HMA7_ARATH
ID HMA7_ARATH Reviewed; 1001 AA.
AC Q9S7J8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Copper-transporting ATPase RAN1;
DE EC=7.2.2.8;
DE AltName: Full=Protein HEAVY METAL ATPASE 7;
DE AltName: Full=Protein RESPONSIVE TO ANTAGONIST 1;
GN Name=RAN1; Synonyms=HMA7; OrderedLocusNames=At5g44790;
GN ORFNames=K23L20.14, T19K24.18;
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 [GENOMIC DNA / MRNA], AND MUTAGENESIS.
RC STRAIN=cv. Columbia;
RX PubMed=10319818; DOI=10.1016/s0092-8674(00)80747-3;
RA Hirayama T., Kieber J.J., Hirayama N., Kogan M., Guzman P., Nourizadeh S.,
RA Alonso J.M., Dailey W.P., Dancis A., Ecker J.R.;
RT "Responsive-to-antagonist 1, a Menkes/Wilson disease-related copper
RT transporter, is required for ethylene signaling in Arabidopsis.";
RL Cell 97:383-393(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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: Involved in copper import into the cell. Essential for
CC ethylene signaling, which requires copper. Acts by delivering copper to
CC create functional hormone receptors.
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 -!- 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; AF091112; AAD29115.1; -; Genomic_DNA.
DR EMBL; AF082565; AAD29109.1; -; mRNA.
DR EMBL; AB016874; BAB08832.1; -; Genomic_DNA.
DR EMBL; AC002342; AAC79141.2; -; Genomic_DNA.
DR EMBL; CP002688; AED95163.1; -; Genomic_DNA.
DR RefSeq; NP_199292.1; NM_123847.3.
DR PDB; 3DXS; X-ray; 1.70 A; X=56-128.
DR PDBsum; 3DXS; -.
DR AlphaFoldDB; Q9S7J8; -.
DR SMR; Q9S7J8; -.
DR BioGRID; 19759; 3.
DR IntAct; Q9S7J8; 2.
DR STRING; 3702.AT5G44790.1; -.
DR TCDB; 3.A.3.5.32; the p-type atpase (p-atpase) superfamily.
DR SwissPalm; Q9S7J8; -.
DR PaxDb; Q9S7J8; -.
DR PRIDE; Q9S7J8; -.
DR ProteomicsDB; 232096; -.
DR EnsemblPlants; AT5G44790.1; AT5G44790.1; AT5G44790.
DR GeneID; 834509; -.
DR Gramene; AT5G44790.1; AT5G44790.1; AT5G44790.
DR KEGG; ath:AT5G44790; -.
DR Araport; AT5G44790; -.
DR TAIR; locus:2156354; AT5G44790.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_3_1; -.
DR InParanoid; Q9S7J8; -.
DR OMA; ITFFGWM; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; Q9S7J8; -.
DR BioCyc; ARA:AT5G44790-MON; -.
DR EvolutionaryTrace; Q9S7J8; -.
DR PRO; PR:Q9S7J8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7J8; baseline and differential.
DR Genevisible; Q9S7J8; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; 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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; TAS:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR CDD; cd00371; HMA; 2.
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; 2.
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; 2.
DR TIGRFAMs; TIGR00003; TIGR00003; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Copper; Copper transport;
KW Ethylene signaling pathway; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1001
FT /note="Copper-transporting ATPase RAN1"
FT /id="PRO_0000046402"
FT TOPO_DOM 1..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..602
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 932..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..963
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..1001
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 56..122
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 133..199
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 207..273
FT /note="HMA 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 658
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 70
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 144
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 147
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 877
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 881
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 173
FT /note="G->E: In ran1-2."
FT /evidence="ECO:0000269|PubMed:10319818"
FT MUTAGEN 497
FT /note="T->I: In ran1-1."
FT /evidence="ECO:0000269|PubMed:10319818"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3DXS"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:3DXS"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3DXS"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3DXS"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3DXS"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3DXS"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:3DXS"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3DXS"
SQ SEQUENCE 1001 AA; 107395 MW; 7E820909C60D5B0F CRC64;
MAPSRRDLQL TPVTGGSSSQ ISDMEEVGLL DSYHNEANAD DILTKIEEGR DVSGLRKIQV
GVTGMTCAAC SNSVEAALMN VNGVFKASVA LLQNRADVVF DPNLVKEEDI KEAIEDAGFE
AEILAEEQTQ ATLVGQFTIG GMTCAACVNS VEGILRDLPG VKRAVVALST SLGEVEYDPN
VINKDDIVNA IEDAGFEGSL VQSNQQDKLV LRVDGILNEL DAQVLEGILT RLNGVRQFRL
DRISGELEVV FDPEVVSSRS LVDGIEEDGF GKFKLRVMSP YERLSSKDTG EASNMFRRFI
SSLVLSIPLF FIQVICPHIA LFDALLVWRC GPFMMGDWLK WALVSVIQFV IGKRFYVAAW
RALRNGSTNM DVLVALGTSA SYFYSVGALL YGAVTGFWSP TYFDASAMLI TFVLLGKYLE
SLAKGKTSDA MKKLVQLTPA TAILLTEGKG GKLVGEREID ALLIQPGDTL KVHPGAKIPA
DGVVVWGSSY VNESMVTGES VPVSKEVDSP VIGGTINMHG ALHMKATKVG SDAVLSQIIS
LVETAQMSKA PIQKFADYVA SIFVPVVITL ALFTLVGWSI GGAVGAYPDE WLPENGTHFV
FSLMFSISVV VIACPCALGL ATPTAVMVAT GVGATNGVLI KGGDALEKAH KVKYVIFDKT
GTLTQGKATV TTTKVFSEMD RGEFLTLVAS AEASSEHPLA KAIVAYARHF HFFDESTEDG
ETNNKDLQNS GWLLDTSDFS ALPGKGIQCL VNEKMILVGN RKLMSENAIN IPDHVEKFVE
DLEESGKTGV IVAYNGKLVG VMGIADPLKR EAALVVEGLL RMGVRPIMVT GDNWRTARAV
AKEVGIEDVR AEVMPAGKAD VIRSLQKDGS TVAMVGDGIN DSPALAAADV GMAIGAGTDV
AIEAADYVLM RNNLEDVITA IDLSRKTLTR IRLNYVFAMA YNVVSIPIAA GVFFPVLRVQ
LPPWAAGACM ALSSVSVVCS SLLLRRYKKP RLTTVLKITT E
