ATP9B_MOUSE
ID ATP9B_MOUSE Reviewed; 1146 AA.
AC P98195; Q68FM3; Q99LI3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 03-AUG-2022, entry version 165.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 709-1146 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-1095 (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11015572; DOI=10.1152/physiolgenomics.1999.1.3.139;
RA Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA Williamson P.L., Schlegel R.A.;
RT "Differential expression of putative transbilayer amphipath transporters.";
RL Physiol. Genomics 1:139-150(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P98195-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98195-2; Sequence=VSP_035908;
CC -!- TISSUE SPECIFICITY: Found in most tissues except spleen and muscle.
CC Most abundant in testis. Also detected in fetal tissues.
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; BC003246; AAH03246.1; -; mRNA.
DR EMBL; BC079626; AAH79626.1; -; mRNA.
DR EMBL; AF155913; AAF08476.1; -; mRNA.
DR CCDS; CCDS29370.1; -. [P98195-2]
DR CCDS; CCDS89288.1; -. [P98195-1]
DR RefSeq; NP_001188498.1; NM_001201569.1.
DR RefSeq; NP_056620.2; NM_015805.3.
DR AlphaFoldDB; P98195; -.
DR SMR; P98195; -.
DR BioGRID; 206103; 1.
DR STRING; 10090.ENSMUSP00000089394; -.
DR iPTMnet; P98195; -.
DR PhosphoSitePlus; P98195; -.
DR SwissPalm; P98195; -.
DR EPD; P98195; -.
DR MaxQB; P98195; -.
DR PaxDb; P98195; -.
DR PRIDE; P98195; -.
DR ProteomicsDB; 277133; -. [P98195-1]
DR ProteomicsDB; 277134; -. [P98195-2]
DR DNASU; 50771; -.
DR GeneID; 50771; -.
DR KEGG; mmu:50771; -.
DR UCSC; uc008fti.2; mouse. [P98195-1]
DR CTD; 374868; -.
DR MGI; MGI:1354757; Atp9b.
DR eggNOG; KOG0210; Eukaryota.
DR InParanoid; P98195; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; P98195; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 50771; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Atp9b; mouse.
DR PRO; PR:P98195; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P98195; protein.
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:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Golgi apparatus; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1146
FT /note="Probable phospholipid-transporting ATPase IIB"
FT /id="PRO_0000046378"
FT TOPO_DOM 1..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 960..961
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..1011
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1033..1040
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1041..1061
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1062..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1087..1105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1129..1146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 508..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 873
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 877
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1091..1101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035908"
FT CONFLICT 366
FT /note="N -> K (in Ref. 1; AAH79626)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="V -> I (in Ref. 1; AAH79626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1146 AA; 129017 MW; 334AAEE291DFDC2E CRC64;
MADQIPLYPV RSAGAAASHR RAAYYSSAGP GPGADRRGRY QLEDESAHLD EMPLMMSEEG
FENDESDYHT LPRARITRRK RGLEWFVCGG WKFLCTSCCD WLINVCQRKK ELKARTVWLG
CPEKCEEKHP RNSIKNQKYN VFTFIPGVLY EQFKFFLNLY FLVVSCSQFV PALKIGYLYT
YWAPLGFVLA VTIAREAIDE FRRFQRDKEM NSQLYSKLTV RGKVQVKSSD IQVGDLIIVE
KNQRIPSDMV FLRTSEKAGS CFIRTDQLDG ETDWKLKVAV SCTQRLPALG DLFSISAYVY
AQKPQLDIHS FEGTFTREDS DPPIHESLSI ENTLWASTIV ASGTVIGVVI YTGKETRSVM
NTSNPNNKVG LLDLELNQLT KALFLALVVL SVVMVTLQGF AGPWYRNLFR FLLLFSYIIP
ISLRVNLDMG KAAYGWMIMK DENIPGTVVR TSTIPEELGR LVYLLTDKTG TLTQNEMVFK
RLHLGTVSYG TDTMDEIQSH VLNSYLQVHS QPSGHNPSSA PLRRSQSSTP KVKKSVSSRI
HEAVKAIALC HNVTPVYEAR AGITGETEFA EADQDFSDEN RTYQASSPDE VALVRWTESV
GLTLVSRDLA SMQLKTPSGQ VLTYCILQMF PFTSESKRMG IIVRDESTAE ITFYMKGADV
AMSTIVQYND WLEEECGNMA REGLRTLVVA KRTLTEEQYQ DFESRYSQAK LSIHDRALKV
AAVVESLERE MELLCLTGVE DQLQADVRPT LEMLRNAGIK IWMLTGDKLE TATCIAKSSH
LVSRTQDIHV FRPVTSRGEA HLELNAFRRK HDCALVISGD SLEVCLRYYE HELVELACQC
PAVVCCRCSP TQKAHIVTLL RQHTRKRTCA IGDGGNDVSM IQAADCGIGI EGKEGKQASL
AADFSITQFR HIGRLLMVHG RNSYKRSAAL GQFVMHRGLI ISTMQAVFSS VFYFASVPLY
QGFLMVGYAT IYTMFPVFSL VLDQDVKPEM AILYPELYKD LTKGRSLSFK TFLIWVLISI
YQGGILMYGA LLLFEDEFVH VVAISFTALI LTELLMVALT IRTWHWLMVV AEFLSLGCYV
ASLAFLNEYF GIGRVSFGAF LDVAFITTVT FLWKVSAITV VSCLPLYVLK YLKRKLSPPS
YSKLSS
