ID A0A5N6M2P3_9ASTR Unreviewed; 1112 AA.
AC A0A5N6M2P3;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=E3N88_36017 {ECO:0000313|EMBL:KAD3068137.1};
OS Mikania micrantha.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Eupatorieae; Mikania.
OX NCBI_TaxID=192012 {ECO:0000313|EMBL:KAD3068137.1, ECO:0000313|Proteomes:UP000326396};
RN [1] {ECO:0000313|EMBL:KAD3068137.1, ECO:0000313|Proteomes:UP000326396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLD-2019 {ECO:0000313|EMBL:KAD3068137.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAD3068137.1};
RA Liu B.;
RT "Mikania micrantha, genome provides insights into the molecular mechanism
RT of rapid growth.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00000363,
CC ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAD3068137.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SZYD01000017; KAD3068137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6M2P3; -.
DR Proteomes; UP000326396; Miscellaneous, Linkage group lg7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR Gene3D; 1.20.5.170; -; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR024750; Ca_ATPase_N_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF529; CALCIUM-TRANSPORTING ATPASE 10, PLASMA MEMBRANE-TYPE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12515; CaATP_NAI; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000326396};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 197..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 226..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 376..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 430..456
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1032..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 140..214
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 121194 MW; 5070266C4B400422 CRC64;
MSSGGSPYRK HRKDLESGDG SSGGYDDLES VYDPFDIART KSASVDRLRR WRQAALVLNA
SRRFRYTLDL KRAEEKKELI AKIRTHAQVI RAAYLFQAAG GKPEGTSKAP PSPIPTGGYD
VSPEQLSTMT REHDFSALQN FGGVKGLAEK LKTNLDKGIH EDDLNILDRK NVYGSNTYPR
KKGRSFWRFM LDACRDTTLI ILMVAAAASL ALGIKTEGIK EGWYDGGSIA LAVIIVILVT
ATSDYKQSLQ FQNLNEEKQN IQLEVVRGGR RVEISIFDIV VGDVIPLKIG DQVPADGVLI
SGHSLAIDES SMTGESKIVF KDHKSPFLMS GCKVADGYGT MLATSVGINT EWGLLMASIS
EDNGEETPLQ VRLNGVATFI GIVGLVVAIS VLIILLVRFF TGHTKDDEEN VEFIAGKTSV
GDAVDGAIKI FTVAVTIVVV AVPEGLPLAV TLTLAYSMRK MMADKALVRR LSACETMGSA
TTICSDKTGT LTLNLMTVVE AYICGKKIDP PSNASELPSG VTSLLIESVA QNTIGSVFLP
ENGKDVEVSG SPTEKAILQW GVNLGMNFEA VRSESSIFHA CPFNSENKRG GVAVKRPDSQ
VHVHWKGAAE IILAACTAYM DTTEQHIPLD DGKVEYFKKA IEDMAARSLR CVAIAYRPLK
GETVPKEEIL SFWDMPNDDL VLLAIVGLKD PCRSGVKDAV RLCVKAGVKV RMVTGDNLQT
ARAIALECGI LGSNADASEP NLIEGKSFRA LSEAQRLEIA DKISVMGRSS PNDKLLLVQA
LRKRGHVVAV TGDGTNDAPA LHEADIGLAM GIQGTEVAKE SSDIIILDDN FASVVKVVRW
GRSVYANIQK FIQFQLTVNV AALVINVVAA LSSGDVPLNA VQLLWVNLIM DTLGALALAT
EPPTDHLMDR LPVGRREPLI TNIMWRNLLI QALYQVTILL VLNFGGRDIL HSQHEPNEHA
TKEKNTLIFN SFVFAQIFNE FNARKPDEMN VFKGVTRNRL FMGIVGFTVV LQVIIIMFLG
KFTTTVRLSW QLWLVSIAIG FVSWPLAAAG KFIPVSERPF ADYFVGIFSW CRNGGLDDGM
LRPGAALLWP EWWPVAQPAE ALLWPDAPRS PA
//
