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Protein ZINC INDUCED FACILITATOR-LIKE 1 (Protein ZIF-LIKE 1)

 ZIFL1_ARATH             Reviewed;         478 AA.
Q94BZ1; C0Z283; Q2V381; Q56WZ9; Q8LC71; Q9FKI7;
02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 107.
RecName: Full=Protein ZINC INDUCED FACILITATOR-LIKE 1;
AltName: Full=Protein ZIF-LIKE 1;
Name=ZIFL1; OrderedLocusNames=At5g13750; ORFNames=MXE10.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-478.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
DISRUPTION PHENOTYPE.
PubMed=17277087; DOI=10.1104/pp.106.092015;
Haydon M.J., Cobbett C.S.;
"A novel major facilitator superfamily protein at the tonoplast
influences zinc tolerance and accumulation in Arabidopsis.";
Plant Physiol. 143:1705-1719(2007).
[8]
FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=19440702; DOI=10.1007/s00253-009-2025-5;
Cabrito T.R., Teixeira M.C., Duarte A.A., Duque P., Sa-Correia I.;
"Heterologous expression of a Tpo1 homolog from Arabidopsis thaliana
confers resistance to the herbicide 2,4-D and other chemical stresses
in yeast.";
Appl. Microbiol. Biotechnol. 84:927-936(2009).
[9]
FUNCTION (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3),
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=23524662; DOI=10.1105/tpc.113.110353;
Remy E., Cabrito T.R., Baster P., Batista R.A., Teixeira M.C.,
Friml J., Sa-Correia I., Duque P.;
"A major facilitator superfamily transporter plays a dual role in
polar auxin transport and drought stress tolerance in Arabidopsis.";
Plant Cell 25:901-926(2013).
-!- FUNCTION: Major facilitator superfamily (MFS) transporter probably
involved in 2,4-dichlorophenoxyacetic acid (2,4-D) export
(PubMed:19440702). K(+) may be the physiological substrate of the
transporter (PubMed:23524662). {ECO:0000269|PubMed:19440702,
ECO:0000269|PubMed:23524662}.
-!- FUNCTION: Isoform 1: Modulates root auxin-related processes.
Involved in auxin efflux and acts as a positive regulator of
shootward transport at the root apex. May mediate proton efflux
from the vacuolar compartment. {ECO:0000269|PubMed:23524662}.
-!- FUNCTION: Isoform 3: Mediates drought stress tolerance by
regulating stomatal closure. {ECO:0000269|PubMed:23524662}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19440702};
Multi-pass membrane protein {ECO:0000269|PubMed:19440702}.
-!- SUBCELLULAR LOCATION: Isoform 1: Vacuole membrane
{ECO:0000269|PubMed:23524662}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane
{ECO:0000269|PubMed:23524662}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q94BZ1-1; Sequence=Displayed;
Name=2;
IsoId=Q94BZ1-2; Sequence=VSP_039992;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q94BZ1-3; Sequence=VSP_039995, VSP_039996;
Note=Derived from EST data. No experimental confirmation
available.;
Name=4;
IsoId=Q94BZ1-4; Sequence=VSP_039993, VSP_039994;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in roots and stomatal
guard cells. Detected in anther stamen filaments and shoot apical
meristem. In the mature portion of roots, restricted to the
cortex. At the root tip, highly expressed in both the cortical and
epidermal cell layers of the apical meristem and the transition
zone, while absent from the quiescent center or the columella
cells. Not detected in lateral root primordia.
{ECO:0000269|PubMed:23524662}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development.
{ECO:0000269|PubMed:23524662}.
-!- INDUCTION: By 2,4-D treatment. {ECO:0000269|PubMed:19440702}.
-!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
conditions (PubMed:23524662). No visible phenotype when grown in
presence of zinc (PubMed:17277087). Hypersensitivity to drought
stress and auxin-related defects (PubMed:23524662).
{ECO:0000269|PubMed:17277087, ECO:0000269|PubMed:23524662}.
-!- MISCELLANEOUS: Heterologous expression of ZIFL1 in yeast leads to
increased resistance to 2,4-dichlorophenoxyacetic acid (2,4-D),
indole-3-acetic acid (IAA), aluminum and thallium. Not involved in
zinc stress resistance.
-!- SIMILARITY: Belongs to the major facilitator superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB10596.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAD94202.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB011484; BAB10596.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED91935.1; -; Genomic_DNA.
EMBL; CP002688; AED91936.1; -; Genomic_DNA.
EMBL; CP002688; AED91937.1; -; Genomic_DNA.
