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B9DFX7 (HMA8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase PAA2, chloroplastic
EC=3.6.3.4
Alternative name(s):
Protein HEAVY METAL ATPASE 8
Gene names
Name:PAA2
Synonyms:HMA8
Ordered Locus Names:At5g21930
ORF Names:F13M11, T6G21
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mediates copper transfer across the chloroplast thylakoid membrane. Required for copper delivery into the thylakoids lumen, which is essential for the function of copper proteins. Ref.1

Catalytic activity

ATP + H2O + Cu2+(In) = ADP + phosphate + Cu2+(Out).

Subcellular location

Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Expressed in the shoots only and not in the roots. Ref.1

Disruption phenotype

High-chlorophyll-fluorescence phenotype. Ref.1

Sequence similarities

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

Contains 1 HMA domain.

Sequence caution

The sequence AAO73891.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAC34486.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: B9DFX7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6565Chloroplast Potential
Chain66 – 883818Copper-transporting ATPase PAA2, chloroplastic
PRO_0000416858

Regions

Transmembrane179 – 19921Helical; Potential
Transmembrane209 – 22921Helical; Potential
Transmembrane250 – 27021Helical; Potential
Transmembrane274 – 29421Helical; Potential
Transmembrane445 – 46521Helical; Potential
Transmembrane499 – 51921Helical; Potential
Transmembrane822 – 84221Helical; Potential
Transmembrane846 – 86621Helical; Potential
Domain77 – 14771HMA
Nucleotide binding761 – 7688ATP Potential

Sites

Active site54814-aspartylphosphate intermediate By similarity
Metal binding871Copper Potential
Metal binding901Copper Potential
Metal binding7621Magnesium By similarity
Metal binding7661Magnesium By similarity

Experimental info

Sequence conflict3121L → P in AAP55720. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: F5E365AB6B7A90C3

FASTA88394,260
        10         20         30         40         50         60 
MASNLLRFPL PPPSSLHIRP SKFLVNRCFP RLRRSRIRRH CSRPFFLVSN SVEISTQSFE 

        70         80         90        100        110        120 
STESSIESVK SITSDTPILL DVSGMMCGGC VARVKSVLMS DDRVASAVVN MLTETAAVKF 

       130        140        150        160        170        180 
KPEVEVTADT AESLAKRLTE SGFEAKRRVS GMGVAENVKK WKEMVSKKED LLVKSRNRVA 

       190        200        210        220        230        240 
FAWTLVALCC GSHTSHILHS LGIHIAHGGI WDLLHNSYVK GGLAVGALLG PGRELLFDGI 

       250        260        270        280        290        300 
KAFGKRSPNM NSLVGLGSMA AFSISLISLV NPELEWDASF FDEPVMLLGF VLLGRSLEER 

       310        320        330        340        350        360 
AKLQASTDMN ELLSLISTQS RLVITSSDNN TPVDSVLSSD SICINVSVDD IRVGDSLLVL 

       370        380        390        400        410        420 
PGETFPVDGS VLAGRSVVDE SMLTGESLPV FKEEGCSVSA GTINWDGPLR IKASSTGSNS 

       430        440        450        460        470        480 
TISKIVRMVE DAQGNAAPVQ RLADAIAGPF VYTIMSLSAM TFAFWYYVGS HIFPDVLLND 

       490        500        510        520        530        540 
IAGPDGDALA LSLKLAVDVL VVSCPCALGL ATPTAILIGT SLGAKRGYLI RGGDVLERLA 

       550        560        570        580        590        600 
SIDCVALDKT GTLTEGRPVV SGVASLGYEE QEVLKMAAAV EKTATHPIAK AIVNEAESLN 

       610        620        630        640        650        660 
LKTPETRGQL TEPGFGTLAE IDGRFVAVGS LEWVSDRFLK KNDSSDMVKL ESLLDHKLSN 

       670        680        690        700        710        720 
TSSTSRYSKT VVYVGREGEG IIGAIAISDC LRQDAEFTVA RLQEKGIKTV LLSGDREGAV 

       730        740        750        760        770        780 
ATVAKNVGIK SESTNYSLSP EKKFEFISNL QSSGHRVAMV GDGINDAPSL AQADVGIALK 

       790        800        810        820        830        840 
IEAQENAASN AASVILVRNK LSHVVDALSL AQATMSKVYQ NLAWAIAYNV ISIPIAAGVL 

       850        860        870        880 
LPQYDFAMTP SLSGGLMALS SIFVVSNSLL LQLHKSETSK NSL

« Hide

References

« Hide 'large scale' references
[1]"Two P-type ATPases are required for copper delivery in Arabidopsis thaliana chloroplasts."
Abdel-Ghany S.E., Muller-Moule P., Niyogi K.K., Pilon M., Shikanai T.
Plant Cell 17:1233-1251(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY297817 mRNA. Translation: AAP55720.1.
AC140977 Genomic DNA. Translation: AAO73891.1. Sequence problems.
AL589883 Genomic DNA. Translation: CAC34486.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED92956.1.
CP002688 Genomic DNA. Translation: AED92957.1.
AK316941 mRNA. Translation: BAH19644.1.
IPIIPI00520494.
RefSeqNP_001031920.1. NM_001036843.1.
NP_680181.2. NM_147876.4.
UniGeneAt.44341.

3D structure databases

ProteinModelPortalB9DFX7.
SMRB9DFX7. Positions 75-150, 216-872.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT5G21930.2-P.

Proteomic databases

PaxDbB9DFX7.
PRIDEB9DFX7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G21930.1; AT5G21930.1; AT5G21930.
AT5G21930.2; AT5G21930.2; AT5G21930.
GeneID832253.
KEGGath:AT5G21930.

Organism-specific databases

TAIRAt5g21930.

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250397.
OMAHDMDNMH.
PhylomeDBB9DFX7.
ProtClustDBCLSN2681230.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14496.

Gene expression databases

GenevestigatorB9DFX7.

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.
IPR023214. HAD-like_dom.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PANTHERPTHR24093. PTHR24093. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMA8_ARATH
AccessionPrimary (citable) accession number: B9DFX7
Secondary accession number(s): Q7Y051, Q9C594
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: March 24, 2009
Last modified: May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents