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B9DFX7

- HMA8_ARATH

UniProt

B9DFX7 - HMA8_ARATH

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Protein
Copper-transporting ATPase PAA2, chloroplastic
Gene
PAA2, HMA8, At5g21930, F13M11, T6G21
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + H2O + Cu2+(Side 1) = ADP + phosphate + Cu2+(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Copper Reviewed prediction
Metal bindingi90 – 901Copper Reviewed prediction
Active sitei548 – 54814-aspartylphosphate intermediate By similarity
Metal bindingi762 – 7621Magnesium By similarity
Metal bindingi766 – 7661Magnesium By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi761 – 7688ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. copper ion transmembrane transporter activity Source: TAIR
  3. copper-exporting ATPase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. copper ion transmembrane transport Source: GOC
  2. copper ion transport Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciARA:AT5G21930-MONOMER.
ARA:GQT-886-MONOMER.
MetaCyc:MONOMER-14496.

Protein family/group databases

TCDBi3.A.3.5.12. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-transporting ATPase PAA2, chloroplastic (EC:3.6.3.4)
Alternative name(s):
Protein HEAVY METAL ATPASE 8
Gene namesi
Name:PAA2
Synonyms:HMA8
Ordered Locus Names:At5g21930
ORF Names:F13M11, T6G21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G21930.

Subcellular locationi

Plastidchloroplast thylakoid membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei179 – 19921Helical; Reviewed prediction
Add
BLAST
Transmembranei209 – 22921Helical; Reviewed prediction
Add
BLAST
Transmembranei250 – 27021Helical; Reviewed prediction
Add
BLAST
Transmembranei274 – 29421Helical; Reviewed prediction
Add
BLAST
Transmembranei445 – 46521Helical; Reviewed prediction
Add
BLAST
Transmembranei499 – 51921Helical; Reviewed prediction
Add
BLAST
Transmembranei822 – 84221Helical; Reviewed prediction
Add
BLAST
Transmembranei846 – 86621Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. chloroplast thylakoid membrane Source: TAIR
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

High-chlorophyll-fluorescence phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565Chloroplast Reviewed prediction
Add
BLAST
Chaini66 – 883818Copper-transporting ATPase PAA2, chloroplastic
PRO_0000416858Add
BLAST

Proteomic databases

PaxDbiB9DFX7.
PRIDEiB9DFX7.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriB9DFX7.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G21930.2-P.

Structurei

3D structure databases

ProteinModelPortaliB9DFX7.
SMRiB9DFX7. Positions 216-872.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 14771HMA
Add
BLAST

Sequence similaritiesi

Contains 1 HMA domain.

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2217.
HOGENOMiHOG000250397.
KOiK01533.
OMAiHDMDNMH.
PhylomeDBiB9DFX7.

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.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: B9DFX7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MASNLLRFPL PPPSSLHIRP SKFLVNRCFP RLRRSRIRRH CSRPFFLVSN    50
SVEISTQSFE STESSIESVK SITSDTPILL DVSGMMCGGC VARVKSVLMS 100
DDRVASAVVN MLTETAAVKF KPEVEVTADT AESLAKRLTE SGFEAKRRVS 150
GMGVAENVKK WKEMVSKKED LLVKSRNRVA FAWTLVALCC GSHTSHILHS 200
LGIHIAHGGI WDLLHNSYVK GGLAVGALLG PGRELLFDGI KAFGKRSPNM 250
NSLVGLGSMA AFSISLISLV NPELEWDASF FDEPVMLLGF VLLGRSLEER 300
AKLQASTDMN ELLSLISTQS RLVITSSDNN TPVDSVLSSD SICINVSVDD 350
IRVGDSLLVL PGETFPVDGS VLAGRSVVDE SMLTGESLPV FKEEGCSVSA 400
GTINWDGPLR IKASSTGSNS TISKIVRMVE DAQGNAAPVQ RLADAIAGPF 450
VYTIMSLSAM TFAFWYYVGS HIFPDVLLND IAGPDGDALA LSLKLAVDVL 500
VVSCPCALGL ATPTAILIGT SLGAKRGYLI RGGDVLERLA SIDCVALDKT 550
GTLTEGRPVV SGVASLGYEE QEVLKMAAAV EKTATHPIAK AIVNEAESLN 600
LKTPETRGQL TEPGFGTLAE IDGRFVAVGS LEWVSDRFLK KNDSSDMVKL 650
ESLLDHKLSN TSSTSRYSKT VVYVGREGEG IIGAIAISDC LRQDAEFTVA 700
RLQEKGIKTV LLSGDREGAV ATVAKNVGIK SESTNYSLSP EKKFEFISNL 750
QSSGHRVAMV GDGINDAPSL AQADVGIALK IEAQENAASN AASVILVRNK 800
LSHVVDALSL AQATMSKVYQ NLAWAIAYNV ISIPIAAGVL LPQYDFAMTP 850
SLSGGLMALS SIFVVSNSLL LQLHKSETSK NSL 883
Length:883
Mass (Da):94,260
Last modified:March 24, 2009 - v1
Checksum:iF5E365AB6B7A90C3
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121L → P in AAP55720. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001031920.1. NM_001036843.1. [B9DFX7-1]
NP_680181.2. NM_147876.4. [B9DFX7-1]
UniGeneiAt.44341.

Genome annotation databases

EnsemblPlantsiAT5G21930.1; AT5G21930.1; AT5G21930. [B9DFX7-1]
AT5G21930.2; AT5G21930.2; AT5G21930. [B9DFX7-1]
GeneIDi832253.
KEGGiath:AT5G21930.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001031920.1. NM_001036843.1. [B9DFX7-1 ]
NP_680181.2. NM_147876.4. [B9DFX7-1 ]
UniGenei At.44341.

3D structure databases

ProteinModelPortali B9DFX7.
SMRi B9DFX7. Positions 216-872.
ModBasei Search...

Protein-protein interaction databases

STRINGi 3702.AT5G21930.2-P.

Protein family/group databases

TCDBi 3.A.3.5.12. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbi B9DFX7.
PRIDEi B9DFX7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G21930.1 ; AT5G21930.1 ; AT5G21930 . [B9DFX7-1 ]
AT5G21930.2 ; AT5G21930.2 ; AT5G21930 . [B9DFX7-1 ]
GeneIDi 832253.
KEGGi ath:AT5G21930.

Organism-specific databases

TAIRi AT5G21930.

Phylogenomic databases

eggNOGi COG2217.
HOGENOMi HOG000250397.
KOi K01533.
OMAi HDMDNMH.
PhylomeDBi B9DFX7.

Enzyme and pathway databases

BioCyci ARA:AT5G21930-MONOMER.
ARA:GQT-886-MONOMER.
MetaCyc:MONOMER-14496.

Gene expression databases

Genevestigatori B9DFX7.

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.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view ]
Pfami PF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SUPFAMi SSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHMA8_ARATH
AccessioniPrimary (citable) accession number: B9DFX7
Secondary accession number(s): Q7Y051, Q9C594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: March 24, 2009
Last modified: June 11, 2014
This is version 51 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi