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   14-DEC-2022, entry version 154.
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   ProteomicsDB; 328776; -.
DR   Antibodypedia; 33765; 135 antibodies from 29 providers.
DR   DNASU; 76295; -.
DR   Ensembl; ENSMUST00000029257; ENSMUSP00000029257; ENSMUSG00000037400.
DR   GeneID; 76295; -.
DR   KEGG; mmu:76295; -.
DR   UCSC; uc008oyt.1; mouse.
DR   AGR; MGI:1923545; -.
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: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; PHOSPHOLIPID-TRANSPORTING ATPASE IF-RELATED; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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
//