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Probable cation-transporting ATPase 13A3 (EC 3.6.3.-)

 AT133_MOUSE             Reviewed;        1219 AA.
Q5XF89;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
28-MAR-2018, entry version 129.
RecName: Full=Probable cation-transporting ATPase 13A3;
EC=3.6.3.-;
Name=Atp13a3; Synonyms=Gm542;
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 [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
PubMed=15381061; DOI=10.1016/j.bbrc.2004.08.156;
Schultheis P.J., Hagen T.T., O'Toole K.K., Tachibana A., