HMA5_ARATH
ID HMA5_ARATH Reviewed; 995 AA.
AC Q9SH30;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Probable copper-transporting ATPase HMA5;
DE EC=7.2.2.8;
DE AltName: Full=Probable copper-transporting ATPase 3;
DE AltName: Full=Protein HEAVY METAL ATPASE 5;
GN Name=HMA5; OrderedLocusNames=At1g63440; ORFNames=F2K11.18;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, INTERACTION WITH ATX1, TISSUE SPECIFICITY, INDUCTION BY COPPER,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16367966; DOI=10.1111/j.1365-313x.2005.02601.x;
RA Andres-Colas N., Sancenon V., Rodriguez-Navarro S., Mayo S., Thiele D.J.,
RA Ecker J.R., Puig S., Penarrubia L.;
RT "The Arabidopsis heavy metal P-type ATPase HMA5 interacts with
RT metallochaperones and functions in copper detoxification of roots.";
RL Plant J. 45:225-236(2006).
CC -!- FUNCTION: Involved in copper import into the cell. May play a role in
CC copper detoxification in roots. {ECO:0000269|PubMed:16367966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC -!- SUBUNIT: Interacts with ATX1. {ECO:0000269|PubMed:16367966}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:16367966}.
CC -!- INDUCTION: By copper. {ECO:0000269|PubMed:16367966}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are hypersensitive to copper excess.
CC {ECO:0000269|PubMed:16367966}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008047; AAF19707.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34100.1; -; Genomic_DNA.
DR PIR; B96660; B96660.
DR RefSeq; NP_176533.1; NM_105023.2.
DR AlphaFoldDB; Q9SH30; -.
DR SMR; Q9SH30; -.
DR BioGRID; 27871; 2.
DR IntAct; Q9SH30; 1.
DR STRING; 3702.AT1G63440.1; -.
DR PaxDb; Q9SH30; -.
DR PRIDE; Q9SH30; -.
DR ProteomicsDB; 230230; -.
DR EnsemblPlants; AT1G63440.1; AT1G63440.1; AT1G63440.
DR GeneID; 842650; -.
DR Gramene; AT1G63440.1; AT1G63440.1; AT1G63440.
DR KEGG; ath:AT1G63440; -.
DR Araport; AT1G63440; -.
DR TAIR; locus:2031361; AT1G63440.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_3_1; -.
DR InParanoid; Q9SH30; -.
DR OMA; IEKTGYE; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; Q9SH30; -.
DR BioCyc; ARA:MON-14503; -.
DR BioCyc; MetaCyc:MON-14503; -.
DR BRENDA; 7.2.2.9; 399.
DR PRO; PR:Q9SH30; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SH30; baseline and differential.
DR Genevisible; Q9SH30; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0010273; P:detoxification of copper ion; IMP:TAIR.
DR GO; GO:0046688; P:response to copper ion; IMP:TAIR.
DR CDD; cd00371; HMA; 3.
DR Gene3D; 3.40.1110.10; -; 2.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
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 Pfam; PF00403; HMA; 3.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 3.
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 TIGRFAMs; TIGR00003; TIGR00003; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 3.
PE 1: Evidence at protein level;
KW ATP-binding; Copper; Copper transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..995
FT /note="Probable copper-transporting ATPase HMA5"
FT /id="PRO_0000046404"
FT TOPO_DOM 1..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..952
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 972..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..117
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 129..195
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 204..270
FT /note="HMA 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 661
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 65
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 140
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 143
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 866
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 870
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 995 AA; 108336 MW; C9289E6FDE7D727B CRC64;
MATKLLSLTC IRKERFSERY PLVRKHLTRS RDGGGGSSSE TAAFEIDDPI SRAVFQVLGM
TCSACAGSVE KAIKRLPGIH DAVIDALNNR AQILFYPNSV DVETIRETIE DAGFEASLIE
NEANERSRQV CRIRINGMTC TSCSSTIERV LQSVNGVQRA HVALAIEEAE IHYDPRLSSY
DRLLEEIENA GFEAVLISTG EDVSKIDLKI DGELTDESMK VIERSLEALP GVQSVEISHG
TDKISVLYKP DVTGPRNFIQ VIESTVFGHS GHIKATIFSE GGVGRESQKQ GEIKQYYKSF
LWSLVFTVPV FLTAMVFMYI PGIKDLLMFK VINMLTVGEI IRCVLATPVQ FVIGWRFYTG
SYKALRRGSA NMDVLIALGT NAAYFYSLYT VLRAATSPDF KGVDFFETSA MLISFIILGK
YLEVMAKGKT SQAIAKLMNL APDTAILLSL DKEGNVTGEE EIDGRLIQKN DVIKIVPGAK
VASDGYVIWG QSHVNESMIT GEARPVAKRK GDTVIGGTLN ENGVLHVKVT RVGSESALAQ
IVRLVESAQL AKAPVQKLAD RISKFFVPLV IFLSFSTWLA WFLAGKLHWY PESWIPSSMD
SFELALQFGI SVMVIACPCA LGLATPTAVM VGTGVGASQG VLIKGGQALE RAHKVNCIVF
DKTGTLTMGK PVVVKTKLLK NMVLREFYEL VAATEVNSEH PLAKAIVEYA KKFRDDEENP
AWPEACDFVS ITGKGVKATV KGREIMVGNK NLMNDHKVII PDDAEELLAD SEDMAQTGIL
VSINSELIGV LSVSDPLKPS AREAISILKS MNIKSIMVTG DNWGTANSIA REVGIDSVIA
EAKPEQKAEK VKELQAAGHV VAMVGDGIND SPALVAADVG MAIGAGTDIA IEAADIVLMK
SNLEDVITAI DLSRKTFSRI RLNYVWALGY NLMGIPIAAG VLFPGTRFRL PPWIAGAAMA
ASSVSVVCCS LLLKNYKRPK KLDHLEIREI QVERV
