ID G3U3U9_LOXAF Unreviewed; 1394 AA.
AC G3U3U9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10D {ECO:0000313|Ensembl:ENSLAFP00000022507.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022507.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000022507.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022507.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000022507.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022507.1};
RG Ensembl;
RL Submitted (NOV-2023) 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 -!- 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}.
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DR Ensembl; ENSLAFT00000029937.1; ENSLAFP00000022507.1; ENSLAFG00000014000.3.
DR GeneTree; ENSGT00940000156728; -.
DR HOGENOM; CLU_000846_3_4_1; -.
DR Proteomes; UP000007646; 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; 2.
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; 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|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:UP000007646};
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 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1113..1132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1144..1165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1193..1215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1227..1245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1252..1277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1297..1316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 68..123
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1081..1326
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 474..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 157159 MW; A0E70D1087CADF10 CRC64;
MTEPLQWTRY HWRRLIGGAN RDNDERPYNY SSLLACGGKT SQTPKLAGKH RVVVPHLRPF
KEEYEKFSGA YMNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLVTKVY SPKEKKYIDR CWKDVTVGDF
IRLSCNEVIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVARGYTEQ DSEVDPEKFS
SRIECESPNN DLNRFRGFLE HSNKKRVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA
MLNNSGPRYK RSKLERRANT DVLWCVLLLI IMCFTGALGH EIWLSRYEDV PFFNIPEPDG
RLTSPLLAGF YMFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQNDVDFY NEKMDSTVQC
RALNITEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY SHKENAKRLE SYQEAVSEDE
DFADTPSGSP SDMAKPKAHS CRTAHNGPLG SKPLNHLSGS SFALGNGEGA SEVPHSRQTA
FSSPIETDVV PDTRLLEKFS QITPQLFTPP DEMAHSLPLE TLCIMDFFIA LAICNTVVVS
APNQPRQKVR LSSLTGMPIK SLEEIKNLFQ RLSVRRSSSP SLASGKEPSS GVPNAFVNRL
SLFSRIKLAS PVEEEGSQMS ESPQGSSNST CHEETEKQNS GAGVTNGKVD SLPGQPLASD
LCYEAESPDE AALVYAARAY QCTLQSRTPE QVMVDFAALG PLTFQLLHIL PFDSVRKRMS
VVVRHPLSNQ VVVYTKGADS VIMELLSVAS PDGTSLEKQQ MIREKTQKHL DDYAKRGLRT
LCIAKKVMSD TEYAEWLKNH FLAETSIDNR EELLFESAMR LENKLTLLGA TGIEDRLQEG
VPESIEALQK AGIKIWMLTG DKQETAVNIA YACKLLEPDD KLFILNTQSK DACEMLMSTI
LKELQKNNRA SPEQVPLSEN LHQPPVPQDL GLRAGLVITG KTLEFALQES LQRQFLELTA
WCRAVVCCRA TPLQKSEVVK LVRNHLRVMT LAIGDGANDV SMIQVADVGI GISGQEGMQA
VMASDFAISQ FRHLSKLLLV HGHWCYTRLS NMILYFFYKN VAYVNLLFWY QFFCGFSGTS
MTDYWVLIFF NLLFTSAPPV IYGVLEKDVS AETLIQLPEL YTSGQKSEAY LPLTFWITLL
DAFYQSLVCF FVPYYTYQGS DIDIFTFGNP LNTAALFIIL LHLVIESKSL TWIHMVVIIG
SILSYFLFAL AFGATCITCN PPSNPYWIMQ EHLLDPMFYL VCVLTTCIAL LPRFMYRVFQ
ESLFPSPILR AKHLDRLTPE EKTEALKKWK KTGKMDQAMS KYAGYSAATS GRRPMSGHST
VSAMMLATSY AIEQ
//