ID D7MLH0_ARALL Unreviewed; 1004 AA.
AC D7MLH0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Responsive-to-antagonist1 {ECO:0000313|EMBL:EFH39804.1};
GN Name=RAN1 {ECO:0000313|EMBL:EFH39804.1};
GN ORFNames=ARALYDRAFT_494501 {ECO:0000313|EMBL:EFH39804.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; GL348720; EFH39804.1; -; Genomic_DNA.
DR RefSeq; XP_002863545.1; XM_002863499.1.
DR AlphaFoldDB; D7MLH0; -.
DR STRING; 81972.D7MLH0; -.
DR EnsemblPlants; fgenesh2_kg.8__317__AT5G44790.1; fgenesh2_kg.8__317__AT5G44790.1; fgenesh2_kg.8__317__AT5G44790.1.
DR GeneID; 9299621; -.
DR Gramene; fgenesh2_kg.8__317__AT5G44790.1; fgenesh2_kg.8__317__AT5G44790.1; fgenesh2_kg.8__317__AT5G44790.1.
DR KEGG; aly:9299621; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_3_1; -.
DR OrthoDB; 7279at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0010119; P:regulation of stomatal movement; IEA:EnsemblPlants.
DR GO; GO:0009723; P:response to ethylene; IEA:EnsemblPlants.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 3.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
DR PANTHER; PTHR46594:SF6; COPPER-TRANSPORTING ATPASE RAN1; 1.
DR PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 306..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 403..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 558..583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 938..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 58..124
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 136..202
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 210..276
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 107559 MW; 3073518B92935736 CRC64;
MAPSRRDLQL TPVTGESSSE VGDMEEVRLL DSYYNEENAD DILSKIEEGG GGDDSGLRKI
QVGITGMTCA ACSNSVEGAL MNVNGVFKAS VALLQNRADV VFDPNLVKEE DIKEAIEDAG
FEAEILAEVV ATGTTLVGQF TIGGMTCAAC VNSVEGILRD LPGVKRAVVA LSTSLGEVEY
DPNVINKDDI VTAIEDAGFE GSLVQSNQQD KLVLRVEGIM NELDAQVLEG ILTRLNGVRQ
FRLDRISGEL EVVFDPEVVS SRSLVDGIEG DGYGKFKLRV MSPYERLTSK DTGEASNMFR
RFISSLVLSI PLFFIQVICP HIALFDALLV WRCGPFMMGD WLKWALVSVI QFVIGKRFYV
AAWRALRNGS TNMDVLVALG TSASYFYSVG ALLYGAVTGF WSPTYFDASA MLITFVLLGK
YLESLAKGKT SDAMKKLVQL TPATAILLIE GKGGKLVGER EIDALLIQPG DTLKVHPGAK
IPADGVVVWG SSYVNESMVT GESVPVSKEV DSPVIGGTIN MHGALHMKAT KVGSDAVLSQ
IISLVETAQM SKAPIQKFAD YVASIFVPVV ITLALFTLIG WSIGGAVGAY PDEWLPENGT
HFVFSLMFSI SVVVIACPCA LGLATPTAVM VATGVGATNG VLIKGGDALE KAHKVKYVIF
DKTGTLTQGK ATVTTTKVFS EMDRGEFLTL VASAEASSEH PLAKAIVAYA RHFHFFDEST
EDGETNNKDL QNSGWLLNTS DFSALPGKGI QCLVNEKMIL VGNRKLMSEN TITIPDHVEK
FVEDLEESGK TGVIVAYSGK LVGVMGIADP LKREAAVVVE GLLRMGVQPI MVTGDNWRTA
RAVAKEVGIK DVRAEVMPAG KADVIRSLQK DGSTVAMVGD GINDSPALAA ADVGMAIGAG
TDVAIEAADY VLMRNNLEDV ITAIDLSRKT LTRIRLNYVF AMAYNVVSIP IAAGVFFPVL
RVQLPPWAAG ACMALSSVSV VCSSLLLRRY KKPRLTTILE ITTE
//