ID V4A4M8_LOTGI Unreviewed; 859 AA.
AC V4A4M8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=LOTGIDRAFT_218380 {ECO:0000313|EMBL:ESO89930.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO89930.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO89930.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362082}.
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DR EMBL; KB202518; ESO89930.1; -; Genomic_DNA.
DR RefSeq; XP_009059403.1; XM_009061155.1.
DR AlphaFoldDB; V4A4M8; -.
DR STRING; 225164.V4A4M8; -.
DR EnsemblMetazoa; LotgiT218380; LotgiP218380; LotgiG218380.
DR GeneID; 20246781; -.
DR KEGG; lgi:LOTGIDRAFT_218380; -.
DR CTD; 20246781; -.
DR HOGENOM; CLU_001828_0_3_1; -.
DR OMA; WHYTENP; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 430..457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 154..226
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 859 AA; 96696 MW; B9B6CC50A842B191 CRC64;
MNHPTDSTDQ SGALKNILLT KITLNKGTED ELECYAYKTD PVKNVIFILL VLLTGGLLLL
LLYWKPELEC YLRRGRCPLY KAKFILVEDH VGEYSTTTVQ TGLSEHQQGN YSGHSVVDND
ENRFLISNND ITLRYFDFHN VRYIWDKNQH VYCRLGDLST NVKCAELHDQ YNGLTSLQQA
EQLDIHGPNV IDIKVKSYWR LFIEEVLNPF YIFQIASIIL WAIDEYYYYA GCIFFISLVS
ISISLYETRK QSVTLRDMVS TVVDKISVCR GDNEYEEIPS SQLVPGDVIV IPVHGCVLTC
DAVLIAGTCI VNESMLTGES VPVTKTSLTH QDDLEIYSPQ NHKRHTLFAG THIIQTRYYG
HAKVKAVVVR TGYNTAKGEL VRAILFPKPL GFKFYQDAMR FILFLAVVAS CGMVYSLVML
IRDGVSTGQI VLRVLDIITI VIPPALPAAM TVGTVYAQSR LKKKGIFCIS PPRINFCGRI
NAFCFDKTGT LTEDGLDMWG VVPAFSSSFY SPERNVHEMS MGPTLICMAT CHSLTIIDGE
LTGDPLDLIM FNSINWILEE PGEDTSKYDT IMPTIVKPCH RNHFSDEVVG IIRQFTFSSS
MQRMSVVTRS MSNNYMEVYC KGAPEIVASL CKPSTVPENF QHILHKYTVQ GFRVIALAYK
TLEPRINWHQ VQRVSRDKIE KELIFLGLMV LQNQLKPQTT SVIKTLKKAD IRPVMVTGDM
IQTAISVARN CNMVGQRDEV VIVKAVRPSK DTGAYIEWVN AELVAPEETF DPDSSDSYQP
ISLGEVDSKI HLAITGESFS VITHHFPHLL PKICTKGTIF ARMAPDQKYQ LVETLQKLDY
IVGMCGDGAN DCEVNIVII
//
