ID A0A4S8IK09_MUSBA Unreviewed; 1238 AA.
AC A0A4S8IK09;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=C4D60_Mb06t02490 {ECO:0000313|EMBL:THU48767.1};
OS Musa balbisiana (Banana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX NCBI_TaxID=52838 {ECO:0000313|EMBL:THU48767.1, ECO:0000313|Proteomes:UP000317650};
RN [1] {ECO:0000313|EMBL:THU48767.1, ECO:0000313|Proteomes:UP000317650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH-PKW {ECO:0000313|Proteomes:UP000317650};
RC TISSUE=Leaves {ECO:0000313|EMBL:THU48767.1};
RA Yao X.;
RT "Genome sequencing of Musa balbisiana reveals subgenome evolution and
RT function divergence in polyploid bananas.";
RL Nat. Plants 0:0-0(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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:THU48767.1}.
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DR EMBL; PYDT01000009; THU48767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S8IK09; -.
DR STRING; 52838.A0A4S8IK09; -.
DR Proteomes; UP000317650; Chromosome 6.
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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF224; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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; 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|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000317650};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1238
FT /note="Phospholipid-transporting ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020389210"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 307..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 951..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1037..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1105..1124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1144..1163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 45..112
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 923..1173
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 464..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 139508 MW; 5C1EDE561B893183 CRC64;
MARRVRKRDR LRWSLLYTFA CARPAVLADD EQTPFLQGPG YSRIVHCNQS QLHGKKPLDY
SSNYISTTRY NAITFLPKAL FEQFRRVANI YFLLAAIISI TPVSPFNPMS MIAPLAFVVG
LSMAKEALED WRRFYQDMKV NSRKVSVHKG QGQFGYKPWQ KIQVGDVVKV EKDRFFPADL
LLLSSSYEDG ICYVETMNLD GETNLKVKRS LEVTLALEDD EAFRDFTATL RCEDPNPNLY
TFVGNLEYER QVYALDPNQV LLRDSKLRNT SYVYGVVIFT GHDSKVMQNA TESPSKRSRI
EKKMDKIIYI LFTVLVLISL VSSIGFAVMT KYDMPNWWFL EPNNTTSLYD PSKPVLSGVF
HMVTALILYG YLIPISLYVS IEVVKVLQAT FINQDVLMYD EEIGKPARAR TSNLNEELGQ
VDTILSDKTG TLTCNQMDFL KCSIAGVSYG VRASEVEIAA AKQLASEASG SPEHHDDTEE
LGEDNAGFYG TSDIELANGI TCMVEKSHKP AIKGFSFEDD RLMHGNWTNE PAASTILMFF
RILALCQTAI PEHNKETGGF TYEAESPDEG AFLVAAREFG FEFCKRTQSS VFIREKYSPS
EDPVEREFKI LNLLEFNSKR KRMSVIVRDE GGQIILLCKG ADSIIFDRLS KNGRLYENDT
SKHLNEYGEA GLRTLALAYR MLDESEYSAW NTEFLKAKTT IGPDREAQVE RVSEMMERDL
ILVGATAVED KLQRGITPAQ VQQCIDKLAQ AGLKIWVLTG DKIETAINIG FACSLLRQGM
KQISLSITNI DLLTHDANKG VRLHLMTDQA AKENLSMQIT NAFQMIKLEK DPDAAFALII
DGKTLTYALE DDLKNQFLSL AVDCASVICC RVSPKQKAMV TRLVKEGTGK VTLAVGDGAN
DVGMIQEADI GVGISGVEGM QAVMASDFSI SQFRFLERLL VVHGHWCYKR IALMICYFFY
KNIAFGLTIF YFEAYTGFSG QSVYDDWYML LFNVVLTSLP VISLGVFEQD VSSEVCLQFP
ALYQQGPRDL FFGWYRIIGW MFNGLSASII IFLLNIAIFY HGAFRAGGQT ADLAAVGTTM
FTCIIWAVNV QIALIMSHFT WIQHLFVWGS VVAWYLFLVA YGLSSPTISG NAHQILSEAL
GPAPVYWSAT LLVTAVCNIP YLVHISFQRT FNPLDNHVIH EIKYYKKDVE DQHMWKREKS
KARQKTKIGF TARVDAKIRQ LRGKLHRKVS SLTIHTVS
//
