Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9S7J8 (HMA7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase RAN1

EC=3.6.3.54
Alternative name(s):
Protein HEAVY METAL ATPASE 7
Protein RESPONSIVE TO ANTAGONIST 1
Gene names
Name:RAN1
Synonyms:HMA7
Ordered Locus Names:At5g44790
ORF Names:K23L20.14, T19K24.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1001 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 3 HMA domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10011001Copper-transporting ATPase RAN1
PRO_0000046402

Regions

Topological domain1 – 298298Cytoplasmic Potential
Transmembrane299 – 32022Helical; Potential
Topological domain321 – 33818Extracellular Potential
Transmembrane339 – 35820Helical; Potential
Topological domain359 – 3657Cytoplasmic Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 40317Extracellular Potential
Transmembrane404 – 42421Helical; Potential
Topological domain425 – 558134Cytoplasmic Potential
Transmembrane559 – 58123Helical; Potential
Topological domain582 – 60221Extracellular Potential
Transmembrane603 – 62018Helical; Potential
Topological domain621 – 931311Cytoplasmic Potential
Transmembrane932 – 95120Helical; Potential
Topological domain952 – 96312Extracellular Potential
Transmembrane964 – 98219Helical; Potential
Topological domain983 – 100119Cytoplasmic Potential
Domain57 – 12367HMA 1
Domain134 – 20067HMA 2
Domain208 – 27467HMA 3; degenerate

Sites

Active site65814-aspartylphosphate intermediate By similarity
Metal binding671Copper Potential
Metal binding701Copper Potential
Metal binding1441Copper Potential
Metal binding1471Copper Potential
Metal binding8771Magnesium By similarity
Metal binding8811Magnesium By similarity

Experimental info

Mutagenesis1731G → E in ran1-2.
Mutagenesis4971T → I in ran1-1.

Secondary structure

................ 1001
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9S7J8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7E820909C60D5B0F

FASTA1,001107,395
        10         20         30         40         50         60 
MAPSRRDLQL TPVTGGSSSQ ISDMEEVGLL DSYHNEANAD DILTKIEEGR DVSGLRKIQV 

        70         80         90        100        110        120 
GVTGMTCAAC SNSVEAALMN VNGVFKASVA LLQNRADVVF DPNLVKEEDI KEAIEDAGFE 

       130        140        150        160        170        180 
AEILAEEQTQ ATLVGQFTIG GMTCAACVNS VEGILRDLPG VKRAVVALST SLGEVEYDPN 

       190        200        210        220        230        240 
VINKDDIVNA IEDAGFEGSL VQSNQQDKLV LRVDGILNEL DAQVLEGILT RLNGVRQFRL 

       250        260        270        280        290        300 
DRISGELEVV FDPEVVSSRS LVDGIEEDGF GKFKLRVMSP YERLSSKDTG EASNMFRRFI 

       310        320        330        340        350        360 
SSLVLSIPLF FIQVICPHIA LFDALLVWRC GPFMMGDWLK WALVSVIQFV IGKRFYVAAW 

       370        380        390        400        410        420 
RALRNGSTNM DVLVALGTSA SYFYSVGALL YGAVTGFWSP TYFDASAMLI TFVLLGKYLE 

       430        440        450        460        470        480 
SLAKGKTSDA MKKLVQLTPA TAILLTEGKG GKLVGEREID ALLIQPGDTL KVHPGAKIPA 

       490        500        510        520        530        540 
DGVVVWGSSY VNESMVTGES VPVSKEVDSP VIGGTINMHG ALHMKATKVG SDAVLSQIIS 

       550        560        570        580        590        600 
LVETAQMSKA PIQKFADYVA SIFVPVVITL ALFTLVGWSI GGAVGAYPDE WLPENGTHFV 

       610        620        630        640        650        660 
FSLMFSISVV VIACPCALGL ATPTAVMVAT GVGATNGVLI KGGDALEKAH KVKYVIFDKT 

       670        680        690        700        710        720 
GTLTQGKATV TTTKVFSEMD RGEFLTLVAS AEASSEHPLA KAIVAYARHF HFFDESTEDG 

       730        740        750        760        770        780 
ETNNKDLQNS GWLLDTSDFS ALPGKGIQCL VNEKMILVGN RKLMSENAIN IPDHVEKFVE 

       790        800        810        820        830        840 
DLEESGKTGV IVAYNGKLVG VMGIADPLKR EAALVVEGLL RMGVRPIMVT GDNWRTARAV 

       850        860        870        880        890        900 
AKEVGIEDVR AEVMPAGKAD VIRSLQKDGS TVAMVGDGIN DSPALAAADV GMAIGAGTDV 

       910        920        930        940        950        960 
AIEAADYVLM RNNLEDVITA IDLSRKTLTR IRLNYVFAMA YNVVSIPIAA GVFFPVLRVQ 

       970        980        990       1000 
LPPWAAGACM ALSSVSVVCS SLLLRRYKKP RLTTVLKITT E 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_199292.1. NM_123847.2.
UniGeneAt.24482.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DXSX-ray1.70X56-127[»]
ProteinModelPortalQ9S7J8.
SMRQ9S7J8. Positions 12-993.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19759. 1 interaction.
IntActQ9S7J8. 2 interactions.
MINTMINT-8066708.

Protein family/group databases

TCDB3.A.3.5.32. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbQ9S7J8.
PRIDEQ9S7J8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G44790.1; AT5G44790.1; AT5G44790.
GeneID834509.
KEGGath:AT5G44790.

Organism-specific databases

TAIRAT5G44790.

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250397.
InParanoidQ9S7J8.
KOK17686.
OMAHGMAHVY.
PhylomeDBQ9S7J8.
ProtClustDBCLSN2687280.

Enzyme and pathway databases

BioCycARA:AT5G44790-MONOMER.

Gene expression databases

GenevestigatorQ9S7J8.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. 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.
IPR027183. Cu-transptr_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
[Graphical view]
PANTHERPTHR24093:SF42. PTHR24093:SF42. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF55008. SSF55008. 3 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 2 hits.
PS50846. HMA_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9S7J8.
PROQ9S7J8.

Entry information

Entry nameHMA7_ARATH
AccessionPrimary (citable) accession number: Q9S7J8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names