CAX1_ARATH
ID CAX1_ARATH Reviewed; 463 AA.
AC Q39253; O80442; Q56WC8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Vacuolar cation/proton exchanger 1;
DE AltName: Full=Ca(2+)/H(+) antiporter CAX1;
DE AltName: Full=Ca(2+)/H(+) exchanger 1;
DE AltName: Full=Protein CATION EXCHANGER 1;
DE AltName: Full=Protein RARE COLD INDUCIBLE 4;
GN Name=CAX1; Synonyms=RCI4; OrderedLocusNames=At2g38170; ORFNames=F16M14.10;
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 [MRNA].
RX PubMed=11706183; DOI=10.1104/pp.010409;
RA Pittman J.K., Hirschi K.D.;
RT "Regulation of CAX1, an Arabidopsis Ca(2+)/H+ antiporter. Identification of
RT an N-terminal autoinhibitory domain.";
RL Plant Physiol. 127:1020-1029(2001).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-463.
RX PubMed=8710949; DOI=10.1073/pnas.93.16.8782;
RA Hirschi K.D., Zhen R.-G., Cunningham K.W., Rea P.A., Fink G.R.;
RT "CAX1, an H+/Ca2+ antiporter from Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8782-8786(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-463.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RX PubMed=10559438; DOI=10.2307/3871013;
RA Hirschi K.D.;
RT "Expression of Arabidopsis CAX1 in tobacco: altered calcium homeostasis and
RT increased stress sensitivity.";
RL Plant Cell 11:2113-2122(1999).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=11562366; DOI=10.1074/jbc.m106637200;
RA Shigaki T., Cheng N.-H., Pittman J.K., Hirschi K.D.;
RT "Structural determinants of Ca2+ transport in the Arabidopsis H+/Ca2+
RT antiporter CAX1.";
RL J. Biol. Chem. 276:43152-43159(2001).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [10]
RP MUTAGENESIS OF THR-6; SER-10; SER-24; SER-25; ARG-29; ARG-32 AND THR-33.
RX PubMed=12006570; DOI=10.1074/jbc.m202563200;
RA Pittman J.K., Shigaki T., Cheng N.-H., Hirschi K.D.;
RT "Mechanism of N-terminal autoinhibition in the Arabidopsis Ca(2+)/H(+)
RT antiporter CAX1.";
RL J. Biol. Chem. 277:26452-26459(2002).
RN [11]
RP ACTIVITY REGULATION, AND INTERACTION WITH GRXS14.
RX PubMed=12480930; DOI=10.1074/jbc.m210883200;
RA Cheng N.-H., Hirschi K.D.;
RT "Cloning and characterization of CXIP1 A novel PICOT domain-containing
RT Arabidopsis protein that associates with CAX1.";
RL J. Biol. Chem. 278:6503-6509(2003).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12566577; DOI=10.1105/tpc.007385;
RA Cheng N.-H., Pittman J.K., Barkla B.J., Shigaki T., Hirschi K.D.;
RT "The Arabidopsis cax1 mutant exhibits impaired ion homeostasis,
RT development, and hormonal responses and reveals interplay among vacuolar
RT transporters.";
RL Plant Cell 15:347-364(2003).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14630965; DOI=10.1105/tpc.015248;
RA Catala R., Santos E., Alonso J.M., Ecker J.R., Martinez-Zapater J.M.,
RA Salinas J.;
RT "Mutations in the Ca2+/H+ transporter CAX1 increase CBF/DREB1 expression
RT and the cold-acclimation response in Arabidopsis.";
RL Plant Cell 15:2940-2951(2003).
RN [14]
RP ACTIVITY REGULATION, AND INTERACTION WITH CXIP4.
RX PubMed=14960315; DOI=10.1016/s0014-5793(04)00036-5;
RA Cheng N.-H., Liu J.-Z., Nelson R.S., Hirschi K.D.;
RT "Characterization of CXIP4, a novel Arabidopsis protein that activates the
RT H+/Ca2+ antiporter, CAX1.";
RL FEBS Lett. 559:99-106(2004).
