ATXA_LEIDO
ID ATXA_LEIDO Reviewed; 974 AA.
AC P11718;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable proton ATPase 1A;
DE EC=7.1.2.1;
DE AltName: Full=LdH1A;
GN Name=H1A;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2828921; DOI=10.1128/mcb.7.11.3937-3946.1987;
RA Meade J.C., Shaw J., Lemaster S., Gallagher G., Stringer J.R.;
RT "Structure and expression of a tandem gene pair in Leishmania donovani that
RT encodes a protein structurally homologous to eucaryotic cation-transporting
RT ATPases.";
RL Mol. Cell. Biol. 7:3937-3946(1987).
RN [2]
RP SEQUENCE REVISION TO 55-56, AND DEVELOPMENTAL STAGE.
RC STRAIN=MHOM/ET/67/L82;
RX PubMed=2469011; DOI=10.1016/0166-6851(89)90045-5;
RA Meade J.C., Hudson K.M., Stringer S.L., Stringer J.R.;
RT "A tandem pair of Leishmania donovani cation transporting ATPase genes
RT encode isoforms that are differentially expressed.";
RL Mol. Biochem. Parasitol. 33:81-91(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: More abundant in promastigotes than amastigotes.
CC {ECO:0000269|PubMed:2469011}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
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DR EMBL; AF109296; AAA29227.2; -; Genomic_DNA.
DR PIR; A27124; PXLNPD.
DR AlphaFoldDB; P11718; -.
DR SMR; P11718; -.
DR TCDB; 3.A.3.3.2; the p-type atpase (p-atpase) superfamily.
DR PRIDE; P11718; -.
DR VEuPathDB; TriTrypDB:LdBPK_181510.1; -.
DR VEuPathDB; TriTrypDB:LdCL_180020300; -.
DR VEuPathDB; TriTrypDB:LDHU3_18.1890; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..974
FT /note="Probable proton ATPase 1A"
FT /id="PRO_0000046180"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..112
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..137
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..286
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..321
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..661
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..684
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..712
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..737
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..761
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..812
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..840
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..868
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..887
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 888..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 974 AA; 107479 MW; 6BAB38F5153928A0 CRC64;
MSSKKYELDA AAFEDKPESH SDAEMTPQKP QRRQSVLSKA VSEHDERATG PATDLLPPSK
GLTTEEAEEL LKKYGRNELP EKKTPSWLIY VRGLWGPMPA ALWIAIIIEF ALENWPDGAI
LFAIQIANAT IGWYETIKAG DAVAALKNSL KPTATVYRDS KWQQIDAAVL VPGDLVKLAS
GSAVPADCSI NEGVIDVDEA ALTGESLPVT MGPEHMPKMG SNVVRGEVEG TVQYTGSLTF
FGKTAALLQS VESDLGNIHV ILRRVMFSLC AISFMLCMCC FIYLLARFYE TFRHALQFAV
VVLVVSIPIA LEIVVTTTLA VGSKHLSKHK IIVTKLSAIE MMSGVNMLCS DKTGTLTLNK
MEIQEQCFTF EEGNDLKSTL VLAALAAKWR EPPRDALDTM VLGAADLDEC DNYQQLNFVP
FDPTTKRTAA TLVDRRSGEK FDVTKGAPHV ILQMVYNQDE INDEVVDIID SLAARGVRCL
SVAKTDQQGR WHMAGILTFL DPPRPDTKDT IRRSKEYGVD VKMITGDHLL IAKEMCRMLD
LDPNILTADK LPQIKDANDL PEDLGEKYGD MMLSVGGFAQ VFPEHKFMIV ETLRQRGYTC
AMTGDGVNDA PALKRADVGI AVHGATDAAR AAADMVLTEP GLSVVVEAML VSREVFQRML
SFLTYRISAT LQLVCFFFIA CFSLTPKAYG SVDPHFQFFH LPVLMFMLIT LLNDGCLMTI
GYDHVIPSER PQKWNLPVVF VSASILAAVA CGSSLMLLWI GLEGYSSQYY ENSWFHRLGL
AQLPQGKLVT MMYLKISISD FLTLFSSRTG GHFFFYMPPS PILFCGAIIS LLVSTMAASF
WHKSRPDNVL TEGLAWGQTN AEKLLPLWVW IYCIVWWFVQ DVVKVLAHIC MDAVDLFGCV
SDASGSGPIK PYSDDMKVNG FEPVKKPAEK STEKALNSSV SSASHKALEG LREDTHSPIE
EASPVNVYVS RDQK
