ID A0A1D5P8E2_CHICK Unreviewed; 1139 AA.
AC A0A1D5P8E2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 42.
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:ENSGALP00010009662.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010009662.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010009662.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010009662.1};
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 RefSeq; XP_003640794.1; XM_003640746.3.
DR AlphaFoldDB; A0A1D5P8E2; -.
DR SMR; A0A1D5P8E2; -.
DR STRING; 9031.ENSGALP00000048989; -.
DR PaxDb; 9031-ENSGALP00000020629; -.
DR Ensembl; ENSGALT00010017474.1; ENSGALP00010009662.1; ENSGALG00010007319.1.
DR GeneID; 420817; -.
DR KEGG; gga:420817; -.
DR CTD; 374868; -.
DR VEuPathDB; HostDB:geneid_420817; -.
DR GeneTree; ENSGT00940000157071; -.
DR InParanoid; A0A1D5P8E2; -.
DR OMA; IAITTWH; -.
DR OrthoDB; 275833at2759; -.
DR Reactome; R-GGA-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000031323; Expressed in liver and 13 other cell types or tissues.
DR ExpressionAtlas; A0A1D5P8E2; baseline and differential.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR CDD; cd07541; P-type_ATPase_APLT_Neo1-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; PF00122; E1-E2_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; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D5P8E2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
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 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 401..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 927..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1031..1052
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1059..1078
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1098..1122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 118..175
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 893..1131
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1139 AA; 128598 MW; C55AEEE90C8DE695 CRC64;
MADQIPLHPV PRSAQRRAAY YSSASAAQRH NRYQVEDESS HLDEMPLMMS EEGFENDESD
YHTLPRARIS QRKRGLEWFI CGGWKFLCTS CSDWLINICR RKKELKARTV WLGCPEKCEE
KYPKNAIKNQ KYNIFTFIPG VLYEQFKFFL NLYFLVVSCS QFVPALKIGY LYTYWAPLGF
VLTVTVVREA VDEYRRYKRD KEMNSQLYSK LTVRGKVQVK SSDIQVGDLI IVEKNQRIPS
DMVFLRTSEK TGSCFIRTDQ LDGETDWKLK VAVSCTQRLP ALGDLFSINA YVYAQKPQLD
IHSFEGTFTR EDSDPAVHES LSIENTLWAS TVVASGTVIG VVIYTGKETR SVMNTSNPKN
KVGLLDLELN QLTKALFLAL VALSVVMVTL QGFVGPWYRN LFRFLLLFSY IIPISLRVNL
DMGKAAYGWM IMKDDNIPGT VVRTSTIPEE LGRLVYLLTD KTGTLTQNEM IFKRLHLGTV
SYGTDTMDEI QSHIINSYSQ VHSQNSGNST SSTPSRKPQS SAPKVRKSVS SRIHEAVKAI
ALCHNVTPVY ESRAGVSGET EYAEVDQDFS DENRAYQASS PDEVALVQWT ESVGLTLVNR
DLTSMQLKTP GGHILTYYIL QIFPFTSESK RMGIIVRDES SGEITFYMKG ADVAMSTIVQ
YNDWLEEECG NMAREGLRTL VVAKKSLTEE QYQDFESRYN QAKLSIHDRN LKVAAVVESL
EREMELLCLT GVEDQLQADV RPTLEMLRNA GIKIWMLTGD KLETATCIAK SSHLVSRTQD
IHIFRPVTTR GEAHLELNAF RRKHDCALVI SGDSLEVCLK YYEHEFVELA CQCPAVVCCR
CSPTQKAHIV KLLQHHTGKR TCAIGDGGND VSMIQAADCG IGIEGKEGKQ ASLAADFSIT
QFKHIGRLLM VHGRNSYKRS AALGQFVMHR GLIISTMQAV FSSVFYFASV PLYQGFLMVG
YATIYTMFPV FSLVLDQDVK PEMALLYPEL YKDLTKGRSL SFKTFLIWVL ISIYQGGILM
YGALLLFESE FVHVVAISFT ALILTELLMV ALTIRTWHWL MVVAEFLSLG CYVASLAFLN
EYFGIGRVSF GAFLDVAFIT TVTFLWKVSA ITVVSCLPLY ILKYLKRKFS PPSYSKLTS
//
