ID A0A371FY84_MUCPR Unreviewed; 1080 AA.
AC A0A371FY84;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN Name=ALA3 {ECO:0000313|EMBL:RDX83241.1};
GN ORFNames=CR513_35864 {ECO:0000313|EMBL:RDX83241.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX83241.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDX83241.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDX83241.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) 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}.
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:RDX83241.1}.
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DR EMBL; QJKJ01007414; RDX83241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371FY84; -.
DR STRING; 157652.A0A371FY84; -.
DR Proteomes; UP000257109; 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: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; 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; 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:SF180; PHOSPHOLIPID-TRANSPORTING ATPASE 3; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 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 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 162..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 210..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 771..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 809..828
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 849..872
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 892..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 946..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 740..986
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDX83241.1"
SQ SEQUENCE 1080 AA; 122765 MW; F454127184ED02A4 CRC64;
NSGYPAIPVR GLAAPLRYLG LTTMVKQDGF FPADVLFLAS TNADGVCYIE TANLDGETNL
KIRKALEKTW DYVTPEKASE FKGEIQCEQP NNSLYTFTGN LIIQKQTLPL SPNQILLRGC
SLRNTEYIVG VVIFTGHETK VMMNTMNVPS KRSTLERKLD KLILTLFATL FMMCFIGAIG
SAIFVNKKYF YLHLDSSEKG SAQFNPKNRF LVFILTMFTL ITLYSTIIPI SLYVSIEMIK
FIQSTQFINK DLSMYHNETN TPALARTSNL NEELGQVEYI FSDKTGTLTR NLMEFFKCSI
GGELYGNGVT EIERGLAERN GMKIEENKSP NAVQERGFNF DDARLMRGAW RNEPNPDACK
EFFRCLAICH TVLPEGDESP EKIRYQAASP DESALVIAAK NFGFFFYRRT PTMIYVRESH
IEKMGKIEDV SYEILNVLEF NSTRKRQSVV CRYPDGRLVL YCKGADTVIY ERLSAGNNDI
KKVTREHLEQ FGSSGLRTLC LAYKELHPDV YESWNEKFIQ AKSSLNDREK KLDEVAELIE
NDLILIGSTA IEDKLQEGVP FCIETLQRAG IKVWVLTGDK IETAINIAYA CNLINNEMKQ
FIISSETDAI REVEDRGDQV EIARFIKDEV KKELKKCLEE AESYFHTLSG PKLALVIDGK
CLMYALDPNL RVMLLNLSLN CHAVVCCRVS PLQKAQVTSM VKKGAQKITL SIGDGANDVS
MIQAAHVGVG ISGLEGMQAV MASDFAIAQF RYLADLLLVH GRWSYLRICK VVIYFFYKNL
TFTLTQFWFT FQTGFSGQRF YDDWFQSLYN VIFTALPVII VGLFDKDVSS SLSKKYPELY
MEGIRNVFFK WKVVAIWAFF SVYQSLIFFY FVSTSNLSGK NSAGKIFGLW DVSTMAFTCV
VITVNLRLLM ICNSITRWHY ISVGGRITTP YDRQVNSLST LGVENIYFVI YVLMSTFYFY
VMLLLVPVAA LFCDFVYQGV QRWFFPYDYQ IIQEMHRHEL DSAGRTQLLE IGNQLTPAEA
RSYAISQLPR ELSKHTGFAF DSPGYESFFA AQLGVYAPPK AWDVARRASM RSKPKTGRQK
//
