
DR AlphaFoldDB; Q5E930; -.
DR SMR; Q5E930; -.
DR STRING; 3702.AT1G62280.1; -.
DR PaxDb; Q5E930; -.
DR PRIDE; Q5E930; -.
DR EnsemblPlants; AT1G62280.1; AT1G62280.1; AT1G62280.
DR GeneID; 842525; -.
DR Gramene; AT1G62280.1; AT1G62280.1; AT1G62280.
DR KEGG; ath:AT1G62280; -.
DR Araport; AT1G62280; -.
DR TAIR; locus:2018027; AT1G62280.
DR eggNOG; ENOG502QSGW; Eukaryota.
DR HOGENOM; CLU_044414_2_0_1; -.
DR InParanoid; Q5E930; -.
DR OMA; NECALCM; -.
DR OrthoDB; 947189at2759; -.
DR PhylomeDB; Q5E930; -.
DR PRO; PR:Q5E930; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5E930; baseline and differential.
DR Genevisible; Q5E930; 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; IEA:InterPro.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:TAIR.
DR GO; GO:0006821; P:chloride transport; IMP:TAIR.
DR GO; GO:1901529; P:positive regulation of anion channel activity; IDA: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 2: Evidence at transcript level;
KW Cell membrane; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..385
FT /note="S-type anion channel SLAH1"
FT /id="PRO_0000404260"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..81
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..150
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..207
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..330
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 366..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 215
FT /note="L -> I (in Ref. 3; AAO42083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43407 MW; C29F4BCC0AD81991 CRC64;
MEIPRQEIHI EIDNSIPSSK EFKTGLADAK PVVLMSALRS LHAGYFRISL SLCSQALLWK
IMIAPESPSM SHMHSKLPSM AFHLLWYLAL VTQVSLCFLY ALKCIFFFDK VKEEFLHYIG
VNYLYAPSIS WLLMLQSAPM MEPNSVLYQT LFWIFAVPVL TLDIKLYGQW FTTEKRFLSM
LANPASQVSV IANLVAARGA AEMGWNECAL CMFSLGMVHY LVIFVTLYQR LPGGNNFPAK
LRPIFFLFVA APAMASLAWN SICGTFDAVA KMLFFLSLFI FMSLVCRPNL FKKSMKRFNV
AWWAYSFPLT FLALDSVQYA QEVKDPVGSG LMLIFSSISV LIFLGMMVLT AANSNRLLRH
DPVLGSATDP KDKQKTLSLN ATNQN
