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Phospholipid-transporting ATPase 11C (EC 3.6.3.1) (ATPase class VI type 11C) (P4-ATPase flippase complex alpha subunit ATP11C)

 AT11C_MOUSE             Reviewed;        1129 AA.
Q9QZW0; Q3KQR4;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
12-SEP-2018, entry version 143.
RecName: Full=Phospholipid-transporting ATPase 11C;
EC=3.6.3.1;
AltName: Full=ATPase class VI type 11C;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP11C;
Name=Atp11c;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thyroid;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 767-1129 (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=11015572;
Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
Williamson P.L., Schlegel R.A.;
"Differential expression of putative transbilayer amphipath
transporters.";
Physiol. Genomics 1:139-150(1999).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
FUNCTION.
PubMed=21423172; DOI=10.1038/ni.2012;
Siggs O.M., Arnold C.N., Huber C., Pirie E., Xia Y., Lin P.,
Nemazee D., Beutler B.;
"The P4-type ATPase ATP11C is essential for B lymphopoiesis in adult
bone marrow.";
Nat. Immunol. 12:434-440(2011).
[5]
FUNCTION, AND INVOLVEMENT IN DEFECTIVE LYMPHOPOIESIS.
PubMed=21423173; DOI=10.1038/ni.2011;
Yabas M., Teh C.E., Frankenreiter S., Lal D., Roots C.M., Whittle B.,
Andrews D.T., Zhang Y., Teoh N.C., Sprent J., Tze L.E.,
Kucharska E.M., Kofler J., Farell G.C., Broer S., Goodnow C.C.,
Enders A.;
"ATP11C is critical for the internalization of phosphatidylserine and
differentiation of B lymphocytes.";
Nat. Immunol. 12:441-449(2011).
[6]
FUNCTION, AND INVOLVEMENT IN CHOLESTASIS.
PubMed=21518881; DOI=10.1073/pnas.1104631108;
Siggs O.M., Schnabl B., Webb B., Beutler B.;
"X-linked cholestasis in mouse due to mutations of the P4-ATPase
ATP11C.";
Proc. Natl. Acad. Sci. U.S.A. 108:7890-7895(2011).
-!- FUNCTION: Catalytic component of a P4-ATPase flippase complex
which catalyzes the hydrolysis of ATP coupled to the transport of
aminophospholipids from the outer to the inner leaflet of various
membranes and ensures the maintenance of asymmetric distribution
of phospholipids. Phospholipid translocation seems also to be
implicated in vesicle formation and in uptake of lipid signaling
molecules. Required for B cell differentiation past the pro-B cell
stage. Seems to mediate phosphatidylserine (PS) flipping in pro-B
cells. May be involved in the transport of cholestatic bile acids.
{ECO:0000269|PubMed:21423172, ECO:0000269|PubMed:21423173,
ECO:0000269|PubMed:21518881}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
phosphate + phospholipid(Side 2).
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit.
Interacts with TMEM30A (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}. Note=Efficient exit from the endoplasmic reticulum
requires the presence of TMEM30A. Some cell membrane localization
observed in the presence of TMEM30B (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9QZW0-1; Sequence=Displayed;
Name=2;
IsoId=Q9QZW0-2; Sequence=VSP_022222, VSP_022223;
-!- DISEASE: Note=Mice defective in Atp11c show defective B
lymphopoiesis, specifically in mature bone marrow,
hyperbilirubinemia linked to mild cholestasis and hepatocellular
carcinoma. {ECO:0000269|PubMed:21423173,
ECO:0000269|PubMed:21518881}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC106087; AAI06088.1; -; mRNA.
EMBL; AF156547; AAF09445.1; -; mRNA.
CCDS; CCDS40988.1; -. [Q9QZW0-1]
RefSeq; NP_001032952.1; NM_001037863.1. [Q9QZW0-1]
RefSeq; XP_006528153.1; XM_006528090.3. [Q9QZW0-1]
RefSeq; XP_006528154.1; XM_006528091.3. [Q9QZW0-1]
RefSeq; XP_011245917.1; XM_011247615.2. [Q9QZW0-1]
RefSeq; XP_011245918.1; XM_011247616.1. [Q9QZW0-1]
UniGene; Mm.490394; -.
ProteinModelPortal; Q9QZW0; -.
BioGrid; 236409; 1.
STRING; 10090.ENSMUSP00000099066; -.
iPTMnet; Q9QZW0; -.
PhosphoSitePlus; Q9QZW0; -.
SwissPalm; Q9QZW0; -.
PaxDb; Q9QZW0; -.
PRIDE; Q9QZW0; -.
Ensembl; ENSMUST00000101527; ENSMUSP00000099066; ENSMUSG00000062949. [Q9QZW0-1]
Ensembl; ENSMUST00000206006; ENSMUSP00000146015; ENSMUSG00000108408. [Q9QZW0-1]
GeneID; 320940; -.
KEGG; mmu:320940; -.
UCSC; uc009tia.1; mouse. [Q9QZW0-1]
CTD; 286410; -.
MGI; MGI:1859661; Atp11c.
eggNOG; KOG0206; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00910000144008; -.
HOGENOM; HOG000202528; -.
HOVERGEN; HBG050601; -.
InParanoid; Q9QZW0; -.
KO; K01530; -.
OMA; VLKMFTD; -.
OrthoDB; EOG091G03B1; -.
PhylomeDB; Q9QZW0; -.
BRENDA; 3.6.3.1; 3474.
Reactome; R-MMU-936837; Ion transport by P-type ATPases.
ChiTaRS; Atp11c; mouse.
PRO; PR:Q9QZW0; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000062949; Expressed in 246 organ(s), highest expression level in left lobe of liver.
