ZIP1_ARATH
ID ZIP1_ARATH Reviewed; 355 AA.
AC O81123;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Zinc transporter 1;
DE AltName: Full=ZRT/IRT-like protein 1;
DE Flags: Precursor;
GN Name=ZIP1; OrderedLocusNames=At3g12750; ORFNames=MBK21.13;
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], FUNCTION, AND INDUCTION.
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;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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).
CC -!- FUNCTION: Mediates zinc uptake from the rhizosphere. May also transport
CC copper and cadmium ions. {ECO:0000269|PubMed:9618566}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the roots of zinc-
CC deficient plants.
CC -!- INDUCTION: By zinc starvation. {ECO:0000269|PubMed:9618566}.
CC -!- MISCELLANEOUS: Zinc uptake is 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; AF033535; AAC24197.1; -; mRNA.
DR EMBL; AB024033; BAB02419.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75242.1; -; Genomic_DNA.
DR PIR; T52183; T52183.
DR RefSeq; NP_187881.1; NM_112111.3.
DR AlphaFoldDB; O81123; -.
DR SMR; O81123; -.
DR STRING; 3702.AT3G12750.1; -.
DR TCDB; 2.A.5.1.3; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR PaxDb; O81123; -.
DR PRIDE; O81123; -.
DR EnsemblPlants; AT3G12750.1; AT3G12750.1; AT3G12750.
DR GeneID; 820457; -.
DR Gramene; AT3G12750.1; AT3G12750.1; AT3G12750.
DR KEGG; ath:AT3G12750; -.
DR Araport; AT3G12750; -.
DR TAIR; locus:2087705; AT3G12750.
DR eggNOG; KOG1558; Eukaryota.
DR HOGENOM; CLU_027089_3_0_1; -.
DR OMA; TMMIDSV; -.
DR OrthoDB; 981397at2759; -.
DR PhylomeDB; O81123; -.
DR PRO; PR:O81123; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O81123; baseline and differential.
DR Genevisible; O81123; 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; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR Pfam; PF02535; Zip; 1.
DR TIGRFAMs; TIGR00820; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..355
FT /note="Zinc transporter 1"
FT /id="PRO_0000041639"
FT TOPO_DOM 29..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 355 AA; 37812 MW; C21A2A36F4105938 CRC64;
MSECGCFSAT TMLRICVVLI ICLHMCCASS DCTSHDDPVS QDEAEKATKL KLGSIALLLV
AGGVGVSLPL IGKRIPALQP ENDIFFMVKA FAAGVILCTG FVHILPDAFE RLSSPCLEDT
TAGKFPFAGF VAMLSAMGTL MIDTFATGYY KRQHFSNNHG SKQVNVVVDE EEHAGHVHIH
THASHGHTHG STELIRRRIV SQVLEIGIVV HSVIIGISLG ASQSIDTIKP LMAALSFHQF
FEGLGLGGCI SLADMKSKST VLMATFFSVT APLGIGIGLG MSSGLGYRKE SKEAIMVEGM
LNAASAGILI YMSLVDLLAT DFMNPRLQSN LWLHLAAYLS LVLGAGSMSL LAIWA
