HMA8_ARATH
ID HMA8_ARATH Reviewed; 883 AA.
AC B9DFX7; Q7Y051; Q9C594;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Copper-transporting ATPase PAA2, chloroplastic;
DE EC=7.2.2.9;
DE AltName: Full=Protein HEAVY METAL ATPASE 8;
DE Flags: Precursor;
GN Name=PAA2; Synonyms=HMA8; OrderedLocusNames=At5g21930;
GN ORFNames=F13M11, T6G21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15772282; DOI=10.1105/tpc.104.030452;
RA Abdel-Ghany S.E., Muller-Moule P., Niyogi K.K., Pilon M., Shikanai T.;
RT "Two P-type ATPases are required for copper delivery in Arabidopsis
RT thaliana chloroplasts.";
RL Plant Cell 17:1233-1251(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
CC -!- FUNCTION: Mediates copper transfer across the chloroplast thylakoid
CC membrane. Required for copper delivery into the thylakoids lumen, which
CC is essential for the function of copper proteins.
CC {ECO:0000269|PubMed:15772282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.9;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:15772282}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15772282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=B9DFX7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the shoots only and not in the roots.
CC {ECO:0000269|PubMed:15772282}.
CC -!- DISRUPTION PHENOTYPE: High-chlorophyll-fluorescence phenotype.
CC {ECO:0000269|PubMed:15772282}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO73891.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC34486.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY297817; AAP55720.1; -; mRNA.
DR EMBL; AC140977; AAO73891.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL589883; CAC34486.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92956.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92957.1; -; Genomic_DNA.
DR EMBL; AK316941; BAH19644.1; -; mRNA.
DR RefSeq; NP_001031920.1; NM_001036843.1. [B9DFX7-1]
DR RefSeq; NP_680181.2; NM_147876.5. [B9DFX7-1]
DR PDB; 5LBK; X-ray; 1.75 A; A/B=557-689.
DR PDBsum; 5LBK; -.
DR AlphaFoldDB; B9DFX7; -.
DR SMR; B9DFX7; -.
DR STRING; 3702.AT5G21930.2; -.
DR TCDB; 3.A.3.5.12; the p-type atpase (p-atpase) superfamily.
DR PaxDb; B9DFX7; -.
DR ProteomicsDB; 230256; -. [B9DFX7-1]
DR EnsemblPlants; AT5G21930.1; AT5G21930.1; AT5G21930. [B9DFX7-1]
DR EnsemblPlants; AT5G21930.2; AT5G21930.2; AT5G21930. [B9DFX7-1]
DR GeneID; 832253; -.
DR Gramene; AT5G21930.1; AT5G21930.1; AT5G21930. [B9DFX7-1]
DR Gramene; AT5G21930.2; AT5G21930.2; AT5G21930. [B9DFX7-1]
DR KEGG; ath:AT5G21930; -.
DR Araport; AT5G21930; -.
DR TAIR; locus:504956435; AT5G21930.
DR eggNOG; KOG0207; Eukaryota.
DR InParanoid; B9DFX7; -.
DR OMA; MALEPMG; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; B9DFX7; -.
DR BioCyc; ARA:MON-14496; -.
DR BioCyc; MetaCyc:MON-14496; -.
DR BRENDA; 7.2.2.9; 399.
DR PRO; PR:B9DFX7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DFX7; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006825; P:copper ion transport; IMP:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chloroplast; Copper;
KW Copper transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..883
FT /note="Copper-transporting ATPase PAA2, chloroplastic"
FT /id="PRO_0000416858"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 76..146
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 548
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 761..768
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CONFLICT 312
FT /note="L -> P (in Ref. 1; AAP55720)"
FT /evidence="ECO:0000305"
FT STRAND 559..568
FT /evidence="ECO:0007829|PDB:5LBK"
FT HELIX 570..580
FT /evidence="ECO:0007829|PDB:5LBK"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:5LBK"
FT HELIX 587..598
FT /evidence="ECO:0007829|PDB:5LBK"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:5LBK"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:5LBK"
FT STRAND 616..621
FT /evidence="ECO:0007829|PDB:5LBK"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:5LBK"
FT HELIX 631..637
FT /evidence="ECO:0007829|PDB:5LBK"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:5LBK"
FT STRAND 670..676
FT /evidence="ECO:0007829|PDB:5LBK"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:5LBK"
FT STRAND 680..688
FT /evidence="ECO:0007829|PDB:5LBK"
SQ SEQUENCE 883 AA; 94260 MW; F5E365AB6B7A90C3 CRC64;
MASNLLRFPL PPPSSLHIRP SKFLVNRCFP RLRRSRIRRH CSRPFFLVSN SVEISTQSFE
STESSIESVK SITSDTPILL DVSGMMCGGC VARVKSVLMS DDRVASAVVN MLTETAAVKF
KPEVEVTADT AESLAKRLTE SGFEAKRRVS GMGVAENVKK WKEMVSKKED LLVKSRNRVA
FAWTLVALCC GSHTSHILHS LGIHIAHGGI WDLLHNSYVK GGLAVGALLG PGRELLFDGI
KAFGKRSPNM NSLVGLGSMA AFSISLISLV NPELEWDASF FDEPVMLLGF VLLGRSLEER
AKLQASTDMN ELLSLISTQS RLVITSSDNN TPVDSVLSSD SICINVSVDD IRVGDSLLVL
PGETFPVDGS VLAGRSVVDE SMLTGESLPV FKEEGCSVSA GTINWDGPLR IKASSTGSNS
TISKIVRMVE DAQGNAAPVQ RLADAIAGPF VYTIMSLSAM TFAFWYYVGS HIFPDVLLND
IAGPDGDALA LSLKLAVDVL VVSCPCALGL ATPTAILIGT SLGAKRGYLI RGGDVLERLA
SIDCVALDKT GTLTEGRPVV SGVASLGYEE QEVLKMAAAV EKTATHPIAK AIVNEAESLN
LKTPETRGQL TEPGFGTLAE IDGRFVAVGS LEWVSDRFLK KNDSSDMVKL ESLLDHKLSN
TSSTSRYSKT VVYVGREGEG IIGAIAISDC LRQDAEFTVA RLQEKGIKTV LLSGDREGAV
ATVAKNVGIK SESTNYSLSP EKKFEFISNL QSSGHRVAMV GDGINDAPSL AQADVGIALK
IEAQENAASN AASVILVRNK LSHVVDALSL AQATMSKVYQ NLAWAIAYNV ISIPIAAGVL
LPQYDFAMTP SLSGGLMALS SIFVVSNSLL LQLHKSETSK NSL
