ID A0A0N5AVX2_9BILA Unreviewed; 1033 AA.
AC A0A0N5AVX2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000905101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000905101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0N5AVX2; -.
DR STRING; 451379.A0A0N5AVX2; -.
DR WBParaSite; SMUV_0000905101-mRNA-1; SMUV_0000905101-mRNA-1; SMUV_0000905101.
DR Proteomes; UP000046393; Unplaced.
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 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:SF214; 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; 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 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 286..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 332..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 843..861
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 876..896
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 924..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 26..78
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 813..1015
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1033 AA; 117519 MW; F05E65483B8EACB7 CRC64;
MRLKANESNL SPTRAIYIGK RKHNLTVSNA ISTCKYNIWT FIPKFLKEQF RQYNNLYFLL
IVLLQQIPEV SPTGRYNTAV PFALVLLASA VKEIYEDIKR KKSDVRANDT ITTVFRRSGW
RQIKWKDVSI GDILKIYEGE IFPADLLMIS SSNSDNTCLV ETSNLDGETN LKVRDKFNCQ
KEMCTPEQLS QLDCKIVCEQ PIKTIDKFSG FMDINAKPYP LVDNHSISKA FVSVSENLLL
RGTRLKETEF VIGIAVYTGH ETKLFLNFKK CPLKQSTISS VMNGRLIYLF IALIFLTLCS
TLGSLCFEHF ALANAYYLDY TRNSLRSFVT NVGSRFITFL LLYNNFIPIS LQFTMDIVRF
GQAQYINMDK AIYDKSENDM PIARTSNLTE ELGQAIYCEL IQVEYVMCDK TGTLTQNKME
FKYCSIAGKS YSVNSDTSAK IFDIPDDKEV VYIFTKYFGK LCAQLDNYEK EFFRNVTICN
KVRPHTNKLG EITYNSLRPD EDALVRGAAS VNFKLLNRNS EIVSVSELGE EKQYHILNTF
DFTSERKRMS IIVRCPDGSI RVYVKGADSV ILPRIINDCT FKAQLLQDYD GYGLRTLFFA
SRKLDEQLYN SWNLMYQKAS DSCTNREQML CECVELIETK LNLVGISAVE DKLQVGVKET
VRCFIDAGIR VWMLTGDNPK TAIAVGYAAN LCSKNDQKLI LLNRSCDESV GEFRRIAKLI
DGKSNRFMVI DGISLRNMLG EGGREPFLFL VRNCRTVICC RLSPMDKAKV VELIRKDNSV
VMAVGDGAND VAMIRAANVG AGIIGKEGSE AAAASDYAIR QFRFLQRLIF LHGVWNLKRS
MKVILYSFYK NICLYLIQFW YASSSAYSGQ TLFDRWTIAL FNSIFTFFPP IAIGLFEKPI
SAKGCMDKPE VYNTVRATAY SKRYFGWLML DAVLDSLLIY HFSHLILPDL AACKCGRTGG
LLMLGNTCYS LVMVTVCLKA IFMCTTRSYL IFTSSIVSVL LWVLLFYLYS QRTTKFRHGT
PLVLAQRCVA RLP
//