RN [15]
RP BIOTECHNOLOGY.
RX PubMed=15998121; DOI=10.1021/jf050531c;
RA Park S., Kang T.S., Kim C.K., Han J.S., Kim S., Smith R.H., Pike L.M.,
RA Hirschi K.D.;
RT "Genetic manipulation for enhancing calcium content in potato tuber.";
RL J. Agric. Food Chem. 53:5598-5603(2005).
RN [16]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15862304; DOI=10.1016/j.febslet.2005.03.085;
RA Pittman J.K., Shigaki T., Hirschi K.D.;
RT "Evidence of differential pH regulation of the Arabidopsis vacuolar Ca2+/H+
RT antiporters CAX1 and CAX2.";
RL FEBS Lett. 579:2648-2656(2005).
RN [17]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-259; HIS-338;
RP HIS-412; HIS-443 AND HIS-446.
RX PubMed=15994298; DOI=10.1074/jbc.m503610200;
RA Shigaki T., Barkla B.J., Miranda-Vergara M.C., Zhao J., Pantoja O.,
RA Hirschi K.D.;
RT "Identification of a crucial histidine involved in metal transport activity
RT in the Arabidopsis cation/H+ exchanger CAX1.";
RL J. Biol. Chem. 280:30136-30142(2005).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16055687; DOI=10.1104/pp.105.061218;
RA Cheng N.-H., Pittman J.K., Shigaki T., Lachmansingh J., LeClere S.,
RA Lahner B., Salt D.E., Hirschi K.D.;
RT "Functional association of Arabidopsis CAX1 and CAX3 is required for normal
RT growth and ion homeostasis.";
RL Plant Physiol. 138:2048-2060(2005).
RN [19]
RP ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RX PubMed=16244156; DOI=10.1104/pp.105.066266;
RA Park S., Cheng N.-H., Pittman J.K., Yoo K.S., Park J., Smith R.H.,
RA Hirschi K.D.;
RT "Increased calcium levels and prolonged shelf life in tomatoes expressing
RT Arabidopsis H+/Ca2+ transporters.";
RL Plant Physiol. 139:1194-1206(2005).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+)
CC and other metal ions into vacuoles using the proton gradient formed by
CC H(+)-ATPase and H(+)-pyrophosphatase. Involved in ion homeostasis in
CC association with CAX3. May play a role in cold-acclimation response.
CC {ECO:0000269|PubMed:12566577, ECO:0000269|PubMed:14630965,
CC ECO:0000269|PubMed:16055687}.
CC -!- ACTIVITY REGULATION: Activated by monothiol glutaredoxin GRXS14 and
CC CXIP4. Inhibited by excess of Ca(2+) and Cd(2+), Na(+) and K(+), but
CC not Mn(2+). {ECO:0000269|PubMed:11562366, ECO:0000269|PubMed:12480930,
CC ECO:0000269|PubMed:14960315, ECO:0000269|PubMed:16244156}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for Cd(2+) {ECO:0000269|PubMed:15862304,
CC ECO:0000269|PubMed:15994298};
CC KM=225 uM for Zn(2+) {ECO:0000269|PubMed:15862304,
CC ECO:0000269|PubMed:15994298};
CC Note=Measured in vacuolar yeast membrane vesicles with a shorter CAX1
CC starting at Met-37.;
CC pH dependence:
CC Optimum pH is 7.5 for cytosolic pH. {ECO:0000269|PubMed:15862304,
CC ECO:0000269|PubMed:15994298};
CC -!- SUBUNIT: Interacts with GRXS14 and CXIP4. {ECO:0000269|PubMed:12480930,
CC ECO:0000269|PubMed:14960315}.
