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Database: UniProt
Entry: D7MLH0_ARALL
LinkDB: D7MLH0_ARALL
Original site: D7MLH0_ARALL 
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
//
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