UniProt: H0X845

Database: UniProt
Entry: H0X845_OTOGA

LinkDB:  H0X845_OTOGA 
Original site:  H0X845_OTOGA

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
All databases (32)   

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ID   H0X845_OTOGA            Unreviewed;      1312 AA.
AC   H0X845;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 73.
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:ENSOGAP00000011621.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000011621.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000011621.2}
RP   IDENTIFICATION.
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   EMBL; AAQR03007444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03007445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03007446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 30611.ENSOGAP00000011621; -.
DR   Ensembl; ENSOGAT00000012973.2; ENSOGAP00000011621.2; ENSOGAG00000012969.2.
DR   eggNOG; KOG0206; Eukaryota.
DR   GeneTree; ENSGT00940000159531; -.
DR   HOGENOM; CLU_000846_3_4_1; -.
DR   InParanoid; H0X845; -.
DR   OMA; CDRPDTN; -.
DR   TreeFam; TF354252; -.
DR   Proteomes; UP000005225; 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; 2.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
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   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
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:UP000005225};
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}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT   TRANSMEM        88..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        315..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1111..1130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1142..1163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1193..1214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1251..1270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1290..1309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          56..116
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1079..1312
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          494..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1312 AA;  148677 MW;  53EC89AFF9BCCF99 CRC64;
     LSVDSSWLRW QWRVREGSAQ SASEATPLLS AEKARRSYNL RRQRVVFPNN STFHQDWEKV
     SRSYPGNRIH TTKYTLFTFL PQNLFEQFHR WANLYFLLLV ILNWIPSMEV FHREITMLPL
     AIVLFIIMVK DGLEDLKRHR FDKAINCSNI RIYPRKVHNY VRKPWKDVRV GDFIQVQCNE
     IIPADILLLF SSDPSGICHL ETANLDGETN LKQRRVVKGF SQQEVQFQPE RFCNTIVCEK
     PNNHLNRFKG YMEHPDQTRT GFNSENLLLR GCTVRNTEVA VGIVIYAGHE TKAMLNNSGP
     RYKRSKIERR MNTDIFFCIG ILFLMCLIGA VGHSLWNGTF EEHPPFDVPD TNGNFLPLAL
     EGVYMFLTMI ILLQVLIPIS LYVSIELVKL GQVFFLHNDL DLYDEETDSS IQCRALNITE
     DLGQIQYIFS DKTGTLTENK MVFRRCTIMG SEYSHQENAK RLETPKELDS DSEEWTQYQC
     LSFPARWVQG PATMRGQKSA QPLRRCQSAR VPIQGHSRQR SMGHYENSQP AVAFSSSIEK
     DVTPDKNLLT KVRDAALWLE SLSDGRATKP SFSTTSSIAD FFLALTICNS VMVSTTTEPR
     QRKVTIPPST KALGMSLEKI QQLFQRLKLS SLSQSFSSTA PSDTDLGESL GANAPTMDSD
     EKDDSSVCSG GYSTDGGYRS SVWDQGDILG SGSGASLEEE LETPAPGLAG PELCYEAESP
     DEAALVHAAH AYSFTLVSRT PEQVTVRLPQ GTCLTFDLLC TLGFDSVRKR MSVVVRHPLT
     GEIVVYTKGA DSVIMDLLED PASVTDIDLE KKLKKTQART QKHLDLYARD GLRTLCIAKK
     VISEEDFRRW ASFRHEAEAS LENRDELLME TAQHLENRLT LLGATGIEDR LQEGVPDTIA
     ALREAGIQVW VLTGDKQETA VNIAYSCRLL DQTDTVYTIN TENQETCDSI LNCTLEEVKQ
     FHEPQKPDRK LFGFRLRSKT PSTTSAAVLP EVGLVIDGKT LNAIFLGKLE KKFLELTGYC
     RSVLCCRCTP LQKSMIVKLV RDKLSVMTLS IGDGANDVSM IQAADIGIGI SGQEGMQAVM
     SSDFAISRFR HLKKLLLVHG HWCYSRLARM VVYYFYKNVC YVNLLFWYQF FCGFSASTMI
     DYWQMIFFNL FFTSLPPLIF GILDKDISAE TLLALPELYK SGQNSECYNL STFWISMLDA
     FYQSLICFFI PYLTYKDSDI DVFTFGTPIN TISLTTILLH QAMEMKTWTI IHGLILLGSF
     LMYFAVSLLY NATCVTCNSP TNPYWVMEVQ FSDLTFYLVC FLTPVAALLP RF
//

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