Q9M3H5 (AHM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic
EC=3.6.3.3
EC=3.6.3.5

Gene names

Name:	HMA1
Ordered Locus Names:	At4g37270
ORF Names:	C7A10.90, AP22.4

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	819 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cadmium/zinc transport Potential.
Catalytic activity	ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out). ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).
Subcellular location	Plastid › chloroplast inner membrane; Multi-pass membrane protein Potential Ref.6.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Ontologies

Keywords
Cellular component	Chloroplast Membrane Plastid Plastid inner membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	ATP-binding Cadmium Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro cellular copper ion homeostasis Inferred from mutant phenotype. Source: TAIR response to light intensity Inferred from mutant phenotype. Source: TAIR response to toxin Inferred from genetic interaction. Source: TAIR zinc ion homeostasis Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cadmium-exporting ATPase activity Inferred from electronic annotation. Source: EC cadmium-transporting ATPase activity Inferred from genetic interaction. Source: TAIR calcium-transporting ATPase activity Inferred from genetic interaction. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc transporting ATPase activity Inferred from direct assay. Source: TAIR zinc-exporting ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 17	17	Chloroplast Potential
	Chain	18 – 819	802	Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic		PRO_0000046398
Regions
	Topological domain	18 – 122	105	Stromal Potential
	Transmembrane	123 – 144	22	Helical; Potential
	Topological domain	145 – 153	9	Lumenal Potential
	Transmembrane	154 – 173	20	Helical; Potential
	Topological domain	174 – 180	7	Stromal Potential
	Transmembrane	181 – 201	21	Helical; Potential
	Topological domain	202	1	Lumenal Potential
	Transmembrane	203 – 223	21	Helical; Potential
	Topological domain	224 – 361	138	Stromal Potential
	Transmembrane	362 – 384	23	Helical; Potential
	Topological domain	385 – 398	14	Lumenal Potential
	Transmembrane	399 – 416	18	Helical; Potential
	Topological domain	417 – 737	321	Stromal Potential
	Transmembrane	738 – 757	20	Helical; Potential
	Topological domain	758 – 762	5	Lumenal Potential
	Transmembrane	763 – 781	19	Helical; Potential
	Topological domain	782 – 819	38	Stromal Potential
	Compositional bias	79 – 89	11	Poly-His
	Compositional bias	809 – 817	9	Poly-Ser
Sites
	Active site	453	1	4-aspartylphosphate intermediate By similarity
	Metal binding	682	1	Magnesium By similarity
	Metal binding	686	1	Magnesium By similarity
Natural variations
	Natural variant	53	1	N → S in strain: cv. Landsberg erecta.
	Natural variant	105	1	M → V in strain: cv. Landsberg erecta.
	Natural variant	659	1	P → S in strain: cv. Landsberg erecta.

Sequences

	Sequence		Length	Mass (Da)
	Q9M3H5 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: F281EA8F33C0ED52	FASTA	819	88,189
	10 20 30 40 50 60 MEPATLTRSS SLTRFPYRRG LSTLRLARVN SFSILPPKTL LRQKPLRISA SLNLPPRSIR 70 80 90 100 110 120 LRAVEDHHHD HHHDDEQDHH NHHHHHHQHG CCSVELKAES KPQKMLFGFA KAIGWVRLAN 130 140 150 160 170 180 YLREHLHLCC SAAAMFLAAA VCPYLAPEPY IKSLQNAFMI VGFPLVGVSA SLDALMDIAG 190 200 210 220 230 240 GKVNIHVLMA LAAFASVFMG NALEGGLLLA MFNLAHIAEE FFTSRSMVDV KELKESNPDS 250 260 270 280 290 300 ALLIEVHNGN VPNISDLSYK SVPVHSVEVG SYVLVGTGEI VPVDCEVYQG SATITIEHLT 310 320 330 340 350 360 GEVKPLEAKA GDRVPGGARN LDGRMIVKAT KAWNDSTLNK IVQLTEEAHS NKPKLQRWLD 370 380 390 400 410 420 EFGENYSKVV VVLSLAIAFL GPFLFKWPFL STAACRGSVY RALGLMVAAS PCALAVAPLA 430 440 450 460 470 480 YATAISSCAR KGILLKGAQV LDALASCHTI AFDKTGTLTT GGLTCKAIEP IYGHQGGTNS 490 500 510 520 530 540 SVITCCIPNC EKEALAVAAA MEKGTTHPIG RAVVDHSVGK DLPSIFVESF EYFPGRGLTA 550 560 570 580 590 600 TVNGVKTVAE ESRLRKASLG SIEFITSLFK SEDESKQIKD AVNASSYGKD FVHAALSVDQ 610 620 630 640 650 660 KVTLIHLEDQ PRPGVSGVIA ELKSWARLRV MMLTGDHDSS AWRVANAVGI TEVYCNLKPE 670 680 690 700 710 720 DKLNHVKNIA REAGGGLIMV GEGINDAPAL AAATVGIVLA QRASATAIAV ADILLLRDNI 730 740 750 760 770 780 TGVPFCVAKS RQTTSLVKQN VALALTSIFL AALPSVLGFV PLWLTVLLHE GGTLLVCLNS 790 800 810 VRGLNDPSWS WKQDIVHLIN KLRSQEPTSS SSNSLSSAH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a putative heavy metal P-type ATPase in Arabidopsis." Page S.L., Pittman J.K., Krijger G.C., Williams L.E. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"Functional characterization of AtHMA1." Mills R.F., Williams L.E. Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf and Root.
[3]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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. , 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.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana." Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N. Mol. Cell. Proteomics 2:325-345(2003) [PubMed: 12766230] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: cv. Wassilewskija.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ400906 mRNA. Translation: CAB90352.1. AJ872069 mRNA. Translation: CAI43274.1. Z99707 Genomic DNA. Translation: CAB16773.1. AL161591 Genomic DNA. Translation: CAB80393.1. CP002687 Genomic DNA. Translation: AEE86775.1.
IPI	IPI00521022.
PIR	D85440.
RefSeq	NP_195444.1. NM_119890.6.
UniGene	At.56989. At.74483.
3D structure databases
ProteinModelPortal	Q9M3H5.
SMR	Q9M3H5. Positions 145-790.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9M3H5.
Protein family/group databases
TCDB	3.A.3.6.6. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PRIDE	Q9M3H5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G37270.1; AT4G37270.1; AT4G37270.
GeneID	829881.
GenomeReviews	Gene locus AT4G37270 in contig CT486007_GR.
KEGG	ath:AT4G37270.
NMPDR	fig|3702.1.peg.21837.
Organism-specific databases
TAIR	At4g37270.
Phylogenomic databases
GeneTree	EPGT00070000030920.
HOGENOM	HBG507745.
InParanoid	Q9M3H5.
OMA	FKSEDES.
PhylomeDB	Q9M3H5.
ProtClustDB	CLSN2685780.
Gene expression databases
ArrayExpress	Q9M3H5.
Genevestigator	Q9M3H5.
GermOnline	AT4G37270. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AHM1_ARATH

Accession

Primary (citable) accession number: Q9M3H5
Secondary accession number(s): Q5JZZ1, Q9SW66

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	November 16, 2011
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program