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Reviewed, UniProtKB/Swiss-Prot Q9SZC9 (AHM6_ARATH)

Last modified October 13, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative copper-transporting ATPase PAA1
    EC=3.6.3.4
Gene names
Name: PAA1
Ordered Locus Names: At4g33520
ORF Names: T16L1.10, F17M5.280
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length949 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in copper transport Potential.

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IB subfamily.

Contains 1 HMA domain.

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: Q9SZC9-1)

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

Chain1 – 949949Putative copper-transporting ATPase PAA1
PRO_0000046403

Regions

Topological domain1 – 252252Cytoplasmic Potential
Transmembrane253 – 27422 Potential
Topological domain275 – 28612Extracellular Potential
Transmembrane287 – 30620 Potential
Topological domain307 – 3137Cytoplasmic Potential
Transmembrane314 – 33421 Potential
Topological domain335 – 34814Extracellular Potential
Transmembrane349 – 36921 Potential
Topological domain370 – 501132Cytoplasmic Potential
Transmembrane502 – 52423 Potential
Topological domain525 – 54218Extracellular Potential
Transmembrane543 – 56018 Potential
Topological domain561 – 862302Cytoplasmic Potential
Transmembrane863 – 88220 Potential
Topological domain883 – 89412Extracellular Potential
Transmembrane895 – 91319 Potential
Topological domain914 – 94936Cytoplasmic Potential
Domain149 – 22375HMA
Compositional bias115 – 12410Poly-Gly

Sites

Active site59814-aspartylphosphate intermediate By similarity
Metal binding1591Copper Potential
Metal binding1621Copper Potential
Metal binding8081Magnesium By similarity
Metal binding8121Magnesium By similarity

Natural variations

Natural variant2151T → S in strain: cv. Landsberg erecta.
Natural variant238 – 2392KT → QP in strain: cv. Landsberg erecta.
Natural variant2591L → P in strain: cv. Landsberg erecta.
Natural variant3841P → A in strain: cv. Landsberg erecta.
Natural variant9041S → T in strain: cv. Landsberg erecta.

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 716F5E6E63B7F9B8

FASTA94999,997
        10         20         30         40         50         60 
MESTLSAFST VKATAMARSS GGPSLPLLTI SKALNRHFTG ARHLHPLLLA RCSPSVRRLG 

        70         80         90        100        110        120 
GFHGSRFTSS NSALRSLGAA VLPVIRHRLE CLSSSSPSFR SISSGGGSGF GGYNGGSGGG 

       130        140        150        160        170        180 
GGGGSESGDS KSKLGANASD GVSVPSSDII ILDVGGMTCG GCSASVKKIL ESQPQVASAS 

       190        200        210        220        230        240 
VNLTTETAIV WPVPEAKSVP DWQKSLGETL ANHLTNCGFQ STPRDLVTEN FFKVFETKTK 

       250        260        270        280        290        300 
DKQARLKESG RELAVSWALC AVCLVGHLTH FLGVNAPWIH AIHSTGFHVS LCLITLLGPG 

       310        320        330        340        350        360 
RKLVLDGIKS LLKGSPNMNT LVGLGALSSF SVSSLAAMIP KLGWKTFFEE PVMLIAFVLL 

       370        380        390        400        410        420 
GRNLEQRAKI KATSDMTGLL SVLPSKARLL LDGDLQNSTV EVPCNSLSVG DLVVILPGDR 

       430        440        450        460        470        480 
VPADGVVKSG RSTIDESSFT GEPLPVTKES GSQVAAGSIN LNGTLTVEVH RSGGETAVGD 

       490        500        510        520        530        540 
IIRLVEEAQS REAPVQQLVD KVAGRFTYGV MALSAATFTF WNLFGAHVLP SALHNGSPMS 

       550        560        570        580        590        600 
LALQLSCSVL VVACPCALGL ATPTAMLVGT SLGARRGLLL RGGDILEKFS LVDTVVFDKT 

       610        620        630        640        650        660 
GTLTKGHPVV TEVIIPENPR HNLNDTWSEV EVLMLAAAVE SNTTHPVGKA IVKAARARNC 

       670        680        690        700        710        720 
QTMKAEDGTF TEEPGSGAVA IVNNKRVTVG TLEWVKRHGA TGNSLLALEE HEINNQSVVY 

       730        740        750        760        770        780 
IGVDNTLAAV IRFEDKVRED AAQVVENLTR QGIDVYMLSG DKRNAANYVA SVVGINHERV 

       790        800        810        820        830        840 
IAGVKPAEKK NFINELQKNK KIVAMVGDGI NDAAALASSN VGVAMGGGAG AASEVSPVVL 

       850        860        870        880        890        900 
MGNRLTQLLD AMELSRQTMK TVKQNLWWAF GYNIVGIPIA AGVLLPLTGT MLTPSMAGAL 

       910        920        930        940 
MGVSSLGVMT NSLLLRYRFF SNRNDKNVKP EPKEGTKQPH ENTRWKQSS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a cDNA encoding a putative metal-transporting P-type ATPase from Arabidopsis thaliana."
Tabata K., Kashiwagi S., Mori H., Ueguchi C., Mizuno T.
Biochim. Biophys. Acta 1326:1-6(1997) [PubMed: 9188794] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

D89981 mRNA. Translation: BAA23769.1.
AL035678 Genomic DNA. Translation: CAB38810.1.
AL161583 Genomic DNA. Translation: CAB80069.1.
AL031394 Genomic DNA. Translation: CAA20565.1.
IPIIPI00541571.
PIRT06003.
RefSeqNP_974675.1.
UniGeneAt.48932

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB3.A.3.5.11. P-type ATPase (P-ATPase) superfamily.

Proteomic databases

PRIDEQ9SZC9.

Genome annotation databases

GeneID829490.
GenomeReviewsGene locus AT4G33520 in contig CT486007_GR.
NMPDRfig|3702.1.peg.21396.

Organism-specific databases

TAIRAt4g33520.

Enzyme and pathway databases

BRENDA3.6.3.4. 302.

Gene expression databases

GenevestigatorQ9SZC9.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-reg.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe_transpt.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAHM6_ARATH
AccessionPrimary (citable) accession number: Q9SZC9
Secondary accession number(s): O48600, O81870
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: October 13, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents