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Entry: A0A5N5HY84_9ROSA
LinkDB: A0A5N5HY84_9ROSA
Original site: A0A5N5HY84_9ROSA 
ID   A0A5N5HY84_9ROSA        Unreviewed;      1284 AA.
AC   A0A5N5HY84;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=D8674_007929 {ECO:0000313|EMBL:KAB2630410.1};
OS   Pyrus ussuriensis x Pyrus communis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=2448454 {ECO:0000313|EMBL:KAB2630410.1, ECO:0000313|Proteomes:UP000327157};
RN   [1] {ECO:0000313|EMBL:KAB2630410.1, ECO:0000313|Proteomes:UP000327157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 {ECO:0000313|EMBL:KAB2630410.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAB2630410.1};
RA   Ou C.;
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000327157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT   "A de novo genome assembly of a pear dwarfing rootstock.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAB2630410.1, ECO:0000313|Proteomes:UP000327157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 {ECO:0000313|EMBL:KAB2630410.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAB2630410.1};
RA   Wang F., Wang J., Li S., Zhang Y., Fang M., Ma L., Zhao Y., Jiang S.;
RT   "A de novo genome assembly of a pear dwarfing rootstock.";
RL   Submitted (NOV-2019) 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:KAB2630410.1}.
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DR   EMBL; SMOL01000143; KAB2630410.1; -; Genomic_DNA.
DR   Proteomes; UP000327157; Chromosome 12.
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; 2.
DR   PANTHER; PTHR24092:SF148; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
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:UP000327157};
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        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        415..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        473..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1055..1074
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1086..1107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1128..1150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1162..1181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1188..1210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1230..1249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          154..219
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1019..1259
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1284 AA;  144804 MW;  9673EF0346D927AD CRC64;
     MNSEQSLLSS SDSPSASLVP SPSLTKNLVR ICSNASFSSS SLDNSDDAQS DLFEVKDEVA
     VSGCSERPLE NFTTPAGPPS SRFLPQSPLE NPTRDRRRLV SWGTMELHNE NRNSGTLEIS
     QGSSRVQEKL SQRIRHKIVQ FDDNLPHDDN PRLIYINDPK RTNDKYEFTG NEIRTSKYTI
     ITFLPKNLFI QFHRVAYLYF LAIAALNQLP PLAVFGRTVS LFPLLFVLLV TAIKDGYEDW
     RRHRSDRNEN NREALVFQSG QFRPKKWKHI QVGEVLKICA DDTIPCDVVL LGTSDPSGIA
     YIQTMNLDGE SNLKTRYARQ ETTSTVRDGC TFSGLIRCEQ PNRNIYEFTA NMEFNGHKFP
     LSQSNIVLRG CQLKNTDWAV GVAVYAGQET KAMLNSAASP SKRSKLESYM NRETLWLSIF
     LFVMCAVVAT GMGLWLIRHK GQIDTLAYYR KRYYSYGNVN GKTYRFYGIP MEIFFSFLSS
     IIVFQIMIPI SLYITMELVR LGQSYFMIED RHMFDSSSGS RFQCRSLNIN EDLGQIRYIF
     SDKTGTLTEN KMEFRRASIF GRNFGTSLQE ANVAGIGLGR KRWKLKSEIS VDNELMELLH
     KDLSGDDRIA AHEFFLTLAA CNTVVPIVSN GTSSSCGKSE LDDVEAIDYQ GESPDEQALV
     SAASAYGYTL FERTSGHIVM DVNGEKLRLD VLGLHEFDSV RKRMSVVIRF PNNSVKVLVK
     GADTTMLSTL ANDSERDDHV TRLTQNHLSE YSSEGLRTLV VASRDLTDEE LKQWQSMYED
     ASTSLTDRSV KLRQTAGVIE CNLKLLGATA IEDKLQDGVP EAIESLRQAG IKVWVLTGDK
     QETAISIGIS CKLLTADMQQ IIINGTSKDE CRNLLADSME RYGVKSSNKI DPSFKLKKIA
     ENGYLEIPGD AKTSTVPQWN GGKEEGKMNA PLALIIDGNS LVYILEKDLE SELFNLATSC
     SVVLCCRVAP LQKAGIVDLI KTRTDDMTLA IGDGANDVSM IQMADVGVGI CGQEGRQAVM
     ASDFAMGQFR FLKRLLLVHG HWNYQRVGYL VLYNFYRNAV FVMMLFWYIL GTAFSTTSAL
     TDWSSVFYSV IYTSLPTIVV GILDKDLSHR TLLQYPKLYG AGHRHEAYNL HLFWITMLDT
     LWQSLVLFYV PLFTYKDSSI DIWSMGSLWT IAVVVLVNIH LAMDIHRWVF ITHIAVWGSI
     IITYACMIVL DSIPVFPNYW TIYHLAKSPT YWIAILLITV VALLPRFVFK VVYHIFWPSD
     IQIAAEILNR QRKHLSSKQD DSSS
//
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