ATP9B_RAT
ID ATP9B_RAT Reviewed; 1147 AA.
AC D4ABB8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) 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}.
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DR EMBL; CH474021; EDL75216.1; -; Genomic_DNA.
DR RefSeq; NP_001099600.1; NM_001106130.1.
DR AlphaFoldDB; D4ABB8; -.
DR SMR; D4ABB8; -.
DR STRING; 10116.ENSRNOP00000040756; -.
DR PhosphoSitePlus; D4ABB8; -.
DR PaxDb; D4ABB8; -.
DR PeptideAtlas; D4ABB8; -.
DR PRIDE; D4ABB8; -.
DR Ensembl; ENSRNOT00000041380; ENSRNOP00000040756; ENSRNOG00000032039.
DR GeneID; 291411; -.
DR KEGG; rno:291411; -.
DR CTD; 374868; -.
DR RGD; 1563006; Atp9b.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000157071; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; D4ABB8; -.
DR PhylomeDB; D4ABB8; -.
DR TreeFam; TF300590; -.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:D4ABB8; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Proteomes; UP000234681; Chromosome 18.
DR Bgee; ENSRNOG00000032039; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; D4ABB8; baseline and differential.
DR Genevisible; D4ABB8; RN.
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; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
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 3: Inferred from homology;
KW ATP-binding; Golgi apparatus; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1147
FT /note="Probable phospholipid-transporting ATPase IIB"
FT /id="PRO_0000416695"
FT TOPO_DOM 1..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..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..1106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1107..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1130..1147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 509..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 468
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 1147 AA; 129178 MW; 9B3685F2C03102C2 CRC64;
MADQIPLYPV RSAAAAAASH RRAAYYSAVG PGPGADRRGR YQLEDESAHL DEMPLMMSEE
GFENDESDYH TLPRARITRR ERGLEWFVCG GWKFLCTSCC DWLINVCQRK KELKARTVWL
GCPEKCEEKH PRNSIKNQKY NVFTFIPGVL YEQFKFFLNL YFLVVSCSQF VPALKIGYLY
TYWAPLGFVM AVTIAREAID EFRRFQRDKE MNSQLYSKLT VRGKVQVKSS DIQVGDLIIV
EKNQRIPSDM VFLRTSEKAG SCFIRTDQLD GETDWKLKVA VSCTQRLPAL GDLFSISAYV
YAQKPQLDIH SFEGTFTRDD SDPPIHESLS IENTLWASTI VASGTVIGVV IYTGKETRSV
MNTSNPKNKV GLLDLELNQL TKALFLALVV LSVVMVTLQG FAGPWYRNLF RFLLLFSYII
PISLRVNLDM GKAAYGWMIM KDENIPGTVV RTSTIPEELG RLVYLLTDKT GTLTQNEMVF
KRLHLGTVSY GTDTMDEIQS HVLNSYLQVH SQTSGHNPSS APLRRSQSST PKVKKSVSSR
IHEAVKAIAL CHNVTPVYEA RTGITGETEF AEADQDFSDE NRTYQASSPD EVALVRWTES
VGLTLVSRDL ASMQLKTPSG QVLTYCILQM FPFTSESKRM GIIVRDEATA EITFYMKGAD
VAMSTIVQYN DWLEEECGNM AREGLRTLVV AKRTLTEEQY QDFESRYSQA KLSIHDRTLK
VAAVVESLER EMELLCLTGV EDQLQADVRP TLEMLRNAGI KIWMLTGDKL ETATCIAKSS
HLVSRTQDIH IFRPVTNRGE AHLELNAFRR KHDCALVISG DSLEVCLRYY EHELVELACQ
CPAVVCCRCS PTQKAHIVTL LRQHTRKRTC AIGDGGNDVS MIQAADCGIG IEGKEGKQAS
LAADFSITQF RHIGRLLMVH GRNSYKRSAA LGQFVMHRGL IISTMQAVFS SVFYFASVPL
YQGFLMVGYA TIYTMFPVFS LVLDQDVKPE MAILYPELYK DLTKGRSLSF KTFLIWVLIS
IYQGGILMYG ALLLFEAEFV HVVAISFTAL ILTELLMVAL TIRTWHWLMV VAEFLSLGCY
VASLAFLNEY FGIGRVSFGA FLDVAFITTV TFLWKVSAIT VVSCLPLYVL KYLKRKLSPP
SYSKLSS
