AT11B_MOUSE
ID AT11B_MOUSE Reviewed; 1175 AA.
AC Q6DFW5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Phospholipid-transporting ATPase IF;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:Q9Y2G3};
DE AltName: Full=ATPase class VI type 11B;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP11B;
GN Name=Atp11b {ECO:0000303|PubMed:30018401, ECO:0000312|MGI:MGI:1923545};
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 [GENOMIC DNA].
RA Birren B., Nusbaum C., Lander E., Abouelleil A., Allen N., Anderson M.,
RA Anderson S., Arachchi H.M., Barna N., Bastien V., Bloom T., Boguslavkiy L.,
RA Boukhgalter B., Camarata J., Chang J., Choepel Y., Collymore A., Cook A.,
RA Cooke P., Corum B., DeArellano K., Diaz J.S., Dodge S., Dooley K.,
RA Dorris L., Erickson J., Faro S., Ferreira P., FitzGerald M., Gage D.,
RA Galagan J., Gardyna S., Graham L., Grand-Pierre N., Hafez N., Hagopian D.,
RA Hagos B., Hall J., Horton L., Hulme W., Iliev I., Johnson R., Jones C.,
RA Kamat A., Karatas A., Kells C., Landers T., Levine R., Lindblad-Toh K.,
RA Liu G., Liu X., Lui A., Mabbitt R., MacLean C., Macdonald P., Major J.,
RA Manning J., Matthews C., McCarthy M., Meldrim J., Meneus L., Mihova T.,
RA Mlenga V., Murphy T., Naylor J., Nguyen C., Nguyen T., Nicol R., Norbu C.,
RA O'Connor T., O'Donnell P., O'Neil D., Oliver J., Peterson K., Phunkhang P.,
RA Pierre N., Rachupka A., Ramasamy U., Raymond C., Retta R., Rise C.,
RA Rogov P., Roman J., Schauer S., Schupback R., Seaman S., Severy P.,
RA Smith C., Spencer B., Stange-Thomann N., Stojanovic N., Stubbs M.,
RA Talamas J., Tesfaye S., Theodore J., Topham K., Travers M., Vassiliev H.,
RA Venkataraman V.S., Viel R., Vo A., Wilson B., Wu X., Wyman D., Young G.,
RA Zainoun J., Zembek L., Zimmer A., Zody M.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TMEM30A, SUBUNIT, AND
RP TISSUE 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 a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids, phosphatidylserines (PS) and
CC phosphatidylethanolamines (PE), from the outer to the inner leaflet of
CC intracellular membranes. May contribute to the maintenance of membrane
CC lipid asymmetry in endosome compartment.
CC {ECO:0000250|UniProtKB:Q9Y2G3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP11B and an accessory beta subunit TMEM30A.
CC {ECO:0000269|PubMed:30018401}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y2G3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y2G3}. Early endosome
CC {ECO:0000250|UniProtKB:Q9Y2G3}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y2G3}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9Y2G3}. Note=Exit from the endoplasmic
CC reticulum requires the presence of TMEM30A, but not TMEM30B. In the
CC presence of TMEM30A, mainly located in recycling endosomes.
CC {ECO:0000250|UniProtKB:Q9Y2G3}.
CC -!- TISSUE SPECIFICITY: Expressed in retina, brain, liver, testes and
CC kidney (at protein level). {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; AC157780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076603; AAH76603.1; -; mRNA.
DR CCDS; CCDS38414.1; -.
DR RefSeq; NP_083846.2; NM_029570.3.
DR AlphaFoldDB; Q6DFW5; -.
DR SMR; Q6DFW5; -.
DR STRING; 10090.ENSMUSP00000029257; -.
DR PhosphoSitePlus; Q6DFW5; -.
DR EPD; Q6DFW5; -.
DR jPOST; Q6DFW5; -.
DR MaxQB; Q6DFW5; -.
DR PaxDb; Q6DFW5; -.
DR PeptideAtlas; Q6DFW5; -.
DR PRIDE; Q6DFW5; -.
DR ProteomicsDB; 328776; -.
DR Antibodypedia; 33765; 135 antibodies from 30 providers.
DR DNASU; 76295; -.
DR Ensembl; ENSMUST00000029257; ENSMUSP00000029257; ENSMUSG00000037400.
DR GeneID; 76295; -.
DR KEGG; mmu:76295; -.
DR UCSC; uc008oyt.1; mouse.
DR CTD; 23200; -.
DR MGI; MGI:1923545; Atp11b.
DR VEuPathDB; HostDB:ENSMUSG00000037400; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000156162; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q6DFW5; -.
DR OMA; TMWWESH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q6DFW5; -.
DR TreeFam; TF326897; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 76295; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Atp11b; mouse.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6DFW5; protein.
DR Bgee; ENSMUSG00000037400; Expressed in retinal neural layer and 242 other tissues.
DR ExpressionAtlas; Q6DFW5; baseline and differential.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
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:0015917; P:aminophospholipid transport; IEA:InterPro.
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; IPR030362; ATP11B.
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:SF57; PTHR24092:SF57; 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 ATP-binding; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Lipid transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1175
FT /note="Phospholipid-transporting ATPase IF"
FT /id="PRO_0000452279"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 910..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 407
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 824
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
SQ SEQUENCE 1175 AA; 133536 MW; 738F535697754720 CRC64;
MWRWVRQQLG FDPPHQSDTR TIYIANRFPQ NGLYTPQKFI DNRIISSKYT IWNFVPKNLF
EQFRRVANFY FLIIFLVQLM IDTPTSPITS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN
GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE
TNLKTHVSVP ETAVLQTVAN LDSLIAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE
SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLIILISE
AIISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
ECSINGLKYQ EINGKLVPEG PSPDSTEGEV PFLGSLSHLS NSAHLTATSL RTSPESETEL
IKEHDLFFKA VSLCHTVQIS NVQTDGIGDG PWQPNLAPAQ LEYYASSPDE KALVEAAARA
GIIFVGISEE TMEVKVLGRL ERYKLLHILE FDSDRRRMSV IVQAPSGEKL LFAKGAESSI
LPKCIGGEIA KTRIHVDEFA LKGLRTLCIA YRQFTAKEYE DVDRRLFEAR TALQHREEKL
ADAFQYIEKD LILLGATAVE DRLQDKVRET IEALRMAGIK VWVLTGDKHE TAVSVSLSCG
HFHRTMNILE LINQKSDSGC AEQLRQLARR ITEDHVIQHG LVVDGTSLSL ALREHEKLFM
EVCRNCSAVL CCRMAPLQKA KVIRLIKISP EKPITLAVGD GANDVSMIQE AHVGIGIMGK
EGRQAARNSD YAIARFKFLS KLLFVHGHFY YIRIATLVQY FFYKNVCFIT PQFLYQFYCL
FSQQTLYDSV YLTLYNICFT SLPVLIYSLV EQHIDPHVLQ SKPTLYRDIS KNGLLSIKAF
LYWTVLGFSH AFIFFFGSYF LVGKDTSLLG NGQMFGNWTF GTLVFTVMVI TVTVKMALET
HFWTWINHLV TWGSIIFYFI FSLFYGGILW PFLGSQNMYF VFIQLLSSGS AWFAILLMVV
TCLFIDVVKK VFDRQLHPTS TEKAQLAEAH SSVKCLDSVC CFPGETPCAS VGRMLERVIG
RCSPNHISRL WNASDPFYTN DRSILTLSPM DSSTC
