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Copper-transporting ATPase PAA1, chloroplastic (EC 3.6.3.54) (Protein HEAVY METAL ATPASE 6) (Protein glucose insensitive root 1)

 HMA6_ARATH              Reviewed;         949 AA.
Q9SZC9; O48600; O81870; Q0WPL5; Q93YP5;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=Copper-transporting ATPase PAA1, chloroplastic;
EC=3.6.3.54;
AltName: Full=Protein HEAVY METAL ATPASE 6;
AltName: Full=Protein glucose insensitive root 1;
Flags: Precursor;
Name=PAA1; Synonyms=GIR1, HMA6; OrderedLocusNames=At4g33520;
ORFNames=F17M5.280, T16L1.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Landsberg erecta;
PubMed=9188794; DOI=10.1016/S0005-2736(97)00064-3;
Tabata K., Kashiwagi S., Mori H., Ueguchi C., Mizuno T.;
"Cloning of a cDNA encoding a putative metal-transporting P-type
ATPase from Arabidopsis thaliana.";
Biochim. Biophys. Acta 1326:1-6(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=12782727; DOI=10.1105/tpc.011817;
Shikanai T., Muller-Moule P., Munekage Y., Niyogi K.K., Pilon M.;
"PAA1, a P-type ATPase of Arabidopsis, functions in copper transport
in chloroplasts.";
Plant Cell 15:1333-1346(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15772282; DOI=10.1105/tpc.104.030452;
Abdel-Ghany S.E., Muller-Moule P., Niyogi K.K., Pilon M., Shikanai T.;
"Two P-type ATPases are required for copper delivery in Arabidopsis
thaliana chloroplasts.";
Plant Cell 17:1233-1251(2005).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
Lee S.A., Chang K.S., Hwang I., Cheong H., Lim J.;
"Analysis of gir1 (glucose insensitive root 1) reveals that a role of
the chloroplastic copper transporter paa1 in sugar signaling.";
(In) Proceedings of the 21st international conference on Arabidopsis
research, abstract#08115, Yokohama (2010).
[9]
FUNCTION.
PubMed=21878617; DOI=10.1074/jbc.M111.241034;
Catty P., Boutigny S., Miras R., Joyard J., Rolland N.,
Seigneurin-Berny D.;
"Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope
Cu(I)-ATPase.";
J. Biol. Chem. 286:36188-36197(2011).
-!- FUNCTION: Mediates copper transfer across the plastid envelope.
Required for the delivery of copper into the plastid stroma, which
is essential for the function of copper proteins. Seems to be
selective for monovalent copper Cu(+) transport. Plays also a role
in glucose signaling-mediated cell proliferation of root meristem
in non-green tissues. {ECO:0000269|PubMed:12782727,
ECO:0000269|PubMed:15772282, ECO:0000269|PubMed:21878617,
ECO:0000269|Ref.8}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2).
-!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
{ECO:0000269|PubMed:12782727, ECO:0000269|PubMed:15772282}; Multi-
pass membrane protein {ECO:0000269|PubMed:12782727,
ECO:0000269|PubMed:15772282}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9SZC9-1; Sequence=Displayed;
Name=2;
IsoId=Q9SZC9-2; Sequence=VSP_040517, VSP_040518;
-!- TISSUE SPECIFICITY: Expressed in the shoots and roots.
{ECO:0000269|PubMed:15772282}.
-!- DISRUPTION PHENOTYPE: High-chlorophyll-fluorescence phenotype.
Short roots. {ECO:0000269|PubMed:12782727, ECO:0000269|Ref.8}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D89981; BAA23769.1; -; mRNA.
EMBL; AL031394; CAA20565.1; -; Genomic_DNA.
EMBL; AL035678; CAB38810.1; -; Genomic_DNA.
EMBL; AL161583; CAB80069.1; -; Genomic_DNA.
EMBL; CP002687; AEE86239.1; -; Genomic_DNA.
EMBL; CP002687; AEE86240.1; -; Genomic_DNA.
EMBL; AY059869; AAL24351.1; -; mRNA.
EMBL; AY093320; AAM13319.1; -; mRNA.
EMBL; AK229051; BAF00934.1; -; mRNA.
PIR; T06003; T06003.
RefSeq; NP_567924.1; NM_119506.4. [Q9SZC9-2]
RefSeq; NP_974675.1; NM_202946.3. [Q9SZC9-1]
UniGene; At.48932; -.
PDB; 5LBD; X-ray; 1.50 A; A/B=607-734.
PDBsum; 5LBD; -.
ProteinModelPortal; Q9SZC9; -.
SMR; Q9SZC9; -.
BioGrid; 14774; 4.
IntAct; Q9SZC9; 2.
MINT; MINT-8061569; -.
STRING; 3702.AT4G33520.2; -.
TCDB; 3.A.3.5.11; the p-type atpase (p-atpase) superfamily.
PaxDb; Q9SZC9; -.
PRIDE; Q9SZC9; -.
EnsemblPlants; AT4G33520.1; AT4G33520.1; AT4G33520. [Q9SZC9-2]
EnsemblPlants; AT4G33520.2; AT4G33520.2; AT4G33520. [Q9SZC9-1]
GeneID; 829490; -.
Gramene; AT4G33520.1; AT4G33520.1; AT4G33520.
