ID A0A0N8JZG6_SCLFO Unreviewed; 1302 AA.
AC A0A0N8JZG6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Z043_111975 {ECO:0000313|EMBL:KPP69281.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP69281.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP69281.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP69281.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) 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 -!- 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:KPP69281.1}.
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DR EMBL; JARO02004030; KPP69281.1; -; Genomic_DNA.
DR STRING; 113540.ENSSFOP00015067876; -.
DR Proteomes; UP000034805; 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; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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; 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:UP000034805};
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 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 106..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1049..1067
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1079..1100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1142..1166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1172..1198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 50..105
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1016..1247
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 145216 MW; 445D2D791D450C68 CRC64;
MGRGWSSPTG APTSKSISGN QDCPGHKFPG KRRTVIARYG PYKDEYCTIT KGYHGNGIHT
TKYTLVSFIP MNLFEQFHRA ANLYFLFLVL LNWVPVVEAF QKEITMIPLV VVLCVIAFKD
ALEDYRRYRF DKMINSKVTK VYCGKQRQYV DQHWKDICVG DFVYLSCNEI IPADMVLLHS
SNPDGICRIE TANLDGETNL KQKQVIKGLA WQDAEVSPEA FASRIECESP NDDLNRFRGF
MEHANKTRVG LHNENLLLRS CTIRNTESVV GIVVYAGHET KAMKNNSGPR YKRSKLERRL
NTDILWSLVL LLFMCLTAAI GHGIWLSGLK NPPFLIPDGT SPALAGFYLF WTMIIVLQVL
IPISLYVSIE IVKLGQIYLI QSDVDFYDEK QALGMQCRAL NITEDLGQIQ YIFSDKTGTL
TENKMVFRRC SIAGVEYPHE DNSRRLEMYQ AQDCDSELDP SSITVKSKSS LLSLSCRSLN
CNQSSTSLHL LAASDGEMDL QGKPLGTTGC HDVAFSSRTE KGVIPDPQLL LKLNQLSSAE
LLLQDRPEDD PQETAYIVDF FLAITLCNTV VVSSPRLPEP QVSCCSLGFL QVSESPHMAI
KSLESMKLLF QRFSVPQFAS FSTSRSNAPA DSPSSFAQKL FSRGSLSTPA TPQDKVEETK
GLQITAPMEW IPEMDDHARG VAKAGPCGLE AESEALVYAA ESPDEAALVH ATRAYRCTLW
ARSSNQVLVE LPGLGRLAVN LLHILPFDSF RKRMSVVVRH PLTNQVVVYT KGADSVIIKL
VAPLAEGNPT TARLKHIREQ TQRHLDNYAR EGLRTLCVAT KVLEETEYSM WLKKHTFAET
CIENREKLLL ESADELETNL TLLGATGILD RLQEDVPETI EALQGAGIHV WVLTGDKQET
ADACEALLLK LIRVVAEASD SKGDEPSGHM LVIDGQSLEL ALEDSLQEPF LDLAKHCRAV
VCCRSTPLQK SQVVRLVQDR LGVMTLAIGD GANDVSMIQV ANIGVGISGQ EGMQAVMSSD
FAISRFKHLR KLLLVHGHWC YTRLANMTLY FFYKNVAYVN LLFWYQFYCG FSGSTMTNYW
MLIFFNLLFT SAPPLLYGIL DRDASADILQ QLPVLYRAGH FSQAYLPSTF WCTMLDALYQ
SLVCFFVPYF VINTSALLVI LLQQVIQSHT LTWLHGVVLV GSALFYFVFM LVFSATCVTC
NSPSNPLGVD IRHMQDPQFY CVCVLTTVLA LLPRVLYTSV KNSVNPTDLV KAAQLDKLGP
EEQRRGIQNW RTALGYGEPS ITVTAADGDP RGCHPNPVSI NS
//