ZIP2_ARATH
ID ZIP2_ARATH Reviewed; 353 AA.
AC Q9LTH9; O81124;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Zinc transporter 2;
DE AltName: Full=ZRT/IRT-like protein 2;
DE Flags: Precursor;
GN Name=ZIP2; OrderedLocusNames=At5g59520; ORFNames=F2O15.19;
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], AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9618566; DOI=10.1073/pnas.95.12.7220;
RA Grotz N., Fox T., Connolly E., Park W., Guerinot M.L., Eide D.;
RT "Identification of a family of zinc transporter genes from Arabidopsis that
RT respond to zinc deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7220-7224(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION.
RX PubMed=13129917; DOI=10.1074/jbc.m309338200;
RA Wintz H., Fox T., Wu Y.-Y., Feng V., Chen W., Chang H.-S., Zhu T.,
RA Vulpe C.D.;
RT "Expression profiles of Arabidopsis thaliana in mineral deficiencies reveal
RT novel transporters involved in metal homeostasis.";
RL J. Biol. Chem. 278:47644-47653(2003).
CC -!- FUNCTION: Mediates zinc uptake. May also transport copper and cadmium
CC ions. {ECO:0000269|PubMed:9618566}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: In roots by zinc and copper starvation.
CC {ECO:0000269|PubMed:13129917}.
CC -!- MISCELLANEOUS: Zinc uptake is highly pH-dependent and no uptake is seen
CC at pH levels below 5.0. Inhibited by copper and cadmium ions.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
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DR EMBL; AF033536; AAC24198.1; -; mRNA.
DR EMBL; AB025604; BAA97486.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97200.1; -; Genomic_DNA.
DR PIR; T52184; T52184.
DR RefSeq; NP_200760.1; NM_125344.3.
DR AlphaFoldDB; Q9LTH9; -.
DR SMR; Q9LTH9; -.
DR STRING; 3702.AT5G59520.1; -.
DR PaxDb; Q9LTH9; -.
DR PRIDE; Q9LTH9; -.
DR ProteomicsDB; 232305; -.
DR EnsemblPlants; AT5G59520.1; AT5G59520.1; AT5G59520.
DR GeneID; 836071; -.
DR Gramene; AT5G59520.1; AT5G59520.1; AT5G59520.
DR KEGG; ath:AT5G59520; -.
DR Araport; AT5G59520; -.
DR TAIR; locus:2148398; AT5G59520.
DR eggNOG; KOG1558; Eukaryota.
DR HOGENOM; CLU_046211_0_0_1; -.
DR OMA; FGLLAKW; -.
DR OrthoDB; 981397at2759; -.
DR PhylomeDB; Q9LTH9; -.
DR PRO; PR:Q9LTH9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTH9; baseline and differential.
DR Genevisible; Q9LTH9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion transport; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..353
FT /note="Zinc transporter 2"
FT /id="PRO_0000041640"
FT TOPO_DOM 30..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 13
FT /note="F -> V (in Ref. 1; AAC24198)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="S -> G (in Ref. 1; AAC24198)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="V -> I (in Ref. 1; AAC24198)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="R -> L (in Ref. 1; AAC24198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38313 MW; D2CCB8FCD3552FC4 CRC64;
MALSSKTLKS TLFFLSIIFL CFSLILAHGG IDDGDEEEET NQPPPATGTT TVVNLRSKSL
VLVKIYCIII LFFSTFLAGV SPYFYRWNES FLLLGTQFSG GIFLATALIH FLSDANETFR
GLKHKEYPYA FMLAAAGYCL TMLADVAVAF VAAGSNNNHV GASVGESRED DDVAVKEEGR
REIKSGVDVS QALIRTSGFG DTALLIFALC FHSIFEGIAI GLSDTKSDAW RNLWTISLHK
VFAAVAMGIA LLKLIPKRPF FLTVVYSFAF GISSPIGVGI GIGINATSQG AGGDWTYAIS
MGLACGVFVY VAVNHLISKG YKPREECYFD KPIYKFIAVF LGVALLSVVM IWD