ID A0A672TS58_STRHB Unreviewed; 1117 AA.
AC A0A672TS58;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP9B {ECO:0000313|Ensembl:ENSSHBP00005005050.1};
OS Strigops habroptila (Kakapo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Strigops.
OX NCBI_TaxID=2489341 {ECO:0000313|Ensembl:ENSSHBP00005005050.1, ECO:0000313|Proteomes:UP000472266};
RN [1] {ECO:0000313|Ensembl:ENSSHBP00005005050.1, ECO:0000313|Proteomes:UP000472266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jarvis E.D., Howard J., Rhie A., Phillippy A., Korlach J., Digby A.,
RA Iorns D., Eason D., Robertson B., Raemaekers T., Howe K., Lewin H.,
RA Damas J., Hastie A., Tracey A., Chow W., Fedrigo O.;
RT "Strigops habroptila (kakapo) genome, bStrHab1, primary haplotype, v2.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSHBP00005005050.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A672TS58; -.
DR Ensembl; ENSSHBT00005006120.1; ENSSHBP00005005050.1; ENSSHBG00005002277.1.
DR GeneTree; ENSGT00940000157071; -.
DR Proteomes; UP000472266; Chromosome 1.
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; cd07541; P-type_ATPase_APLT_Neo1-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; 3.
DR PANTHER; PTHR24092:SF50; PHOSPHOLIPID-TRANSPORTING ATPASE IIB-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000472266};
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 176..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 379..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 905..927
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 933..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 983..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1037..1056
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1076..1100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 122..179
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 871..1109
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 479..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 126144 MW; EDA9E0BB789380D4 CRC64;
IRTKMLMSCV EGVAEVCAHR NRHQESKLKK LNGNLKYQVE DESSHLDEMP LMMSEEGFEN
DESDYHTLPR ARISQRRRGL EWFICGGWKF LCTSCSDWLI NICRRKKELK ARTVWLGCPE
KCEEKYPKNA IKNQKYNVFT FIPGVLYEQF KFFLNLYFLV VSCSQFVPAL KIGYLYTYWA
PLGFVLTVTV VREAVDEFRR YKRDKEMNSQ LYSKLTVRGK VQVKSSDIQV GDLIIVEKLD
GETDWKLKVA VSCTQRLPAL GDLFSINAYV YAQKPQLDIH SFEGTFTRED SDPAVHESLS
IENTLWASTV VASGTVIGVV IYTGKETRSV LNTSNPKNKV GLLDLELNQL TKALFLALVA
LSVVMVTLQG FVGPWYRNLF RFLLLFSYII PISLRVNLDM GKAAYGWMIM KDDNIPGTVV
RTSTIPEELG RLVYLLTDKT GTLTQNEMIF KRLHLGTVSY GTDTMDEIQS HIINSYSQMH
SQNSGNSTSS TPSRKPQSSA PKVRKSVSSR IHEAVKAIAL CHNVTPVYES RAGVSGETEY
AEVDQDFSDE NRTYQASSPD EVALVQWTES VGLTLVNRDL TSMQLKTPGG HILTYYILQI
FPFTSESKRM GIIVRDESSG EITFYMKGAD VAMSTIVQYN DWLEEECGNM AREGLRTLVV
AKKSLTEEQY QDFESRYNQA KLSIHDRNLK VAAVVESLER EMELLCLTGV EDQLQADVRP
TLEMLRNAGI KIWMLTGDKL ETATCIAKSS HLVSRTQDIH IFRPVTTRGE AHLELNAFRR
KHDCALVISG DSLEVCLKYY EHEFVELACQ CPAVVCCRCS PTQKAHIVKL LQHHTGKRTC
AIGDGGNDVS MIQAADCGIG IEGKEGKQAS LAADFSITQF KHIGRLLMVH GRNSYKRSAA
LGQFVMHRGL IISTMQAVFS SVFYFASVPL YQGFLMVGYA TIYTMFPVFS LVLDQDVKPE
MALLYPELYK DLTKGRSLSF KTFLIWVLIS IYQGGILMYG ALLLFESEFV HVVAISFTAL
ILTELLMVAL TIRTWHWLMV VAEFLSLGCY VASLAFLNEY FGIGRVSFGA FLDVAFITTV
TFLWKVSAIT VVSCLPLYIL KYLKRKFSPP SYSKLTS
//
