ID U3I446_ANAPP Unreviewed; 1153 AA.
AC U3I446;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B1 {ECO:0000313|Ensembl:ENSAPLP00000002017.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000002017.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000002017.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000002017.2}
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; U3I446; -.
DR Ensembl; ENSAPLT00000002598.2; ENSAPLP00000002017.2; ENSAPLG00000002575.2.
DR GeneTree; ENSGT00940000158002; -.
DR HOGENOM; CLU_000846_7_2_1; -.
DR Proteomes; UP000016666; Chromosome Z.
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; 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; 1.
DR PANTHER; PTHR24092:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 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; 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:UP000016666};
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 119..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 291..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 901..922
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 984..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1023..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1048..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1095..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 76..145
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 870..1124
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 132232 MW; 89E1AD9B3D7387DF CRC64;
MISERDSETT FDEDSQPNDE EVPYSDDDTE DELDSRQPGV ESEQAQTNRG TEERRETLRK
DCSWQVKAND QHFYEQPQFK RTILLCFKKS KYAGNAIKTY KYNPITFLPL NLFEQFKRAA
NFYFLVLLIL QAIPQISTLS WYTTLVPLLL VLGITAVKDL VDDIARHKMD NEVNNRTCEV
IRDGSETNLK FKMALEVTDK YLQEESAMAD FNGLIECEEP NNRLDKFTGT LFWRNTSYAL
DADKILLRGC KIRNTDFCHG VVIFAGADTK IMKNSGKTKF KRTKIDSLMN YMVYTIFLVL
ILLSAGLAIG HTYWEQQIGN SSWYLYDAED YSPPYRGFLN FWGYIIVLNT MVPISLYVSV
EVIRLGQSYF INWDLQMYYS EKDTAAKART TTLNEQLGQI HYIFSDKTGT LTQNIMTFKK
CCINGQRYGD CRDGAGQLPS HPEQVDFSWN MYADGKFLFY DHYLIEQIKS RKDPEIQKFF
LLLAICHTVM VDVSDGQINY QAASPDEGAL VTAARNFGYV FLSRTQNTIT ISEMGIEKTY
DVLAILDFNS DRKRMSVIVR DSNGNIRLYC KGADTVIYER LHPRNVKREA TEEALDVFAN
ETLRTLCLCY KDISDDEFEA WNKKFMEASV ATTNRDEALD KVYEEIEKNL ILLGATAIED
KLQDGVPETI SKLSKADIKI WVLTGDKKET AENIGFSCDL LTDETTICYG EDISALLQTR
LENQRNRAGS STHSSLRMNE PFFQGSRDRA LIITGSWLNE ILLEKKKKKK KLKLKFPRTA
EEKQKQIEKR RKAEAYKEQQ QKNFVDLACE CKAVICCRVT PKQKAMVVEL VKKYKKAITL
AIGDGANDVN MIKTAHIGVG ISGQEGMQAV MSSDYSFGQF RYLQRLLLVH GRWSYIRMCK
FLRYFFYKNF AFTLVHIWYS FFNGFSAQTA YEDWFITLYN VLYSSLPVLL VGLFDQDVSD
KLSLRFPRLY VLGQKDLLFN YKKFFLSLLH GAITSLIIFF IPYGAYLQTM GQDGEAPSDY
QSFAITAASS LVFVVNLQIG LDTSYWTFVN AFSVFGSIAI YFGITFDLHS AGIHVLFPSA
FQFTGTAPNA LRQPYLWLTM ALTIAVCLLP VVAQRFLSMT IWPSESDRVS KGLCYFQHMF
TYRHGIGTDT GNK
//
