ID A0A5N4D8Q7_CAMDR Unreviewed; 1232 AA.
AC A0A5N4D8Q7;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=Cadr_000012983 {ECO:0000313|EMBL:KAB1267564.1};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1267564.1, ECO:0000313|Proteomes:UP000299084};
RN [1] {ECO:0000313|EMBL:KAB1267564.1, ECO:0000313|Proteomes:UP000299084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Drom800 {ECO:0000313|EMBL:KAB1267564.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB1267564.1};
RX PubMed=30972949; DOI=.1111/1755-0998.13020;
RA Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA Burger P.A.;
RT "Improving Illumina assemblies with Hi-C and long reads: an example with
RT the North African dromedary.";
RL Mol. Ecol. Resour. 19:1015-1026(2019).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KAB1267564.1}.
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DR EMBL; JWIN03000014; KAB1267564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N4D8Q7; -.
DR Proteomes; UP000299084; 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; 2.
DR PANTHER; PTHR24092:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 2.
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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000299084};
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 354..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1024..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1058..1080
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1124..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1169..1195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 910..1079
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT DOMAIN 1102..1210
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAB1267564.1"
SQ SEQUENCE 1232 AA; 139451 MW; 334A524C67ABE1EF CRC64;
WARPPAPPGP LFTQTSPAPA HLPCCPQCAG EENWVDSRTV YVGHREPPPG AEAYILQRFP
DNRIVSSKYT FWNFIPKNRF ETVQKNSQLL FSYHISGTAD HRPPTSPVTS GLPLFFVITV
TAVSRVTAGP GSRFPSSQGY EDWLRHKADS AVNQCPVHFV STQLVRKQSR KLRRALCRRG
HRMVKEDETF PCDLVFLSSS PQTGPASVTP ASLDGESSHK LGAAGGRRHL PLVPADGCGV
NSHFLSVCRP IMQFKTQRGF TLKRTSAACT PPSSAQQPQP DLYRFVGRIN VYSDLNDPVV
RPLGSENLLL RGATLKNTEK IFGVAVYTGM ETKMALNYQS KSQKRSAVEK SMNVFLIVYL
CILISKALIN TVLKYVWQSD PFRDEPWYNQ KTESERQRNL FLRAFTDFLA FMVLFNYIIP
VSMYVTVEMQ KFLGSYFIAW DEEMFDEEMG EGPLVNTSDL NEELGQVEYV FTDKTGTLTE
NNMEFKECCV GGHVYVPHAV CNGQVLPDAS AIDMIDASPG ASGREQEELF FRALCLCHTV
QVKEDDEVDG PRKSPDAGRR SAYISSSPDE VALVEGVQRL GFTYLRLKDN YMEILNRDND
VERFELLEIL SFDSVRRRMS VIVRSAAGEI YLFCKGADSS IFPRVIEGKV EQIRSRVEHN
AVEGLRTLCV AYRRLTQEEH EGVCKLLQAA RVALQDRERK LAEAYEQIEK NLVLLGATAV
EDRLQEKAAD TIEALQKAGI KVWVLTGDKM ETAAATCYAC KLFRRGTQLL ELTTKKLEEQ
NLHDVLFELS KTVLRCGASL TRDSFSGLSA EMQDYGLIID GAALSLVLKP REDGSSGNYR
ELFLEICRNC SAVLCCRMAP LQKAQIVKLI KFSKEHPITL AIGDGANDVS MILEAHVGIG
VIGKEGRQAA RNSDYAIPRF KHLRKMLLVH GHFYYIRVSE LVQYFFYKNV CFIFPQFLYQ
FFCGFSQQTL YDTAYLTLYN ISFTSLPILL YSLMEQHVGV DTLRRDPSLY RDIAKNALLR
WRVFIYWTFL GVFDALVFFF GAYFMFENTT VTSNGQIFGN WTFGTLVFTV MVFTVTLKVN
PLTSGSSSSP SSPTRTCRGN TAVNAFAFFQ LALDTHYWTW INHLVIWGSL LFYVVFSLLW
GGIIWYGFGR QTVIITWVVL RPFLSYQRMY YVFIQMLSSG PAWLAIVLLI TVSLLPDVLK
KVLCRQLWPS ATERVQVHDE KEMLYTRVLC PR
//
