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Database: UniProt
Entry: A0A3B6C6H1_WHEAT
LinkDB: A0A3B6C6H1_WHEAT
Original site: A0A3B6C6H1_WHEAT 
ID   A0A3B6C6H1_WHEAT        Unreviewed;      1086 AA.
AC   A0A3B6C6H1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-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=CFC21_023538 {ECO:0000313|EMBL:KAF7008887.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS2B02G294800.1};
RN   [1] {ECO:0000313|EMBL:KAF7008887.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7008887.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS2B02G294800.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS2B02G294800.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS2B02G294800.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7008887.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7008887.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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}.
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DR   EMBL; CM022215; KAF7008887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6C6H1; -.
DR   SMR; A0A3B6C6H1; -.
DR   STRING; 4565.A0A3B6C6H1; -.
DR   EnsemblPlants; TraesCS2B02G294800.1; TraesCS2B02G294800.1; TraesCS2B02G294800.
DR   Gramene; TraesCLE_scaffold_016760_01G000400.1; TraesCLE_scaffold_016760_01G000400.1; TraesCLE_scaffold_016760_01G000400.
DR   Gramene; TraesCS2B02G294800.1; TraesCS2B02G294800.1; TraesCS2B02G294800.
DR   Gramene; TraesCS2B03G0769600.1; TraesCS2B03G0769600.1.CDS; TraesCS2B03G0769600.
DR   Gramene; TraesPAR_scaffold_054620_01G000100.1; TraesPAR_scaffold_054620_01G000100.1; TraesPAR_scaffold_054620_01G000100.
DR   Gramene; TraesROB_scaffold_019323_01G000100.1; TraesROB_scaffold_019323_01G000100.1; TraesROB_scaffold_019323_01G000100.
DR   Gramene; TraesWEE_scaffold_054857_01G000400.1; TraesWEE_scaffold_054857_01G000400.1; TraesWEE_scaffold_054857_01G000400.
DR   OMA; HGHTAYQ; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000019116; Chromosome 2B.
DR   Proteomes; UP000815260; Chromosome 2B.
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:SF199; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000019116};
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        282..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        828..846
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        852..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        908..927
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        939..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        967..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1001..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          20..84
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          792..1031
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1086 AA;  121932 MW;  248A6443E7B615CF CRC64;
     MCSALNGTEV TSSSKMQRFV YINDESCRDS YRDNRVSNTK YTLWNFLPKN LLEQFRRFMN
     QYFLLIACLQ LWPTITPVSP ATTWGPLAII FIVSASKEAW DDYNRYLSDK KVNERRIWVV
     KDGIRRQIKA RGIHVGNIVW LHENDEIPCD LVLIGTSDPQ GICYVETAAL DGETDLKTRI
     IPSICADLSS EQLGKIKGVV ECPNPDNDIR RFDANMRLFP PIIDNEKCPL TINNTLLQSC
     YLRYTEWACG VAIYTGNETK SGMSRGTAEP KLTAADSMID KLTVAIFIFQ IAVVLLLGLA
     GNIWMDSHGR KLWYLMYPAE RPWYDFLVIP LRFELLCSIM IPISIKVTLD LAKGVYAKFI
     DCDDQMFDPE TNTPAHSANT AISEDLGQVE YILSDKTGTL TENRMIFRRC CISGVLYGDK
     TGDALKDARL LNAVSSNDPD VVKFLMVMAL CNTVVPIKSN DGTISYKAQS QDEEALVNAA
     SNLNMLLTSK DSSGIAEICF NGSKFYYEVL DVLEFTSDRK RMSIVIKEAK SGRFLLLTKG
     ADEAIFPRSC PGQQTKTYLE AVEMYSHFGL RTLCLGCRDL EEDEYKEWSK KFQDASCSLD
     NREHKIAEVC NSLEQGIHIL GITAIEDRLQ DGVPETIKLL RKAGINVWML TGDKQTTAIQ
     IGLLCNLITP ESKGQLLSIN GKTEDDILQS LERALTIMKT ALERKDLAFV LDGWALEIIL
     KRSLESFTKL AMMSRTAICC RMTPLQKAQL VGILKSSGSL TLAIGDGGND VRMIQEANVG
     VGISGREGLQ AARAADYSIG KFKFLRRLIL VHGRYSYNRT AFISQYSFYK SLLICFIQIL
     FSFSSGLSGT SIFNSISLMA YNVFYTSLPV MTIIFDKDIS ETTVLRYPQI LLYSQAGRLL
     NRSTFAEWFG RSLYHAFVVF LITINAYADE KSDMEELSMV ALSGCIWLQA FVVTLDTNSF
     TCPQITLIWG NFVAFYMINL ILSAVPTLQM HTVMWHLCNQ PSYWITMALI VAAGMGPVLA
     LRYLRNVYRP SAIDVLQQIE QTDGHAQAPG NLESSTGTYL DYLLTDLRRN KSSIHQPLLS
     DSASSR
//
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