ID A0A453SPR4_AEGTS Unreviewed; 1060 AA.
AC A0A453SPR4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=P-type Zn(2+) transporter {ECO:0000256|ARBA:ARBA00039097};
DE EC=7.2.2.12 {ECO:0000256|ARBA:ARBA00039097};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET7Gv21017000.4, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET7Gv21017000.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC Evidence={ECO:0000256|ARBA:ARBA00035906};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR AlphaFoldDB; A0A453SPR4; -.
DR STRING; 200361.A0A453SPR4; -.
DR EnsemblPlants; AET7Gv21017000.4; AET7Gv21017000.4; AET7Gv21017000.
DR Gramene; AET7Gv21017000.4; AET7Gv21017000.4; AET7Gv21017000.
DR Proteomes; UP000015105; Chromosome 7D.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02079; P-type_ATPase_HM; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 382..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 714..736
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 47..113
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 756..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 115146 MW; 308A970888B03A5D CRC64;
LPAIIREAEG WRRQVRRAKK RERKSLATRR EGAMADSTSP AAAARLEKSY FDVLGICCPS
EVPLVEKLLE PLAGVHKVTV VVPSRTVIVL HDAAAISQAQ IVRALNGARL EASVRAYGGA
GQSKVSNKWP SPYVLVCGVL LVVSLFEHFW RPLRWFAVAG AAAGLPPIVL RSVAALRRRT
MDVNILMLIA VAGAIALKDY PEAGFIVFLF TIAEWLETRA CGKATAGMSS LMSMAPQNAV
LAETGQVVAT QDVKINTVIA VKAGEVVPID GVVVDGRSEV DESTLTGESF PVSKQADSQV
WAGTLNIDGY IAVRTTAMAD NSAVAKMARL VEEAQNSRSS TQRLIDTCAK YYTPAVIFMS
AAVAVIPVCV KARNLRHWFE LALVLLVSAC PCALVLSTPV ATFCALLRAA RTGLLIKGGD
VLESLASIKV AAFDKTGTIT RGEFSVEEFQ TVGERVSKQQ LIYWVSSIES RSSHPMASAL
VGYAQSNSVE PKSENVAEFQ IYPGEGIYGE IDGEGVYVGN KRILARASCQ TVPDIVEHMK
GVTIGYVACN KELIGVFSLS DSCRTGSAEA IKELRSLGIK SVMLTGDSTA AATHAQNQLG
NILAEVHAEL LPEDKVRIVD ELKARDGPTL MIGDGMNDAP ALAKADVGVS MGVSGSAVAM
ETSHITLMSN DIRRIPKAIK LARRTHRTIV VNIVFSVTTK LAIVGLAFAG HPLIWAAVLA
DVGTCLLVIM YSMLLLREKG SGKVVKKCCA SSHSKKHEHS TSHHHCSNDH QHDHVSAGKH
SCHDHHHEHD HHKEPSNLHS TDKHGCHDHH HEHDHHKEPS NLHSTDKHGC HDHGHGHSHC
KEPSSQMVTS KHVSHGHGHT HNICSPHPAV SKHDCHDHEH SHHQEPNSSH SADEHDCHDH
KHCEEPISLF CATEHACHDH EQNHEHHCCD EEQTVHVADT HSCHDHKHDD SAADPVPELS
ISIESALPDH HEQEIQCIKE HKEEACGHHL KVKDHVPAPT DCSRGNCHST VSSKGCESKG
KEVCSSWPVG RTGIIRRCCR TRARSCCSHS MLKLPEIIVE
//