CC -!- INTERACTION:
CC Q39253; Q93Z81: CAX3; NbExp=4; IntAct=EBI-2292388, EBI-2292420;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:12566577};
CC Multi-pass membrane protein {ECO:0000305|PubMed:12566577}.
CC Note=Tonoplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q39253-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q39253-2; Sequence=VSP_022343;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, stems and
CC flowers. {ECO:0000269|PubMed:14630965}.
CC -!- INDUCTION: By cold in leaves. Highly induced by Ca(2+) and at low
CC levels by Na(+) and Ni(2+). {ECO:0000269|PubMed:10559438,
CC ECO:0000269|PubMed:14630965}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit a 50% reduction in tonoplast
CC Ca(2+)/H(+) exchange activity, a 40% reduction in tonoplast V-type
CC H(+)-translocating ATPase activity, a 36% increase in tonoplast Ca(2+)-
CC ATPase activity and an increased expression of CAX3 and CAX4. These
CC plants exhibit altered plant development, perturbed hormone
CC sensitivities, altered auxin signaling response, lower sensitivity to
CC other metal ions and increased freezing tolerance after cold
CC acclimation. {ECO:0000269|PubMed:16055687}.
CC -!- BIOTECHNOLOGY: CAX1 expression in tomato increases calcium content and
CC prolonges shelf life and may serve as an alternative to the application
CC of CaCl(2) used to extend shelf life in numerous agricultural
CC commodities. Expression in potato tubers increases calcium content by
CC 3-fold without the adverse effect of increasing other metal ion
CC contents. {ECO:0000269|PubMed:15998121, ECO:0000269|PubMed:16244156}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. Cation/proton exchanger (CAX) subfamily. {ECO:0000305}.
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DR EMBL; AF461691; AAL66749.1; -; mRNA.
DR EMBL; AC003028; AAC27166.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09499.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09501.1; -; Genomic_DNA.
DR EMBL; AF372938; AAK50078.1; -; mRNA.
DR EMBL; U57411; AAB05913.2; -; mRNA.
DR EMBL; AK222114; BAD95074.1; -; mRNA.
DR PIR; T01249; T01249.
DR RefSeq; NP_181352.1; NM_129373.4. [Q39253-1]
DR RefSeq; NP_973630.1; NM_201901.4. [Q39253-2]
DR AlphaFoldDB; Q39253; -.
DR SMR; Q39253; -.
DR BioGRID; 3739; 6.
DR ComplexPortal; CPX-1326; CAX1-CAX3 complex.
DR ComplexPortal; CPX-1428; CAX1 homodimer.
DR IntAct; Q39253; 1.
DR STRING; 3702.AT2G38170.3; -.
DR TCDB; 2.A.19.2.3; the ca(2+):cation antiporter (caca) family.
DR iPTMnet; Q39253; -.
DR PaxDb; Q39253; -.
DR PRIDE; Q39253; -.
DR ProteomicsDB; 223870; -. [Q39253-1]
DR EnsemblPlants; AT2G38170.1; AT2G38170.1; AT2G38170. [Q39253-1]
DR EnsemblPlants; AT2G38170.3; AT2G38170.3; AT2G38170. [Q39253-2]
DR GeneID; 818395; -.
DR Gramene; AT2G38170.1; AT2G38170.1; AT2G38170. [Q39253-1]
DR Gramene; AT2G38170.3; AT2G38170.3; AT2G38170. [Q39253-2]
DR KEGG; ath:AT2G38170; -.
DR Araport; AT2G38170; -.
DR TAIR; locus:2042852; AT2G38170.
DR eggNOG; KOG1397; Eukaryota.
DR HOGENOM; CLU_008721_4_2_1; -.
DR InParanoid; Q39253; -.
DR OMA; EMNTEPC; -.
DR PhylomeDB; Q39253; -.
DR SABIO-RK; Q39253; -.
DR PRO; PR:Q39253; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q39253; baseline and differential.
DR Genevisible; Q39253; AT.