EMBL; CP002688; ANM68710.1; -; Genomic_DNA.
EMBL; AY039542; AAK62597.1; -; mRNA.
EMBL; AY062867; AAL32945.1; -; mRNA.
EMBL; AY102150; AAM26717.1; -; mRNA.
EMBL; AK318697; BAH56812.1; -; mRNA.
EMBL; AY086758; AAM63809.1; -; mRNA.
EMBL; AK221880; BAD94202.1; ALT_INIT; mRNA.
RefSeq; NP_001031877.1; NM_001036800.2. [Q94BZ1-3]
RefSeq; NP_001318556.1; NM_001343292.1. [Q94BZ1-3]
RefSeq; NP_568290.3; NM_121378.5. [Q94BZ1-2]
RefSeq; NP_851036.1; NM_180705.3. [Q94BZ1-1]
UniGene; At.19822; -.
ProteinModelPortal; Q94BZ1; -.
STRING; 3702.AT5G13750.1; -.
PaxDb; Q94BZ1; -.
PRIDE; Q94BZ1; -.
EnsemblPlants; AT5G13750.1; AT5G13750.1; AT5G13750. [Q94BZ1-1]
EnsemblPlants; AT5G13750.2; AT5G13750.2; AT5G13750. [Q94BZ1-2]
EnsemblPlants; AT5G13750.3; AT5G13750.3; AT5G13750. [Q94BZ1-3]
EnsemblPlants; AT5G13750.4; AT5G13750.4; AT5G13750. [Q94BZ1-3]
GeneID; 831220; -.
Gramene; AT5G13750.1; AT5G13750.1; AT5G13750. [Q94BZ1-1]
Gramene; AT5G13750.2; AT5G13750.2; AT5G13750. [Q94BZ1-2]
Gramene; AT5G13750.3; AT5G13750.3; AT5G13750. [Q94BZ1-3]
Gramene; AT5G13750.4; AT5G13750.4; AT5G13750. [Q94BZ1-3]
KEGG; ath:AT5G13750; -.
Araport; AT5G13750; -.
TAIR; locus:2177105; AT5G13750.
eggNOG; KOG2615; Eukaryota.
eggNOG; ENOG410XSE0; LUCA.
HOGENOM; HOG000242165; -.
InParanoid; Q94BZ1; -.
OMA; HQPRAYT; -.
OrthoDB; EOG09360B22; -.
PhylomeDB; Q94BZ1; -.
PRO; PR:Q94BZ1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q94BZ1; baseline and differential.
Genevisible; Q94BZ1; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0022821; F:potassium ion antiporter activity; IGI:TAIR.
GO; GO:0010540; P:basipetal auxin transport; IDA:TAIR.
GO; GO:0009630; P:gravitropism; IMP:TAIR.
GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
CDD; cd06174; MFS; 1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
Pfam; PF07690; MFS_1; 1.
PRINTS; PR01035; TCRTETA.
SUPFAM; SSF103473; SSF103473; 1.
PROSITE; PS50850; MFS; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Vacuole.
CHAIN 1 478 Protein ZINC INDUCED FACILITATOR-LIKE 1.
/FTId=PRO_0000400081.
TRANSMEM 43 63 Helical. {ECO:0000255}.
TRANSMEM 81 101 Helical. {ECO:0000255}.
TRANSMEM 108 128 Helical. {ECO:0000255}.
TRANSMEM 130 150 Helical. {ECO:0000255}.
TRANSMEM 169 189 Helical. {ECO:0000255}.
TRANSMEM 208 228 Helical. {ECO:0000255}.
TRANSMEM 280 300 Helical. {ECO:0000255}.
TRANSMEM 317 337 Helical. {ECO:0000255}.
TRANSMEM 346 367 Helical. {ECO:0000255}.
TRANSMEM 378 398 Helical. {ECO:0000255}.
TRANSMEM 415 435 Helical. {ECO:0000255}.
TRANSMEM 453 473 Helical. {ECO:0000255}.
VAR_SEQ 1 86 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_039992.
VAR_SEQ 390 392 TSA -> VSF (in isoform 4).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_039993.
VAR_SEQ 393 478 Missing (in isoform 4).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_039994.
VAR_SEQ 405 411 RQDQRGA -> TRPKRSS (in isoform 3).
{ECO:0000305}.
/FTId=VSP_039995.
VAR_SEQ 412 478 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_039996.
CONFLICT 373 373 A -> V (in Ref. 5; AAM63809).
{ECO:0000305}.
CONFLICT 379 379 T -> I (in Ref. 4; BAH56812).
{ECO:0000305}.
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


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