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Q9S7J8

- HMA7_ARATH

UniProt

Q9S7J8 - HMA7_ARATH

Protein

Copper-transporting ATPase RAN1

Gene

RAN1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Involved in copper import into the cell. Essential for ethylene signaling, which requires copper. Acts by delivering copper to create functional hormone receptors.

    Catalytic activityi

    ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi67 – 671CopperPROSITE-ProRule annotation
    Metal bindingi70 – 701CopperPROSITE-ProRule annotation
    Metal bindingi144 – 1441CopperPROSITE-ProRule annotation
    Metal bindingi147 – 1471CopperPROSITE-ProRule annotation
    Active sitei658 – 65814-aspartylphosphate intermediateBy similarity
    Metal bindingi877 – 8771MagnesiumPROSITE-ProRule annotation
    Metal bindingi881 – 8811MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cation-transporting ATPase activity Source: InterPro
    3. copper ion binding Source: InterPro
    4. copper ion transmembrane transporter activity Source: TAIR

    GO - Biological processi

    1. copper ion transmembrane transport Source: GOC
    2. ethylene-activated signaling pathway Source: TAIR
    3. regulation of stomatal movement Source: TAIR
    4. response to ethylene Source: TAIR

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Copper transport, Ethylene signaling pathway, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G44790-MONOMER.

    Protein family/group databases

    TCDBi3.A.3.5.32. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Copper-transporting ATPase RAN1 (EC:3.6.3.54)
    Alternative name(s):
    Protein HEAVY METAL ATPASE 7
    Protein RESPONSIVE TO ANTAGONIST 1
    Gene namesi
    Name:RAN1
    Synonyms:HMA7
    Ordered Locus Names:At5g44790
    ORF Names:K23L20.14, T19K24.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G44790.

    Subcellular locationi

    GO - Cellular componenti

    1. endosome Source: TAIR
    2. Golgi apparatus Source: TAIR
    3. integral component of membrane Source: UniProtKB-KW
    4. trans-Golgi network Source: TAIR

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi173 – 1731G → E in ran1-2. 1 Publication
    Mutagenesisi497 – 4971T → I in ran1-1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10011001Copper-transporting ATPase RAN1PRO_0000046402Add
    BLAST

    Proteomic databases

    PaxDbiQ9S7J8.
    PRIDEiQ9S7J8.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9S7J8.

    Interactioni

    Protein-protein interaction databases

    BioGridi19759. 1 interaction.
    IntActiQ9S7J8. 2 interactions.
    MINTiMINT-8066708.

    Structurei

    Secondary structure

    1
    1001
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 638
    Helixi68 – 7912
    Beta strandi84 – 907
    Helixi91 – 933
    Beta strandi95 – 1006
    Turni102 – 1043
    Helixi107 – 11711
    Beta strandi120 – 1267

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DXSX-ray1.70X56-128[»]
    ProteinModelPortaliQ9S7J8.
    SMRiQ9S7J8. Positions 55-270, 291-986.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S7J8.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 298298CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini321 – 33818ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini359 – 3657CytoplasmicSequence Analysis
    Topological domaini387 – 40317ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini425 – 558134CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini582 – 60221ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini621 – 931311CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini952 – 96312ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini983 – 100119CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei299 – 32022HelicalSequence AnalysisAdd
    BLAST
    Transmembranei339 – 35820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei366 – 38621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei404 – 42421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei559 – 58123HelicalSequence AnalysisAdd
    BLAST
    Transmembranei603 – 62018HelicalSequence AnalysisAdd
    BLAST
    Transmembranei932 – 95120HelicalSequence AnalysisAdd
    BLAST
    Transmembranei964 – 98219HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 12367HMA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 20067HMA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini208 – 27467HMA 3; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 HMA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2217.
    HOGENOMiHOG000250397.
    InParanoidiQ9S7J8.
    KOiK17686.
    OMAiMSIMYLA.
    PhylomeDBiQ9S7J8.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view]
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 2 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF55008. SSF55008. 3 hits.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    TIGR00003. TIGR00003. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 2 hits.
    PS50846. HMA_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9S7J8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPSRRDLQL TPVTGGSSSQ ISDMEEVGLL DSYHNEANAD DILTKIEEGR     50
    DVSGLRKIQV GVTGMTCAAC SNSVEAALMN VNGVFKASVA LLQNRADVVF 100
    DPNLVKEEDI KEAIEDAGFE AEILAEEQTQ ATLVGQFTIG GMTCAACVNS 150
    VEGILRDLPG VKRAVVALST SLGEVEYDPN VINKDDIVNA IEDAGFEGSL 200
    VQSNQQDKLV LRVDGILNEL DAQVLEGILT RLNGVRQFRL DRISGELEVV 250
    FDPEVVSSRS LVDGIEEDGF GKFKLRVMSP YERLSSKDTG EASNMFRRFI 300
    SSLVLSIPLF FIQVICPHIA LFDALLVWRC GPFMMGDWLK WALVSVIQFV 350
    IGKRFYVAAW RALRNGSTNM DVLVALGTSA SYFYSVGALL YGAVTGFWSP 400
    TYFDASAMLI TFVLLGKYLE SLAKGKTSDA MKKLVQLTPA TAILLTEGKG 450
    GKLVGEREID ALLIQPGDTL KVHPGAKIPA DGVVVWGSSY VNESMVTGES 500
    VPVSKEVDSP VIGGTINMHG ALHMKATKVG SDAVLSQIIS LVETAQMSKA 550
    PIQKFADYVA SIFVPVVITL ALFTLVGWSI GGAVGAYPDE WLPENGTHFV 600
    FSLMFSISVV VIACPCALGL ATPTAVMVAT GVGATNGVLI KGGDALEKAH 650
    KVKYVIFDKT GTLTQGKATV TTTKVFSEMD RGEFLTLVAS AEASSEHPLA 700
    KAIVAYARHF HFFDESTEDG ETNNKDLQNS GWLLDTSDFS ALPGKGIQCL 750
    VNEKMILVGN RKLMSENAIN IPDHVEKFVE DLEESGKTGV IVAYNGKLVG 800
    VMGIADPLKR EAALVVEGLL RMGVRPIMVT GDNWRTARAV AKEVGIEDVR 850
    AEVMPAGKAD VIRSLQKDGS TVAMVGDGIN DSPALAAADV GMAIGAGTDV 900
    AIEAADYVLM RNNLEDVITA IDLSRKTLTR IRLNYVFAMA YNVVSIPIAA 950
    GVFFPVLRVQ LPPWAAGACM ALSSVSVVCS SLLLRRYKKP RLTTVLKITT 1000
    E 1001
    Length:1,001
    Mass (Da):107,395
    Last modified:May 1, 2000 - v1
    Checksum:i7E820909C60D5B0F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091112 Genomic DNA. Translation: AAD29115.1.
    AF082565 mRNA. Translation: AAD29109.1.
    AB016874 Genomic DNA. Translation: BAB08832.1.
    AC002342 Genomic DNA. Translation: AAC79141.2.
    CP002688 Genomic DNA. Translation: AED95163.1.
    RefSeqiNP_199292.1. NM_123847.2.
    UniGeneiAt.24482.

    Genome annotation databases

    EnsemblPlantsiAT5G44790.1; AT5G44790.1; AT5G44790.
    GeneIDi834509.
    KEGGiath:AT5G44790.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091112 Genomic DNA. Translation: AAD29115.1 .
    AF082565 mRNA. Translation: AAD29109.1 .
    AB016874 Genomic DNA. Translation: BAB08832.1 .
    AC002342 Genomic DNA. Translation: AAC79141.2 .
    CP002688 Genomic DNA. Translation: AED95163.1 .
    RefSeqi NP_199292.1. NM_123847.2.
    UniGenei At.24482.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DXS X-ray 1.70 X 56-128 [» ]
    ProteinModelPortali Q9S7J8.
    SMRi Q9S7J8. Positions 55-270, 291-986.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 19759. 1 interaction.
    IntActi Q9S7J8. 2 interactions.
    MINTi MINT-8066708.

    Protein family/group databases

    TCDBi 3.A.3.5.32. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    PaxDbi Q9S7J8.
    PRIDEi Q9S7J8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G44790.1 ; AT5G44790.1 ; AT5G44790 .
    GeneIDi 834509.
    KEGGi ath:AT5G44790.

    Organism-specific databases

    TAIRi AT5G44790.

    Phylogenomic databases

    eggNOGi COG2217.
    HOGENOMi HOG000250397.
    InParanoidi Q9S7J8.
    KOi K17686.
    OMAi MSIMYLA.
    PhylomeDBi Q9S7J8.

    Enzyme and pathway databases

    BioCyci ARA:AT5G44790-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9S7J8.
    PROi Q9S7J8.

    Gene expression databases

    Genevestigatori Q9S7J8.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view ]
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 2 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF55008. SSF55008. 3 hits.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    TIGR00003. TIGR00003. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 2 hits.
    PS50846. HMA_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Responsive-to-antagonist 1, a Menkes/Wilson disease-related copper transporter, is required for ethylene signaling in Arabidopsis."
      Hirayama T., Kieber J.J., Hirayama N., Kogan M., Guzman P., Nourizadeh S., Alonso J.M., Dailey W.P., Dancis A., Ecker J.R.
      Cell 97:383-393(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS.
      Strain: cv. Columbia.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
      Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
      DNA Res. 5:379-391(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiHMA7_ARATH
    AccessioniPrimary (citable) accession number: Q9S7J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3