DR GO; GO:0061993; C:calcium:proton antiporter complex; IPI:ComplexPortal.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:ComplexPortal.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IDA:TAIR.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:TAIR.
DR GO; GO:0006812; P:cation transport; IMP:ComplexPortal.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:ComplexPortal.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:TAIR.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:TAIR.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0010351; P:lithium ion transport; IMP:ComplexPortal.
DR GO; GO:0055062; P:phosphate ion homeostasis; IGI:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:ComplexPortal.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004713; CaH_exchang.
DR InterPro; IPR004798; CAX-like.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR PANTHER; PTHR31503; PTHR31503; 1.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR TIGRFAMs; TIGR00378; cax; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Antiport; Calcium; Calcium transport;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..463
FT /note="Vacuolar cation/proton exchanger 1"
FT /id="PRO_0000270150"
FT TOPO_DOM 2..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..463
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 25..33
FT /note="Required for autoinhibitory regulation"
FT REGION 56..62
FT /note="Required for interaction with autoinhibitory region"
FT REGION 87..95
FT /note="Required for Ca(2+)/H(+) exchange activity"
FT REGION 137..172
FT /note="Cation selection"
FT /evidence="ECO:0000255"
FT REGION 333..368
FT /note="Cation selection"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 438..463
FT /note="KQNAIHLGHQAMNNVVTATGGGVFSS -> SELVFKCICMLLLGKTIIEAYN
FT THISNGNASSNKVKTG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022343"
FT MUTAGEN 6
FT /note="T->A: No effect on autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 10
FT /note="S->A: No effect on autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 24
FT /note="S->A: No effect on autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 25
FT /note="S->A: No effect on autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 25
FT /note="S->D: Loss of autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 25
FT /note="S->T: No effect on autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 29
FT /note="R->A: Loss of autoinhibitory regulation; when
FT associated with A-32."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 32
FT /note="R->A: Loss of autoinhibitory regulation; when
FT associated with A-29."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 33
FT /note="T->A: Loss of autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 33
FT /note="T->D: Loss of autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 33
FT /note="T->E: Loss of autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 33
FT /note="T->S: Loss of autoinhibitory regulation."
FT /evidence="ECO:0000269|PubMed:12006570"
FT MUTAGEN 259
FT /note="H->A: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 338
FT /note="H->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 338
FT /note="H->K: Reduced transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 338
FT /note="H->N: Increased affinity for Cd(2+) and Zn(2+)
FT transport."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 338
FT /note="H->Q: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 412
FT /note="H->A: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 443
FT /note="H->A: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT MUTAGEN 446
FT /note="H->A: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15994298"
FT CONFLICT 374
FT /note="I -> T (in Ref. 5; AAB05913)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="A -> V (in Ref. 5; AAB05913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50177 MW; C7502A62AA51DF0A CRC64;
MAGIVTEPWS VAENGNPSIT AKGSSRELRL GRTAHNMSSS SLRKKSDLRV IQKVPYKGLK
DFLSNLQEVI LGTKLAILFP AIPAAIICTY CGVSQPWIFG LSLLGLTPLA ERVSFLTEQL
AFYTGPTLGG LLNATCGNAT ELIIAILALT NNKVAVVKYS LLGSILSNLL LVLGTSLFCG
GIANIRREQR FDRKQADVNF FLLLLGFLCH LLPLLVGYLK NGEASAAVLS DMQLSISRGF
SIVMLISYIA YLVFQLWTHR QLFDAQEQED EYDDDVEQET AVISFWSGFA WLVGMTLVIA
LLSEYVVATI EEASDKWNLS VSFISIILLP IVGNAAEHAG AVIFAFKNKL DISLGVALGS
ATQIGLFVVP LTIIVAWILG INMDLNFGPL ETGCLAVSII ITAFTLQDGS SHYMKGLVLL
LCYFIIAICF FVDKLPQKQN AIHLGHQAMN NVVTATGGGV FSS