Gramene; AT4G33520.2; AT4G33520.2; AT4G33520.
KEGG; ath:AT4G33520; -.
Araport; AT4G33520; -.
TAIR; locus:2119265; AT4G33520.
eggNOG; KOG0207; Eukaryota.
eggNOG; COG2217; LUCA.
HOGENOM; HOG000250397; -.
InParanoid; Q9SZC9; -.
KO; K01533; -.
OMA; TEVPCDT; -.
PhylomeDB; Q9SZC9; -.
BioCyc; ARA:AT4G33520-MONOMER; -.
BioCyc; MetaCyc:MONOMER-14495; -.
BRENDA; 3.6.3.4; 399.
PRO; PR:Q9SZC9; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SZC9; baseline and differential.
Genevisible; Q9SZC9; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
GO; GO:0016531; F:copper chaperone activity; IDA:TAIR.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:TAIR.
GO; GO:0055070; P:copper ion homeostasis; IDA:TAIR.
GO; GO:0035434; P:copper ion transmembrane transport; IMP:UniProtKB.
GO; GO:0009767; P:photosynthetic electron transport chain; IMP:UniProtKB.
CDD; cd00371; HMA; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 1.
SUPFAM; SSF55008; SSF55008; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 1.
PROSITE; PS50846; HMA_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Chloroplast;
Complete proteome; Copper; Copper transport; Hydrolase; Ion transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Plastid;
Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 103 Chloroplast. {ECO:0000255}.
CHAIN 104 949 Copper-transporting ATPase PAA1,
chloroplastic.
/FTId=PRO_0000046403.
TRANSMEM 253 274 Helical. {ECO:0000255}.
TRANSMEM 287 306 Helical. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TRANSMEM 349 369 Helical. {ECO:0000255}.
TRANSMEM 502 524 Helical. {ECO:0000255}.
TRANSMEM 543 560 Helical. {ECO:0000255}.
TRANSMEM 863 882 Helical. {ECO:0000255}.
TRANSMEM 895 913 Helical. {ECO:0000255}.
DOMAIN 149 223 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
NP_BIND 807 814 ATP. {ECO:0000255}.
COMPBIAS 115 124 Poly-Gly.
ACT_SITE 598 598 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 159 159 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 162 162 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 808 808 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 812 812 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
VAR_SEQ 225 237 DLVTENFFKVFET -> GEVPEDIAGEFAP (in
isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_040517.
VAR_SEQ 238 949 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_040518.
VARIANT 215 215 T -> S (in strain: cv. Landsberg erecta).
VARIANT 238 239 KT -> QP (in strain: cv. Landsberg
erecta).
VARIANT 259 259 L -> P (in strain: cv. Landsberg erecta).
VARIANT 384 384 P -> A (in strain: cv. Landsberg erecta).
VARIANT 904 904 S -> T (in strain: cv. Landsberg erecta).
SEQUENCE 949 AA; 99997 MW; 716F5E6E63B7F9B8 CRC64;
MESTLSAFST VKATAMARSS GGPSLPLLTI SKALNRHFTG ARHLHPLLLA RCSPSVRRLG
GFHGSRFTSS NSALRSLGAA VLPVIRHRLE CLSSSSPSFR SISSGGGSGF GGYNGGSGGG
GGGGSESGDS KSKLGANASD GVSVPSSDII ILDVGGMTCG GCSASVKKIL ESQPQVASAS
VNLTTETAIV WPVPEAKSVP DWQKSLGETL ANHLTNCGFQ STPRDLVTEN FFKVFETKTK
DKQARLKESG RELAVSWALC AVCLVGHLTH FLGVNAPWIH AIHSTGFHVS LCLITLLGPG
RKLVLDGIKS LLKGSPNMNT LVGLGALSSF SVSSLAAMIP KLGWKTFFEE PVMLIAFVLL
GRNLEQRAKI KATSDMTGLL SVLPSKARLL LDGDLQNSTV EVPCNSLSVG DLVVILPGDR
VPADGVVKSG RSTIDESSFT GEPLPVTKES GSQVAAGSIN LNGTLTVEVH RSGGETAVGD
IIRLVEEAQS REAPVQQLVD KVAGRFTYGV MALSAATFTF WNLFGAHVLP SALHNGSPMS
LALQLSCSVL VVACPCALGL ATPTAMLVGT SLGARRGLLL RGGDILEKFS LVDTVVFDKT
GTLTKGHPVV TEVIIPENPR HNLNDTWSEV EVLMLAAAVE SNTTHPVGKA IVKAARARNC
QTMKAEDGTF TEEPGSGAVA IVNNKRVTVG TLEWVKRHGA TGNSLLALEE HEINNQSVVY
IGVDNTLAAV IRFEDKVRED AAQVVENLTR QGIDVYMLSG DKRNAANYVA SVVGINHERV
IAGVKPAEKK NFINELQKNK KIVAMVGDGI NDAAALASSN VGVAMGGGAG AASEVSPVVL
MGNRLTQLLD AMELSRQTMK TVKQNLWWAF GYNIVGIPIA AGVLLPLTGT MLTPSMAGAL
MGVSSLGVMT NSLLLRYRFF SNRNDKNVKP EPKEGTKQPH ENTRWKQSS


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