ZIFL1_ARATH
ID ZIFL1_ARATH Reviewed; 478 AA.
AC Q94BZ1; C0Z283; Q2V381; Q56WZ9; Q8LC71; Q9FKI7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein ZINC INDUCED FACILITATOR-LIKE 1;
DE AltName: Full=Protein ZIF-LIKE 1;
GN Name=ZIFL1; OrderedLocusNames=At5g13750; ORFNames=MXE10.2;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(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] (ISOFORM 1).
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] (ISOFORM 4).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-478.
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 DISRUPTION PHENOTYPE.
RX PubMed=17277087; DOI=10.1104/pp.106.092015;
RA Haydon M.J., Cobbett C.S.;
RT "A novel major facilitator superfamily protein at the tonoplast influences
RT zinc tolerance and accumulation in Arabidopsis.";
RL Plant Physiol. 143:1705-1719(2007).
RN [8]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19440702; DOI=10.1007/s00253-009-2025-5;
RA Cabrito T.R., Teixeira M.C., Duarte A.A., Duque P., Sa-Correia I.;
RT "Heterologous expression of a Tpo1 homolog from Arabidopsis thaliana
RT confers resistance to the herbicide 2,4-D and other chemical stresses in
RT yeast.";
RL Appl. Microbiol. Biotechnol. 84:927-936(2009).
RN [9]
RP FUNCTION (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3),
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23524662; DOI=10.1105/tpc.113.110353;
RA Remy E., Cabrito T.R., Baster P., Batista R.A., Teixeira M.C., Friml J.,
RA Sa-Correia I., Duque P.;
RT "A major facilitator superfamily transporter plays a dual role in polar
RT auxin transport and drought stress tolerance in Arabidopsis.";
RL Plant Cell 25:901-926(2013).
CC -!- FUNCTION: Major facilitator superfamily (MFS) transporter probably
CC involved in 2,4-dichlorophenoxyacetic acid (2,4-D) export
CC (PubMed:19440702). K(+) may be the physiological substrate of the
CC transporter (PubMed:23524662). {ECO:0000269|PubMed:19440702,
CC ECO:0000269|PubMed:23524662}.
CC -!- FUNCTION: [Isoform 1]: Modulates root auxin-related processes. Involved
CC in auxin efflux and acts as a positive regulator of shootward transport
CC at the root apex. May mediate proton efflux from the vacuolar
CC compartment. {ECO:0000269|PubMed:23524662}.
CC -!- FUNCTION: [Isoform 3]: Mediates drought stress tolerance by regulating
CC stomatal closure. {ECO:0000269|PubMed:23524662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19440702};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19440702}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Vacuole membrane
CC {ECO:0000269|PubMed:23524662}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC {ECO:0000269|PubMed:23524662}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q94BZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94BZ1-2; Sequence=VSP_039992;
CC Name=3;
CC IsoId=Q94BZ1-3; Sequence=VSP_039995, VSP_039996;
CC Name=4;
CC IsoId=Q94BZ1-4; Sequence=VSP_039993, VSP_039994;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots and stomatal guard
CC cells. Detected in anther stamen filaments and shoot apical meristem.
CC In the mature portion of roots, restricted to the cortex. At the root
CC tip, highly expressed in both the cortical and epidermal cell layers of
CC the apical meristem and the transition zone, while absent from the
CC quiescent center or the columella cells. Not detected in lateral root
CC primordia. {ECO:0000269|PubMed:23524662}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:23524662}.
CC -!- INDUCTION: By 2,4-D treatment. {ECO:0000269|PubMed:19440702}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions (PubMed:23524662). No visible phenotype when grown in
CC presence of zinc (PubMed:17277087). Hypersensitivity to drought stress
CC and auxin-related defects (PubMed:23524662).
CC {ECO:0000269|PubMed:17277087, ECO:0000269|PubMed:23524662}.
CC -!- MISCELLANEOUS: Heterologous expression of ZIFL1 in yeast leads to
CC increased resistance to 2,4-dichlorophenoxyacetic acid (2,4-D), indole-
CC 3-acetic acid (IAA), aluminum and thallium. Not involved in zinc stress
CC resistance.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10596.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94202.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011484; BAB10596.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91935.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91936.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91937.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68710.1; -; Genomic_DNA.
DR EMBL; AY039542; AAK62597.1; -; mRNA.
DR EMBL; AY062867; AAL32945.1; -; mRNA.
DR EMBL; AY102150; AAM26717.1; -; mRNA.
DR EMBL; AK318697; BAH56812.1; -; mRNA.
DR EMBL; AY086758; AAM63809.1; -; mRNA.
DR EMBL; AK221880; BAD94202.1; ALT_INIT; mRNA.
DR RefSeq; NP_001031877.1; NM_001036800.2. [Q94BZ1-3]
DR RefSeq; NP_001318556.1; NM_001343292.1. [Q94BZ1-3]
DR RefSeq; NP_568290.3; NM_121378.5. [Q94BZ1-2]
DR RefSeq; NP_851036.1; NM_180705.3. [Q94BZ1-1]
DR AlphaFoldDB; Q94BZ1; -.
DR SMR; Q94BZ1; -.
DR STRING; 3702.AT5G13750.1; -.
DR TCDB; 2.A.1.2.111; the major facilitator superfamily (mfs).
DR PaxDb; Q94BZ1; -.
DR PRIDE; Q94BZ1; -.
DR ProteomicsDB; 232332; -. [Q94BZ1-1]
DR EnsemblPlants; AT5G13750.1; AT5G13750.1; AT5G13750. [Q94BZ1-1]
DR EnsemblPlants; AT5G13750.2; AT5G13750.2; AT5G13750. [Q94BZ1-2]
DR EnsemblPlants; AT5G13750.3; AT5G13750.3; AT5G13750. [Q94BZ1-3]
DR EnsemblPlants; AT5G13750.4; AT5G13750.4; AT5G13750. [Q94BZ1-3]
DR GeneID; 831220; -.
DR Gramene; AT5G13750.1; AT5G13750.1; AT5G13750. [Q94BZ1-1]
DR Gramene; AT5G13750.2; AT5G13750.2; AT5G13750. [Q94BZ1-2]
DR Gramene; AT5G13750.3; AT5G13750.3; AT5G13750. [Q94BZ1-3]
DR Gramene; AT5G13750.4; AT5G13750.4; AT5G13750. [Q94BZ1-3]
DR KEGG; ath:AT5G13750; -.
DR Araport; AT5G13750; -.
DR TAIR; locus:2177105; AT5G13750.
DR eggNOG; KOG2615; Eukaryota.
DR InParanoid; Q94BZ1; -.
DR OMA; LAICRFA; -.
DR PhylomeDB; Q94BZ1; -.
DR PRO; PR:Q94BZ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BZ1; baseline and differential.
DR Genevisible; Q94BZ1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0022821; F:potassium ion antiporter activity; IGI:TAIR.
DR GO; GO:0010540; P:basipetal auxin transport; IDA:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..478
FT /note="Protein ZINC INDUCED FACILITATOR-LIKE 1"
FT /id="PRO_0000400081"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_039992"
FT VAR_SEQ 390..392
FT /note="TSA -> VSF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039993"
FT VAR_SEQ 393..478
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039994"
FT VAR_SEQ 405..411
FT /note="RQDQRGA -> TRPKRSS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039995"
FT VAR_SEQ 412..478
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039996"
FT CONFLICT 373
FT /note="A -> V (in Ref. 5; AAM63809)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> I (in Ref. 4; BAH56812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52299 MW; 1E64D8D31150FF7F CRC64;
MAEEYAECLL EKNFHEDCSG CKVDQMKRLR RGFPFWELFT VWIIVLCTAL PISSLFPFLY
FMIDDFNIAK KEEDIGFYAG FVGCSFMLGR AFTSVAWGLV ADRYGRKPVI LIGTASVVVF
NTLFGLSLNF WMAIITRFCL GSFNGLLGPI KAYAMEIFRD EYQGLALSAV STAWGIGLII
GPAIGGFLAQ PAKQYPSLFS QDSIFGKFPF FLPCLAISVF AFLVTIVSSR IPETLHNHKF
NDDESYDALK DLSDDPESNK VAERNGKSSL LNNWPLISSI IVYCVFSLHD MAYTEIFSLW
ANSPRKYGGL GYSTADVGSV LAFSGFGLLI FQLSLYSYAE RLLGPIIVTR ISGSLAMVVL
SCYPLIAKLS GLALTVTVTS ASVAKSVLGT SAITGLFILQ NKAVRQDQRG AANGIAMTAM
SLFKAIGPAA AGIIFSWSEK RQGAAFLPGT QMVFFILNVV LALGVVLTFK PFLAETQQ
