ID A0A0R3T0F9_RODNA Unreviewed; 909 AA.
AC A0A0R3T0F9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=HNAJ_LOCUS298 {ECO:0000313|EMBL:VDN96157.1};
OS Rodentolepis nana (Dwarf tapeworm) (Hymenolepis nana).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Rodentolepis.
OX NCBI_TaxID=102285 {ECO:0000313|Proteomes:UP000046398, ECO:0000313|WBParaSite:HNAJ_0000029701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HNAJ_0000029701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN96157.1, ECO:0000313|Proteomes:UP000278807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|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|RuleBase:RU362033}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR EMBL; UZAE01000070; VDN96157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3T0F9; -.
DR STRING; 102285.A0A0R3T0F9; -.
DR WBParaSite; HNAJ_0000029701-mRNA-1; HNAJ_0000029701-mRNA-1; HNAJ_0000029701.
DR Proteomes; UP000046398; Unplaced.
DR Proteomes; UP000278807; 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: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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR PANTHER; PTHR24092:SF212; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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:UP000278807};
KW Translocase {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 312..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..100
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
SQ SEQUENCE 909 AA; 102186 MW; B23226C98B87D576 CRC64;
MCGVSSCTMN LKKLFKRKVD DSEFKGRTII VNSIPSLSEE ADANNRKFID NEIISSHYKW
WNFLPVNLFE QFHVVANFFF LLISILYFFG ETPINPVTTI APLVVVIGIS MAKDAIDDIK
RHKSDRKFNR NRFMVLTHDL ADNTSSFAQR YSQDIHCGDI VICYNNSSFP CDMLILASSN
SNGKVFITTD NLDGESSIKT TNALAFTQNL LSPTIAKIEK LQHHNIELGL ERSTIICQNP
CEDLKAFEGS LNLPSESIPL ALNNVVYRGA NLHHTTFMIG VAIYTGKETK LSLNGKPGFR
KFSSTAGRFN DILLAFIGAM FVVTLIITIL HFVWNAMPYG EPWYFFTPIA TNWRRVQQYL
TLLFIINYLI PISIMVTMEL QQLVLAFFIN KDVELYDPET NEKTQVNATN LADELGQIEF
LFSDKTGTLT QNKMIFKSYS LANDHYVYDV EEEGLFKVRS KNKSSTITDP TKVSPTTPCD
VNAADYFSFS EDEEESLEVG LESSDDLTTQ KEKERVYILS KEAEQFWTNI VLNHSVEAKT
SVNNDTLEEV ITYNAASPDE KALIDAAAKV GITYIGLDDS IGSKNGDYNT HLVRFDPGTL
SGKPSKVVTR KFKVDAVIEF NSVRKRMSVM VRDDEGRCVV YTKGAEVTML DPRRCDKTPS
LTKDKIIRNV TEFALSGLRT LVFARRELDG DTYNSLLKKY RWAQCQLGIE RVRALEEASA
DIEANMSLIG VSAVEDKLQP GVRQCLQSLI SAGIQIWVLT GDKEETAVQI SQATGHFPPG
TTLIRLTNGQ STEEVGRAIY VQQEGMKARL EVKKGRSRFK RLFQKRDALD SFGLDSEAFD
SDTSSDSDDE ETKIKKHKSS LISRFNRRFR SAVADGLRRH RRKNPGGANE PVGLVIDGAT
LRYAISCTV
//
