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Database: UniProt
Entry: A0A314UJ41_PRUYE
LinkDB: A0A314UJ41_PRUYE
Original site: A0A314UJ41_PRUYE 
ID   A0A314UJ41_PRUYE        Unreviewed;       999 AA.
AC   A0A314UJ41;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=Pyn_21177 {ECO:0000313|EMBL:PQM37573.1};
OS   Prunus yedoensis var. nudiflora.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQM37573.1, ECO:0000313|Proteomes:UP000250321};
RN   [1] {ECO:0000313|EMBL:PQM37573.1, ECO:0000313|Proteomes:UP000250321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PQM37573.1};
RA   Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA   Yu H.-J., Mun J.-H.;
RT   "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL   Submitted (FEB-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:PQM37573.1}.
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DR   EMBL; PJQY01003432; PQM37573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A314UJ41; -.
DR   STRING; 2094558.A0A314UJ41; -.
DR   Proteomes; UP000250321; 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; 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:SF70; 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:UP000250321};
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        302..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        353..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        916..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        948..965
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          40..105
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          881..995
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   999 AA;  112764 MW;  43D33DE6A617BD26 CRC64;
     MGGGRRKKQH FGRIHAFSCG KASFNGEHSR IGGPGFSRVV YCNDPDCLEA TAHSYESNYV
     RTTKYRLATF LPKALFEQFR RVANIYFLIC AILSFTPLSP YSAVSNVVPL VVVIGVTMGK
     EAVEDWRRKR QDIEMNNRKV RVHHGDGVFE YTKWRDLKVG DIVKVEKDEY FPADLILLSS
     SYDEALCYVE TTNLDGETNL KLKQALDATS NLHEDSSFDN FKGVIRCEDP NANLYSFVGS
     LEIEEQPYPL TPQQLLLRDS KLRNTDFVYG VVIFTGHDTK VMQNSTAPPS KRSKVEKRMD
     KIIYFLFFLL VLMSFVGATV FGVTTRKDLE NGRMIRWYLR PDDTTVYYDP TRAPVAAILQ
     FLTAIMLYMH FHKPDLHMYY EETDQPALAR TSNLNEELGQ VDTILSDKTG TLTCNSMEFI
     KCSIAGTAFG RGVTEVERAL AGRKGSSKSS LAEEVTEEES HVEDLTEPKS LIKGFNFRDE
     RIMNGHWVNE PRADIIQKFL QLLAICHTAI PDIDEETGRV SYEAESPDEA AFVIAARELG
     FEFYNRTQTS ISVHELDPIY GRKVERAYKL LSILEFSSSR KRMSVIIRTE EGKILLLCKG
     ADSVMFERLA KNGREFEEKT KEHINEYADA GLRTLVLAYR ELDEEEYVEF DKEFTEAKNL
     VSSDREEIVE QVSEKIERDL ILLGATAVED KLQNGVPECI DKLAQAGIKI WVLTGDKMET
     AINIGYACSL LRQGMKQIVI SSETPEVKAL EKVEDKSMVV PRKGELKALK ESVVHQINEG
     KALLTSPVEN SEALALIIDG TSLAYALEKD VKDLFIELAI GCASVICCRS SPKQKALVTR
     LVKERNGNTT LAIGDGANDV GMLQEADIGV GISGVEGMQA VMSSDVAIAQ FCFLERLLLV
     HGHWCYRRIS SMICYFFYKN IAFGFTIFFF EIYASFSGQT AYNDWYLSLY NVFFTSLPVI
     ALGVFDQDVS AKFCLKFPLL YQEGAQNVLF SWLRILDGQ
//
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