HMA4_ARATH
ID HMA4_ARATH Reviewed; 1172 AA.
AC O64474;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Putative cadmium/zinc-transporting ATPase HMA4;
DE EC=7.2.2.12;
DE EC=7.2.2.21;
DE AltName: Full=Protein HEAVY METAL ATPASE 4;
DE AltName: Full=Putative cadmium/zinc-transporting ATPase 2;
GN Name=HMA4; OrderedLocusNames=At2g19110; ORFNames=T20K24.12;
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].
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=12848823; DOI=10.1046/j.1365-313x.2003.01790.x;
RA Mills R.F., Krijger G.C., Baccarini P.J., Hall J.L., Williams L.E.;
RT "Functional expression of AtHMA4, a P1B-type ATPase of the Zn/Co/Cd/Pb
RT subclass.";
RL Plant J. 35:164-176(2003).
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).
CC -!- FUNCTION: Involved in cadmium/zinc transport. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AJ297264; CAC19544.1; -; mRNA.
DR EMBL; AC002392; AAD12041.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06848.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62252.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62253.1; -; Genomic_DNA.
DR EMBL; AY096796; AAM19954.1; -; mRNA.
DR PIR; F84572; F84572.
DR RefSeq; NP_001318247.1; NM_001335621.1.
DR RefSeq; NP_001324425.1; NM_001335622.1.
DR RefSeq; NP_179501.1; NM_127468.5.
DR PDB; 2KKH; NMR; -; A=2-96.
DR PDBsum; 2KKH; -.
DR AlphaFoldDB; O64474; -.
DR SMR; O64474; -.
DR BioGRID; 1785; 1.
DR IntAct; O64474; 1.
DR STRING; 3702.AT2G19110.1; -.
DR TCDB; 3.A.3.6.18; the p-type atpase (p-atpase) superfamily.
DR PaxDb; O64474; -.
DR PRIDE; O64474; -.
DR ProteomicsDB; 230352; -.
DR EnsemblPlants; AT2G19110.1; AT2G19110.1; AT2G19110.
DR EnsemblPlants; AT2G19110.2; AT2G19110.2; AT2G19110.
DR EnsemblPlants; AT2G19110.3; AT2G19110.3; AT2G19110.
DR GeneID; 816428; -.
DR Gramene; AT2G19110.1; AT2G19110.1; AT2G19110.
DR Gramene; AT2G19110.2; AT2G19110.2; AT2G19110.
DR Gramene; AT2G19110.3; AT2G19110.3; AT2G19110.
DR KEGG; ath:AT2G19110; -.
DR Araport; AT2G19110; -.
DR TAIR; locus:2059083; AT2G19110.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_3_1_1; -.
DR InParanoid; O64474; -.
DR OMA; HENAGLE; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; O64474; -.
DR BioCyc; ARA:AT2G19110-MON; -.
DR EvolutionaryTrace; O64474; -.
DR PRO; PR:O64474; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64474; baseline and differential.
DR Genevisible; O64474; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016463; F:P-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015691; P:cadmium ion transport; IMP:TAIR.
DR GO; GO:0030001; P:metal ion transport; IMP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR GO; GO:0032025; P:response to cobalt ion; IMP:TAIR.
DR GO; GO:0010038; P:response to metal ion; IMP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IMP:TAIR.
DR GO; GO:0055069; P:zinc ion homeostasis; IGI:TAIR.
DR GO; GO:0006829; P:zinc ion transport; IMP:TAIR.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cadmium; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..1172
FT /note="Putative cadmium/zinc-transporting ATPase HMA4"
FT /id="PRO_0000046399"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..680
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..1172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..83
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 401
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2KKH"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:2KKH"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:2KKH"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:2KKH"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:2KKH"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:2KKH"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2KKH"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2KKH"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2KKH"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2KKH"
SQ SEQUENCE 1172 AA; 127209 MW; 1E913B9450443440 CRC64;
MALQNKEEEK KKVKKLQKSY FDVLGICCTS EVPIIENILK SLDGVKEYSV IVPSRTVIVV
HDSLLISPFQ IAKALNEARL EANVRVNGET SFKNKWPSPF AVVSGLLLLL SFLKFVYSPL
RWLAVAAVAA GIYPILAKAF ASIKRPRIDI NILVIITVIA TLAMQDFMEA AAVVFLFTIS
DWLETRASYK ATSVMQSLMS LAPQKAIIAE TGEEVEVDEV KVDTVVAVKA GETIPIDGIV
VDGNCEVDEK TLTGEAFPVP KQRDSTVWAG TINLNGYICV KTTSLAGDCV VAKMAKLVEE
AQSSKTKSQR LIDKCSQYYT PAIILVSACV AIVPVIMKVH NLKHWFHLAL VVLVSGCPCG
LILSTPVATF CALTKAATSG LLIKSADYLD TLSKIKIVAF DKTGTITRGE FIVIDFKSLS
RDINLRSLLY WVSSVESKSS HPMAATIVDY AKSVSVEPRP EEVEDYQNFP GEGIYGKIDG
NDIFIGNKKI ASRAGCSTVP EIEVDTKGGK TVGYVYVGER LAGFFNLSDA CRSGVSQAMA
ELKSLGIKTA MLTGDNQAAA MHAQEQLGNV LDVVHGDLLP EDKSRIIQEF KKEGPTAMVG
DGVNDAPALA TADIGISMGI SGSALATQTG NIILMSNDIR RIPQAVKLAR RARRKVVENV
CLSIILKAGI LALAFAGHPL IWAAVLVDVG TCLLVIFNSM LLLREKKKIG NKKCYRASTS
KLNGRKLEGD DDYVVDLEAG LLTKSGNGQC KSSCCGDKKN QENVVMMKPS SKTSSDHSHP
GCCGDKKEEK VKPLVKDGCC SEKTRKSEGD MVSLSSCKKS SHVKHDLKMK GGSGCCASKN
EKGKEVVAKS CCEKPKQQVE SVGDCKSGHC EKKKQAEDIV VPVQIIGHAL THVEIELQTK
ETCKTSCCDS KEKVKETGLL LSSENTPYLE KGVLIKDEGN CKSGSENMGT VKQSCHEKGC
SDEKQTGEIT LASEEETDDQ DCSSGCCVNE GTVKQSFDEK KHSVLVEKEG LDMETGFCCD
AKLVCCGNTE GEVKEQCRLE IKKEEHCKSG CCGEEIQTGE ITLVSEEETE STNCSTGCCV
DKEEVTQTCH EKPASLVVSG LEVKKDEHCE SSHRAVKVET CCKVKIPEAC ASKCRDRAKR
HSGKSCCRSY AKELCSHRHH HHHHHHHHHV SA
