AT8B2_MOUSE
ID AT8B2_MOUSE Reviewed; 1209 AA.
AC P98199;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phospholipid-transporting ATPase ID;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P98198};
DE AltName: Full=ATPase class I type 8B member 2;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP8B2;
GN Name=Atp8b2 {ECO:0000303|PubMed:30018401, ECO:0000312|MGI:MGI:1859660};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 863-1209.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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, INTERACTION WITH TMEM30A, AND TISSUE
RP SPECIFICITY.
RX PubMed=30018401; DOI=10.1038/s41598-018-29108-z;
RA Wang J., Molday L.L., Hii T., Coleman J.A., Wen T., Andersen J.P.,
RA Molday R.S.;
RT "Proteomic Analysis and Functional Characterization of P4-ATPase
RT Phospholipid Flippases from Murine Tissues.";
RL Sci. Rep. 8:10795-10795(2018).
CC -!- FUNCTION: Catalytic component of P4-ATPase flippase complex, which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC phosphatidylcholine (PC) from the outer to the inner leaflet of the
CC plasma membrane. May contribute to the maintenance of membrane lipid
CC asymmetry. {ECO:0000250|UniProtKB:P98198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:P98198};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P98198};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC Evidence={ECO:0000250|UniProtKB:P98198};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP8B2 and an accessory beta subunit TMEM30A or
CC TMEM30B. {ECO:0000250|UniProtKB:P98198, ECO:0000269|PubMed:30018401}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P98198};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:P98198}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum
CC requires the presence of TMEM30A or TMEM30B.
CC {ECO:0000250|UniProtKB:P98198}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testes (at protein level).
CC {ECO:0000269|PubMed:30018401}.
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; AC163616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF156546; AAF09444.1; -; mRNA.
DR CCDS; CCDS89658.1; -.
DR RefSeq; XP_006501777.1; XM_006501714.3.
DR AlphaFoldDB; P98199; -.
DR SMR; P98199; -.
DR BioGRID; 207713; 1.
DR STRING; 10090.ENSMUSP00000103019; -.
DR iPTMnet; P98199; -.
DR PhosphoSitePlus; P98199; -.
DR EPD; P98199; -.
DR jPOST; P98199; -.
DR MaxQB; P98199; -.
DR PaxDb; P98199; -.
DR PRIDE; P98199; -.
DR ProteomicsDB; 265135; -.
DR Antibodypedia; 34152; 92 antibodies from 16 providers.
DR Ensembl; ENSMUST00000069805; ENSMUSP00000063384; ENSMUSG00000060671.
DR UCSC; uc008qah.1; mouse.
DR MGI; MGI:1859660; Atp8b2.
DR VEuPathDB; HostDB:ENSMUSG00000060671; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000160804; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; P98199; -.
DR OrthoDB; 587717at2759; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 54667; 2 hits in 71 CRISPR screens.
DR PRO; PR:P98199; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P98199; protein.
DR Bgee; ENSMUSG00000060671; Expressed in humerus cartilage element and 239 other tissues.
DR ExpressionAtlas; P98199; baseline and differential.
DR Genevisible; P98199; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0140345; F:phosphatidylcholine flippase activity; ISO:MGI.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030347; ATP8B2.
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:SF46; PTHR24092:SF46; 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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1209
FT /note="Phospholipid-transporting ATPase ID"
FT /id="PRO_0000046366"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..91
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..338
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..922
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 994..1011
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1033..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1082
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 12..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 833
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 837
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98198"
FT CONFLICT 989
FT /note="F -> L (in Ref. 2; AAF09444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1209 AA; 136968 MW; 4722C6D25F280273 CRC64;
MTVPKEIPEK WARAGAPPSW SQKKPSWGTE EERRARANDR EYNEKFQYAS NCIKTSKYNI
VTFLPVNLFE QFQEVANTYF LFLLILQLIP QISSLSWFTT IVPLVLVLTI TAVKDATDDY
FRHKSDNQVN NRHSQVLING VLQQEQWMNV CVGDIIKLEN NQFVAADLLL LSSSEPHGLC
YIETAELDGE TNMKVRQAIP VTSELGDVSQ LARFDGEVIC EPPNNKLDKF SGTLYWKENK
FPLSNQNMLL RGCVLRNTEW CFGLVIFAGP DTKLMQNSGR TKFKRTSIDR LMNTLVLWIF
GFLVCMGVIL AIGNAIWEHE VGTRFQVYLP WDEAVDSAFF SGFLSFWSYI IILNTVVPIS
LYVSVEVIRL GHSYFINWDK KMFCMKKRTP AEARTTTLNE ELGQVEYIFS DKTGTLTQNI
MVFNKCSING HSYGDVFDVL GHKAELGERP EPVDFSFNPL ADKKFLFWDS SLLEAVKMGD
PHTHEFFRLL SLCHTVMSEE KNEGELYYKA QSPDEGALVT AARNFGFVFR SRTPKTITVH
ELGTAITYQL LAILDFNNIR KRMSVIVRNP EGKIRLYCKG ADTILLDRLH PPTQELLSST
TDHLNEYAGD GLRTLVLAYK DLDEEYYEEW ARRRLQASLA QDSREDRLAS IYEEVESDMM
LLGATAIEDK LQQGVPETIA LLTLANIKIW VLTGDKQETA VNIGYSCKML TDDMTEVFVV
TGHTVLEVRE ELRKARKKMV DSSHAVGNGF TYQGNLSSSK LTSVLEAVAG EYALVINGHS
LAHALEADME LEFLETACAC KAVICCRVTP LQKAQVVELV KKYKKAVTLA IGDGANDVSM
IKTAHIGVGI SGQEGIQAVL ASDYSFSQFK FLQRLLLVHG RWSYLRMCKF LCYFFYKNFA
FTMVHFWFGF FCGFSAQTVY DQYFITLYNI VYTSLPVLAM GVFDQDVPEQ RSMEYPKLYE
PGQLNLLFNK REFFICIAQG IYTSVLMFFI PYGVFAEATR DDGTQLADYQ SFAVTVATSL
VIVVSVQIGL DTGYWTAINH FFIWGSLAVY FAILFAMHSN GLFDMFPNQF RFVGNAQNTL
AQPTVWLTIA LTTAVCIMPV VAFRFLRLSL KPDLSDTVRY TQLVRKKQKA QHRCMRRVGR
TGSRRSGYAF SHQEGFGELI MSGKNMRLSS LALSSFSTRS SSSWIESLRR KKSDSANSPS
GGAEKPLKG
