ID A0A2J7QMT4_9NEOP Unreviewed; 1134 AA.
AC A0A2J7QMT4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B7P43_G09443 {ECO:0000313|EMBL:PNF29892.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF29892.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF29892.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF29892.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) 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}.
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:PNF29892.1}.
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DR EMBL; NEVH01013203; PNF29892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7QMT4; -.
DR Proteomes; UP000235965; 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 Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 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; 1.
DR PANTHER; PTHR24092:SF91; 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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000235965};
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 88..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 979..997
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1036..1059
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1079..1100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 865..1109
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 354..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 127094 MW; 5967C800F3D17CF9 CRC64;
MFEPRKFKSV VEVDGPTTKI YRFHGAIVHP SGERIPVGTE NLLLRECVLK NTDFVEGIVV
YAGHETKAML NNGGPRYKRS NLERQMNLDV IWCVLILFVL CVIGAVGCKL WLSSYENYDN
HSVPFIPLAE SPITEGFLGF WTFIIILQVM IPLSLYVTLE MAKLMQVYHI HNDVDMYDPE
TNKQIECRAL NISEELGQVQ YIFSDKTGTL TENKMIFRRC SIAGVDYNHP PPENVQNLKL
RPGAPMPLLV NTQLQEDLCQ VDLRQAPERS DLRQILHAQR IQEFLLLLSV CNTVVVSRHP
HHDMMDASGV IESVPSVLGS HSGASVNVAS SHAHRDNNLS SITARQSVVM AVGSTQTDKY
SRLSESRSVT PSPPPPHAHS YPPHTSINFP TSDATPFGRR ALNYPGSGKP PMEFPHQPIL
SPINSSSEST PTADSPTASQ AIKQVSRPKL LNVPSLLSVC SSKKSSISKS GNSQNSQQRS
ATPSPCELKP IFEAESPDEL ALVDAAYSYN CRLVKRTPQF ATVALPGEGV LEFEILQVFP
FDSARKCMSV VLSHPITREK ILYCKGADST ILPQLAPSDD FMMQQLIFRT QQHLNSYARQ
GLRVLVMARR TLSDVEYNDW LRKHGEATLM IENRERRLRE SYSRLETNLT LLGATGIEDR
LQDGVPETIN ALISAGIVVW VLTGDKPETA INVAYSAKLF SPQMELLKLS ARSKDAAEST
IMFYLADIER ESPPDIGITS GPPGLNQVGV FARANVSSGD APSQHQRGPL HSNKKRALVI
DGKTLTYILD QRSNLQKPFL QLTRYCSSVL CCRATPLQKA YIVRVVKEQL KMRTLAIGDG
ANDVSMIQTA DVGIGISGQE GMQAVMASDF ALSRFKYLER FLLVHGHWCY DRLSRMVLYF
FHKNATSVFL VFWYQLYCGF SGSVMIDQMY LMLYNLLFTS LPPVVIGVYD QDAPEELLLA
RPNLYRQGRL GLVYKPHSFW ITMADSLYQS IVIFFLAEGA YHDTDVGIWE FGTTIATSCL
FVMLFHVAIE TRSWTVIHVF SIFVSIGIYF AFSLVYNSLC VQCLNLPSNY WVVQHAASST
TYWLVVFLSV VMALIPRFVW RTIETSLFPR DVTKAVLDKR RAARRGPPIM EPRM
//