CleanEx; MM_ATP11C; -.
ExpressionAtlas; Q9QZW0; baseline and differential.
Genevisible; Q9QZW0; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IBA:GO_Central.
GO; GO:0045332; P:phospholipid translocation; IMP:UniProtKB.
GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:UniProtKB.
GO; GO:0002329; P:pre-B cell differentiation; IMP:UniProtKB.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030363; ATP11C.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
PANTHER; PTHR24092:SF38; PTHR24092:SF38; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 3.
SUPFAM; SSF81653; SSF81653; 2.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Coiled coil;
Complete proteome; Endoplasmic reticulum; Hydrolase; Lipid transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1129 Phospholipid-transporting ATPase 11C.
/FTId=PRO_0000046374.
TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TOPO_DOM 105 287 Extracellular. {ECO:0000255}.
TRANSMEM 288 308 Helical. {ECO:0000255}.
TOPO_DOM 309 343 Cytoplasmic. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TOPO_DOM 365 876 Extracellular. {ECO:0000255}.
TRANSMEM 877 897 Helical. {ECO:0000255}.
TOPO_DOM 898 905 Cytoplasmic. {ECO:0000255}.
TRANSMEM 906 926 Helical. {ECO:0000255}.
TOPO_DOM 927 952 Extracellular. {ECO:0000255}.
TRANSMEM 953 973 Helical. {ECO:0000255}.
TOPO_DOM 974 988 Cytoplasmic. {ECO:0000255}.
TRANSMEM 989 1009 Helical. {ECO:0000255}.
TOPO_DOM 1010 1023 Extracellular. {ECO:0000255}.
TRANSMEM 1024 1044 Helical. {ECO:0000255}.
TOPO_DOM 1045 1066 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1067 1087 Helical. {ECO:0000255}.
TOPO_DOM 1088 1129 Extracellular. {ECO:0000255}.
COILED 607 643 {ECO:0000255}.
COILED 695 726 {ECO:0000255}.
ACT_SITE 409 409 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 816 816 Magnesium. {ECO:0000250}.
METAL 820 820 Magnesium. {ECO:0000250}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NB49}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NB49}.
MOD_RES 1113 1113 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NB49}.
MOD_RES 1123 1123 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NB49}.
VAR_SEQ 833 835 Missing (in isoform 2).
{ECO:0000303|PubMed:11015572}.
/FTId=VSP_022222.
VAR_SEQ 1097 1129 RNLSCRRASDSLSARPSVRPLLLRTFSDESNIL -> NPNL
ELPMLLSYKHIDRGCS (in isoform 2).
{ECO:0000303|PubMed:11015572}.
/FTId=VSP_022223.
CONFLICT 786 791 LCCRMA -> VCCADQ (in Ref. 2; AAF09445).
{ECO:0000305}.
SEQUENCE 1129 AA; 129240 MW; EE82DFD1F0669294 CRC64;
MFRRTLNRLC AGEEKRVGTR TVFVGNHPIS GTEPYIAQRF CDNRIVSSKY TLWNFLPKNL
FEQFRRIANF YFLIIFLVQV TVDTPTSPVT SGLPLFFVIT VTAIKQGYED WLRHRADNEV
NKSAVYIIEN AKRVRKESEK IKVGDVVEVQ ANETFPCDLI LLSSCTTDGT CYVTTASLDG
ESNCKTHYAV RDTIALCTAE SIDNLRATIE CEQPQPDLYR FVGRISIYSN SIEAVARSLG
PENLLLKGAT LKNTKKIYGV AVYTGMETKM ALNYQGKSQK CSAVEKSINA FLIVYLFILL
TKAAVCTTLK YVWQSSPYND EPWYNQKTQK ERETFQVLKM FTDFLSFMVL FNFIIPVSMY
VTVEMQKFLG SFFISWDKDF FDEEINEGAL VNTSDLNEEL GQVDYVFTDK TGTLTENSME
FIECCIDGHK YKGTTQEVDG LSQTDGPLAY FDKADKNREA LFLRALCLCH TVEMKTNDDV
DGPVEGAGFT YISSSPDEIA LVKGAKRFGF TFLGNQNGYI RVENQRKEIE EYELLHTLNF
DSVRRRMSVI VRTQKGDILL FCKGADSSIF PRVHSHQIEL TKDHVERNAM DGYRTLCVAF
KEIPPDDFER INAQLVEAKM ALQDREEKLE KVFDEIETNM NLIGATAVED KLQDQAAETI
EALHAAGLKV WVLTGDKMET AKSTCYACRL FQTNTELLEL TTKTIEESER KEDRLHELLI
EYRKKLLHEF PKSTRSLKKA WTEHQEYGLI IDGSTLSLIL NSSQDCSSNN YKSIFLQICM
KCTAVLCCRM APLQKAQIVR MVKNLKGSPI TLSIGDGAND VSMILESHVG IGIKGKEGRQ
AARNSDYSVP KFKHLKKLLL VHGHLYYVRI AHLVQYFFYK NLCFILPQFL YQFFCGFSQQ
PLYDAAYLTM YNICFTSLPI LAYSLLEQHI NIDTLTADPR LYMKITGNAM LQLGPFLHWT
FLAAFEGTVF FFGTYFLFQT SSLEDNGKIY GNWTFGTIVF TVLVFTVTLK LALDTRFWTW
INHFVIWGSL AFYVFFSFFW GGIIWPFLKQ QRMYFVFAQM LCSVSTWLAI ILLIFISLFP
EILLIVVKNV RRRSARRNLS CRRASDSLSA RPSVRPLLLR TFSDESNIL


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