ID A0A2C9V3Z1_MANES Unreviewed; 1183 AA.
AC A0A2C9V3Z1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=MANES_10G072200 {ECO:0000313|EMBL:OAY39167.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY39167.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY39167.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY39167.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CM004396; OAY39167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9V3Z1; -.
DR STRING; 3983.A0A2C9V3Z1; -.
DR EnsemblPlants; OAY39167; OAY39167; MANES_10G072200.
DR Gramene; OAY39167; OAY39167; MANES_10G072200.
DR Proteomes; UP000091857; Chromosome lg10.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 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; 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; 2.
DR PANTHER; PTHR24092:SF91; 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:UP000091857};
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 TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 395..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 946..971
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 977..995
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1023..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1085..1114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1120..1143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 78..144
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 910..1150
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 132723 MW; 31D3CF8AE5A41943 CRC64;
MDSNKPTEGF PNSEITLNSA SRRSNSSSHS KASRGNSVRE VTFGDLGSKP VRYGSRGADS
EGFSASQKEI SDEDARLVYL NDPEKTNERF EFSGNSVRTG KYSIISFVPR NLFEQFHRVA
YIYFLIIAVL NQLPQLAVFG RGVSIMPLAF VLLVTAVKDA YEDWRRHRSD RIENNRLAWV
LVNDQFEQKK WKDIRAGEII KIHANETLPC DMVLLSTSDS TGVAYVQTIN LDGESNLKTR
YAKQETLAKT PEKEKISGLI KCEKPNRNIY GFHANMDVDG KRLSLGPSNI ILRGCELKNT
TWSIGVAVYC GRETKVMLNS SGAPSKRSRL ETRMNREIII LSFFLIALCT IVSICAAVWL
RRNRDKLNTM PFYRKKNFND EDKDDYKYYG WGLEIFFTFL MSVIVFQIMI PISLYISMEL
VRVGQAYFMI RDTIMYDEAS NSTFQCRALN INEDLGQIKY VFSDKTGTLT ENKMEFQCAS
IWGVDYSGGK ASSEDKQIEH SVQVDGKTLR PKMKVRVDPE LLQLSRSGKD TEKTKRVHDF
FLALAACNTI VPIVFDDASD PTVKLMDYQG ESPDEQALAY AAAAYGFMLV ERTSGHIVID
IKGERQRFDV LGLHEFDSDR KRMSVILGCP DKTVKVFVKG ADTTMFSVID RSLNMNVIRA
TEAHLHDYSS LGLRTLVIGM RELSDSEFEQ WHSSFETASS ALIGRAAMLR KVASTVEKSL
SILGASAIED KLQQGVPEAI ESLRTAGIKV WVLTGDKQET AISIGYSSKL LTIKMTQIII
NSNSKESCRR SLGDALLMSK KLITVSGTTP DTAGNSGGAV SPVALIIDGT SLVYILDSEL
EEQLFELASK CSVVLCCRVA PLQKAGIVAL VKNRTSDLTL SIGDGANDVS MIQMADVGVG
ISGKEGRQAV MASDFAMGQF RFLVPLLLVH GHWNYQRMGY MILYNFYRNA LFVLVLFWYV
LFTCFTLTTA INEWSSMLYS IIYTSLPTIV VGILDKDLSR RTLLRYPQLY GAGHRQESYN
SKLFWTTMID TLWQSAVIYF IPHLAYWAST IDAPSIGDLW TLAVVILVNL HLAMDVIRWS
WITHAAIWGS IVATFICVMV IDAVPTLVGY WAFYEIAKEG LFWLCLLAII VAALLPRFVV
IVLHQYFSPS DIQISKEAEK FGNGREFGAV EIEMNPILDP SRR
//
