ATP9B_BOVIN
ID ATP9B_BOVIN Reviewed; 1136 AA.
AC A1A4J6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable phospholipid-transporting ATPase IIB;
DE EC=7.6.2.1;
DE AltName: Full=ATPase class II type 9B;
GN Name=ATP9B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-54 is the initiator.
CC {ECO:0000305}.
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DR EMBL; BC126606; AAI26607.1; -; mRNA.
DR RefSeq; NP_001073724.1; NM_001080255.1.
DR AlphaFoldDB; A1A4J6; -.
DR SMR; A1A4J6; -.
DR STRING; 9913.ENSBTAP00000010477; -.
DR PaxDb; A1A4J6; -.
DR PRIDE; A1A4J6; -.
DR Ensembl; ENSBTAT00000010477; ENSBTAP00000010477; ENSBTAG00000001224.
DR GeneID; 510301; -.
DR KEGG; bta:510301; -.
DR CTD; 374868; -.
DR VEuPathDB; HostDB:ENSBTAG00000001224; -.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000157071; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; A1A4J6; -.
DR OMA; IAITTWH; -.
DR OrthoDB; 587717at2759; -.
DR TreeFam; TF300590; -.
DR Reactome; R-BTA-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000001224; Expressed in spermatid and 105 other tissues.
DR ExpressionAtlas; A1A4J6; baseline and differential.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-KW.
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:InterPro.
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 Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030355; ATP9B.
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 PANTHER; PTHR24092:SF50; PTHR24092:SF50; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Golgi apparatus; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1136
FT /note="Probable phospholipid-transporting ATPase IIB"
FT /id="PRO_0000356354"
FT TOPO_DOM 1..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..939
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..962
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..1012
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1013..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1034..1041
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1063..1066
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1067..1087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1088..1098
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1099..1119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1120..1136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 514..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 469
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 874
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 878
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1136 AA; 127457 MW; E89A2F49EC4F4E60 CRC64;
MADQIPLYPV RSAAAVAAAN RKRAAYFSSA GPGPGADRPS RYQLEDESAH LDEMPLMMSE
EGFENDESDY HTLPRARITR RKRGLEWFVC GGWKFLCTSC CDWLINICQR KRELKARTVW
LGCPEKCEEK HPRNSIKNQK YNIFTFIPGV LYEQFKFFLN LYFLIVSCSQ FVPALKIGYL
YTYWAPLGFV LAVTIMREAV DEFRRFQRDK EVNSQLYSKL TVRGKVQVKS SDIQVGDLII
VEKNQRIPSD MVFLRTSEKA GSCFIRTDQL DGETDWKLKV AVSCTQRLPA LGDLFSINAY
VYAQKPQLDI HSFEGTFTRE DSDPPVHESL SIENTLWAST VVASGTVIGV VIYTGKETRS
VMNTSNPKNK VGLLDLELNQ LTKALFLALV ALSVVMVTLQ GFAGPWYRSL FRFLLLFSYI
IPISLRVNLD MGKAAYGWMI MRDEHIPGTV VRTSTIPEEL GRLVYLLTDK TGTLTQNEMV
FKRLHLGTVS YGTDTMDEIQ NHLVNAYTQT QCQAGGSSAA STPPRKAPSS APKVRRSVSS
RVHEAVKAVA LCHNVTPVYE ARGAAGETEV AEADQDFSDD NRTYQASSPD EVALVQWTES
VGLTLVSRDL TSMQLRTPGG QILTYCILQT FPFTSESKRM GVIVRDESTA EITFYMKGAD
VAMASIVQYN DWLEEECGNM AREGLRTLVV AKRALTEEQY QDFESRYNQA KLSLHDRTLK
VAAVVESLER EMELLCLTGV EDQLQADVRP TLEMLRNAGI KIWMLTGDKL ETATCIAKSS
HLVSRTQDTH VFRPVTSRGE AHLELNAFRR KHDCALVISG DSLEVCLKYY EHEFVELACQ
CPAVVCCRCS PTQKAHIVKL LQQHTGRRTC AIGDGGNDVS MIQAADCGIG IEGKEGRQAS
LAADFSITRF KHVGRLLMVH GRSSYKRSAA LGQFVMHRGL IISTMQAVFS SVFYFASVPL
YQGFLMVGYA TVYTMFPVFS LVLDQDVKPE MAMLYPELYK DLTKGRSLSF KTFLVWVLIS
IYQGGILMFG ALVLFESEFV HVVAISFTAL VLTELLMVAL TVRTWHWLMV VAQLLSLGCY
VASLAFLNEY FDVAFITTVT FVWKVSAITV VSCLPLYVLK YLKRKLSPPS YSKLSS
