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
//