ID G3T6M7_LOXAF Unreviewed; 1310 AA.
AC G3T6M7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10B {ECO:0000313|Ensembl:ENSLAFP00000009196.3};
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:ENSLAFP00000009196.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000009196.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009196.3,
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:ENSLAFP00000009196.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009196.3};
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 STRING; 9785.ENSLAFP00000009196; -.
DR Ensembl; ENSLAFT00000010996.3; ENSLAFP00000009196.3; ENSLAFG00000010994.3.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000159531; -.
DR InParanoid; G3T6M7; -.
DR OMA; CDRPDTN; -.
DR TreeFam; TF354252; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140351; F:glycosylceramide flippase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IEA:Ensembl.
DR GO; GO:0097212; P:lysosomal membrane organization; IEA:Ensembl.
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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF79; PHOSPHOLIPID-TRANSPORTING ATPASE VB; 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 113..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 355..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1109..1128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1140..1161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1188..1212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1218..1237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1249..1268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1288..1307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 63..118
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1077..1310
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 489..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 148584 MW; 21638F512ED26764 CRC64;
MALSVDSSWH RWQWRVKDGF PQSASEFTPL LSTRRQSQNY NLRQQRVVFP NNRIFHQDWG
KISRRYSGNR ICTTKYTLLT FLPQNLFEQF HRWANLYFLF LVILNWMPSM EVFHREITML
PLAVVLFIIM AKDGMEDFKR YLFDREVNCS SIQIYERKEQ SYVQKRWKDV CVGDFIQMRC
NEIIPADILL LFSSDPSGIC HLETANLDGE TNLKQRRVVK GFSQREALLE PEHFHNTIVC
EKPNNNLNKF KGYMEHPDKT RTGFGSESLL LRGCTIRNTE MAVGIVIYAG HSSKSIFTQQ
GPTTALRDKM KQKIQISPFY SLGILLCLFS GHSLWNRTFE EHPPFDVPDA NGNFLPLTLG
GFYMFLTMII LLQVLIPISL YVSIELVKLG QVFFLHNDLD LYDEETDVPI QCRALNVTED
LGQIQYIFSD KTGTLTENKM VFRRCTIMGS EFSHQENAKR LETPKELDSD SEEWTHYQCL
SFPSRWAQGP TTVRGQGGAQ PLRRSQSAQV PIQGHSRQRS MGRCENSQPP VAFSSPIEKD
VTPDKSLLTK VRDAALWLET LSDTRPAKPS LSTASSIADF FLALTICNSV MVSTTTEPRQ
RVTISSSTKA LGMSLEKIQQ LFQRLKLLSL SQSFSSTAPS DTDLGESLGT NVPTTDSDER
DDSSVCSGCY STDGGYRSST WDQGDILGSG EGPPLEEVLE GPALGLTSPE LCYEAESPDE
AALVHAAHAY SFTLVSRTPE QVTVRLPQGI CLTFDLLCTL GFDSVRKRMS VVVRHPLTGE
IIVYTKGADS VIMDLLEDPA RVTDSNVEKK LRKIQARTQK HLDLYARDGL RTLCIAKKVV
SEEYFQRWAS FRHEAEAALD NRDELLMETA QHLENQLTLL GATGIEDRLQ DGVPDTIAAL
QEAGIQIWVL TGDKQETAIN IAYSCRLLDQ TDTVYTINTE NQETCDSILN CVLEEVKQFH
GPRKPDRKLF GFCLPSEMPS TASVDVVPKV GLVIDGKTLN VIFQGKLEKK FLELTQYCRS
VLCCRSTPLQ KSMIVKLVRD KLRVMTLSIG DGANDVSMIQ AADIGIGISG QEGMQAVMSS
DFAISRFRHL KKLLLVHGHW CYSRLARMVV YFFYKNVCYV NLLFWYQFFC GFSGSTMIDY
WQTIFFNLFF TSVPPLVFGV LDKDISAETL LALPELYKRG QNSECYNLST FWISMVDAFY
QSLVCFFIPY LTYRDSDIDV FTFGTPINTI ALATILLHQA IEMKTWTIIH VLVLVTSFLM
YFVISLVYNA TCVTCNSPTN PYWVMEGQLS DLTFYLVCFL TPVVALLPRF
//
