ID A0A0J7L9T1_LASNI Unreviewed; 1839 AA.
AC A0A0J7L9T1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=RF55_350 {ECO:0000313|EMBL:KMR04921.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMR04921.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMR04921.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMR04921.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
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:KMR04921.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBMM01000107; KMR04921.1; -; Genomic_DNA.
DR STRING; 67767.A0A0J7L9T1; -.
DR PaxDb; 67767-A0A0J7L9T1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0005254; F:chloride channel activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR021134; Bestrophin-like.
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:SF91; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF01062; Bestrophin; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 305..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1265..1282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1294..1315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1322..1345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1368..1393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1521..1539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..329
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1151..1390
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1839 AA; 204469 MW; A9799857B25214AC CRC64;
MSEDDAQEAA SEEIERQGSL YVFPGAGRPS CATSSSSSIS TASLQPPLSS FLRGGDHSIA
TSTTTTTSNT TTMTTSATTT MTSTSTKISN GDEDEDAVEE VTSPARRRPL PKTHARSASH
GGVLADCTTG RQTYGSFLGA LTTVGSATSA GRPSALKKPG HQRAFSQGQV ADVTQGQSAV
TGHHRVGSRT DFILPPGHRE EGRPPTAGRM PSFRGHSRQA SRSESIYTIR RSVAPPWWRR
LWAHCFGSLP EEPRLRTIVP NHLVSPKTPK SQHPNGDRAD NRVRTTKYTA LSFLPRNLLE
QFHRVANLYF IFIVLLNWVP AINAFGKEVA MIPVVFVLGV TALKDFFEDR RRLASDRRVN
NSTCRVYVSE GDRYMKVAWK DVKVGDLVHL SNNELVPADL LLLRSSDPQG LAYLDTCNLD
GESNLKQRQV VRGFLDLQDT FKPFKFRSVV EVDQPSTRIY RFHGAVVHPN GGRVPVSTEN
LLLRECVLKN TDFVEGIVIY AGHETKALLN NGGPRYKRSR LEKQMNRDVK WCVVILLVLC
VIGAFGCRFW LSAYTGLTVV PFLPVLQEPI YESILTFLTF VIIFQVMIPL SLYVTIEMAK
VGQVYHIGHD PALHDTETGR KAECRALNIT EELGQVQYVF SDKTGTLTEN KMLFRRCAVG
GQDYSHMGDN ENLSPCSRLK EDLLISTFRH RLQEFLIVLA TCNTVVVNSQ PHHDIMNSSG
VIEEPQKNGT SPTRPKLLNV TSIPSLGIGL LGRKLSPDGQ KRRSPDTKNS DELLQSPAIY
EAESPDELAL VYAARAYDVK LVKRTPRSAI VSFPDKSTLA FEILHVLPFD SNRKCMSVLL
RHPYTGEIVL YSKGADSTML PALSPGDENT VASASIRQYL QSYARQGLRT LVMTRKTLTS
QEYEMWREKH DEAELATENR ERRIRDSYAT LESHLTLLGA TGIEDKLQVG VPETMAALVA
AGIVVWVLTG DKPETAVNVA YSARLFSPAM QLLQLQARSK SVAETLIRGY LESACKESAN
NGHPQQPGMM AAGIADPVGM YPNYDSTERD AHRIGSPWPR QRALVVDGKT LTVILDPRSG
LTGPFLELTK TCSSVLACRA TPLQKAYIVR IVKKQLGMRT LAIGDGANDV SMIQTADVGV
GISGQEGTQA VMAADFAISR FSMLSRLLLL HGHWCYDRLA RMILYFFYKN ATFVFLVFWF
QLYCGFSGAV MIDQIYLMLY NLLFTSLPPL ALGIYDRVAA PRVLLSSPEL YIRGRLGLVY
QPHSFWLTIG DALYQSIVIF FITKEVYYDS IIDIWEFGTT IMTACIVVML LHAAIEIRSW
TIIHIGAIFG SLGIFFVFCL FYNAVCVNCM GLPGSFWVME KAITHHTYWF TVVLTSVLAL
MPRYVCVCLT VVLTNVAPRV KKRFPTLEHF VDSGLLLDNE IMIFHSLNAK FPKPSKHWLP
IVWATSIVTR ARKEGRIRDD FAVKTLIDEL NKFRGMCGTI LQYDTISVPL VYTQVVTLAV
YTYFLTCVMG RQWIQNSNSV IDLYFPVFTT LQFFFYMGWL KVAETLINPF GEDDDDFEVN
WLIDRNLQVS YLIVDEMHHD HPELIRDQYW DEIFPTELPY TAASQPFREE HPQHSTAGIQ
LSAAQQELQP SSVKIEDLAP ELSGYQKFNS EIADDAASGI HFTADGKISR SASRVSNRER
NLSGGSTSSN LGGSLTRINS VTSVLKRLFS KEDRPDGGTT SGTKTPAKIT NSISSASLQI
RPPGTSGSMR IGVIEEVDEQ MTLTSLRQSN DNNRPHVKTI FPQGPPPPSD PVDVPRSTQF
HKCDVLSRSA PARGGVVTVA GSMESGTMRE RPSALRLVI
//
