ID A0A2R6XQY1_MARPO Unreviewed; 1128 AA.
AC A0A2R6XQY1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=MARPO_0005s0144 {ECO:0000313|EMBL:PTQ48504.1};
OS Marchantia polymorpha (Common liverwort) (Marchantia aquatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197 {ECO:0000313|EMBL:PTQ48504.1, ECO:0000313|Proteomes:UP000244005};
RN [1] {ECO:0000313|Proteomes:UP000244005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 {ECO:0000313|Proteomes:UP000244005};
RX PubMed=28985561; DOI=10.1016/j.cell.2017.09.030;
RA Bowman J.L., Kohchi T., Yamato K.T., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.S.,
RA Althoff F., Araki T., Arteaga-Vazquez M.A., Balasubrmanian S., Barry K.,
RA Bauer D., Boehm C.R., Briginshaw L., Caballero-Perez J., Catarino B.,
RA Chen F., Chiyoda S., Chovatia M., Davies K.M., Delmans M., Demura T.,
RA Dierschke T., Dolan L., Dorantes-Acosta A.E., Eklund D.M., Florent S.N.,
RA Flores-Sandoval E., Fujiyama A., Fukuzawa H., Galik B., Grimanelli D.,
RA Grimwood J., Grossniklaus U., Hamada T., Haseloff J., Hetherington A.J.,
RA Higo A., Hirakawa Y., Hundley H.N., Ikeda Y., Inoue K., Inoue S.I.,
RA Ishida S., Jia Q., Kakita M., Kanazawa T., Kawai Y., Kawashima T.,
RA Kennedy M., Kinose K., Kinoshita T., Kohara Y., Koide E., Komatsu K.,
RA Kopischke S., Kubo M., Kyozuka J., Lagercrantz U., Lin S.S., Lindquist E.,
RA Lipzen A.M., Lu C.W., De Luna E., Martienssen R.A., Minamino N.,
RA Mizutani M., Mizutani M., Mochizuki N., Monte I., Mosher R., Nagasaki H.,
RA Nakagami H., Naramoto S., Nishitani K., Ohtani M., Okamoto T., Okumura M.,
RA Phillips J., Pollak B., Reinders A., Rovekamp M., Sano R., Sawa S.,
RA Schmid M.W., Shirakawa M., Solano R., Spunde A., Suetsugu N., Sugano S.,
RA Sugiyama A., Sun R., Suzuki Y., Takenaka M., Takezawa D., Tomogane H.,
RA Tsuzuki M., Ueda T., Umeda M., Ward J.M., Watanabe Y., Yazaki K.,
RA Yokoyama R., Yoshitake Y., Yotsui I., Zachgo S., Schmutz J.;
RT "Insights into land plant evolution garnered from the Marchantia polymorpha
RT genome.";
RL Cell 171:287-304.e15(2017).
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; KZ772677; PTQ48504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6XQY1; -.
DR EnsemblPlants; PTQ48504; PTQ48504; MARPO_0005s0144.
DR Gramene; PTQ48504; PTQ48504; MARPO_0005s0144.
DR Proteomes; UP000244005; Unassembled WGS sequence.
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 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; 1.
DR PANTHER; PTHR24092:SF19; 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; SFLDS00003; Haloacid_Dehalogenase; 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:UP000244005};
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 267..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 837..858
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 942..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1008..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 5..70
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 797..1036
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1128 AA; 126891 MW; 2CA7F671DC67EB6C CRC64;
MKRFVYVNDS DLTPSIYCNN RISNTKYTLF NFIPKNLWEQ FSRFMNKYFL LIACLQLWPL
ITPVSPASTW GPLILIFAVS ATKEAWDDHG RYLLDKKANE RSVWVLKKGI KTRTQAQDIQ
VGDILWLRDQ DEVPCDMVLL GTSEPGGICY VETAAMDGET DLKTRVVPPP CIGLTSDLLH
KIKGVIECPQ PDKDIRRFDA NLRLFPPFID NDFCSLTINN TLLQSCYLRN TEWACGVAVY
TGNETKLGLS KGLPEPKLTA VDHMIDTLTG AIFVFQIVVV VILGVAGNMW RLSEGQKIWY
VKYNLTSSPW YEFLVIPLRF ELLCSIMIPI SIKVSLDLVK SVYSKFIDWD LQMYDESTDT
PAVATNTAIS EDLGQVEYIL TDKTGTLTEN IMVFKRCCIN RVCYGDATGD ALTDTQLTRA
LQEHVPEVVK FVKVMAMCNT VVPARSGNGA LSYKAQSQDE EALVQAASRL HMKLISRTGS
RLELDFLGDT LHYEILDVLE FTSDRKRMSV IVRELKSRKI KMLTKGADET ILSIVNPEQQ
CRVISEAVEH YSQVGLRTMC VAWRDLDDEE YSRWSVKFKE ANSSVTDREW KVAEVCQLIE
TNLELLGATA IEDKLQEGVP ETIRTLRKAG INFWMLTGDK QSTAIQIALS CNFVLPEPEG
QLLHVQGRTQ QEVQTSLERV LRTLRISSTE PKVNVQQDEI EMATCDVLKH DIAFVIDGWA
LELALHYNKQ AFEELAMLSK TAICCRVTPS QKAQLVQLVK NCDYRTLAIG DGGNDVKMIQ
EAHVGVGISG REGLQAARAA DFSLGKFRFL ERLILIHGRY SYNRTAFLSQ YSVYKSLLIC
FIQIFFSFVS GVSGTSLFNS FSLMAYNVVY TSIPVMTVVQ DKDLKEETVL QNPEILYICQ
AGRLINPSTF AGWFGRSLYH AAVVFLITIH VYANEKSEME EMAMVAFSGC IWLQAFVVPL
EMNAFTSVQI LGIVGNLVLF YVVNFAVSML KWGGMYTIMD RICRQPAYWL AVTLIVVMGM
GPVFALKYFR FVYRPNAINV LQHYEHMTAS ANANPASVES PLRSFEKGSM PLSLNSPSKA
ELGSVYEPLL CDSPSSSLKR GGLNYSTDFI PSSPSKFTLS AYARSKNN
//
