ID A0A672V2J5_STRHB Unreviewed; 1413 AA.
AC A0A672V2J5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-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=ATP10B {ECO:0000313|Ensembl:ENSSHBP00005021538.1};
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:ENSSHBP00005021538.1, ECO:0000313|Proteomes:UP000472266};
RN [1] {ECO:0000313|Ensembl:ENSSHBP00005021538.1, 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:ENSSHBP00005021538.1}
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 Ensembl; ENSSHBT00005025680.1; ENSSHBP00005021538.1; ENSSHBG00005018243.1.
DR GeneTree; ENSGT00940000159531; -.
DR InParanoid; A0A672V2J5; -.
DR OMA; CDRPDTN; -.
DR Proteomes; UP000472266; Chromosome 15.
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: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: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 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 290..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 333..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1073..1092
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1104..1125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1149..1175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1212..1232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1258..1279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 34..93
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1041..1281
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 490..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1413 AA; 160183 MW; FC913957346354E0 CRC64;
YLSLGRGKVK KKKKKNENKR VIISNLPFES KKWKENPNRY YGSNKIKTTK YTILTFLPKN
IYEQFHRFAN IYFVVIALLN FVPVVNAFQP EVSMIPICVI MAITAIKDVW EDFRRYKLDK
EINHMGCYIY SREEHAYVEK CWKDVQVGDF VQLQCNETIP ADILLLYSSD QNGICHLETA
NLDGETNLKQ RQVVMGFSSQ NTFFEPELFQ NTIICEMPNN DLNKFKGYME QPNHERVGFN
IESLLLRGCT IRNTEVAIGI VIYAGHETKA MLNNNGPRYK RSKIERQMNM DIFLCVGLLF
VMCLVGAVGH GIWTGSFSEH PPYDVPDENG EYLSPFLAGF YMFLTMIILL QVLIPISLYV
SIELVKLGQV FLIHNDVDLY NEEADLPIQC RALNITEDLG QIQYIFSDKT GTLTENKMVF
RRCTVDGIEF SHQENARRLE THKELDLDDE DFAKLQHFTL PPTNIETPDT YKQKTMRPLR
RCQSARAHFQ GHTRNRSLGR RDSNQSQVAF SSPIEKDVTP DSRLLRRVRE AALQTENLSP
FIHMKTSTSL TDFFLALAIC NTVLVSTATE PRQRVTVPPP IKPSGITLEK IHQIFQRLKL
ASLSQSFSSS QSSSDLGASF SARNTEEQLA ALDCCDNGND CCASGRGDEL QGKDSTDIGS
ASLDEVFKSV TNSSLPTDFC YEAESPDEAA LVYAAQAYGF TLVSRTPEQV TVRLPQGTLL
TFDILCTLGF DSVRKRMSVV VRHPLTKEIV VYTKGADSVI MDMLEDSAKD DISKEKKMKR
IKEKTQKHLD YYARDGLRTL CIAKKVLNED DFQKWANFRR EAEAAIDNRD ELLMETAQHL
ETKLTLLGAT GIEDRLQDGV PDTIAALQEA GIQIWVLTGD KQETAVNIAY SCKLLNQRDT
VFTINTESKE TCESLLNLTL EEVRKNYEVE KPRRKFFGII PASFASSEAP GPEFGLVIDG
RTLNVIFQGG LEEKFLALTK HCHSVLCCRS TPLQKSMVAK LVRRQLKVMT LSIGDGANDV
SMIQAADIGI GISGQEGMQA VMASDFAISR FKHLKKLLLV HGHWCYARLA KMVIYFFYKN
VSYVNLLFWY QFFCGFSGST MIDYWQMIFF NLFFTSVPPL LFGVLDRDVS AETLLGLPEL
YKNGQNSEIY NLSTFIITML DAFYQSLVCF FVPYLTYEDS DIDVFSFGNP MNTISLLTIL
LHQALEMKTW TLFHLVTMIG SVVFYLVFSL IYNASCVLCN PPANPYWIME RQLSDPTFYL
LCLITPVIAL LPRFFIFALR GTIGTSLILK AQQLDKLPKG QQDLEIQKLR SRKQPTSVAA
AVSHRDTESQ RLSTSEVNPL RKQTPEKGYY FFNRWAEEES TATDPSAGPF CGHYPLVPSR
VTTPGQDSGK LTKGNVNNFN HGSHRRSVSA VTL
//
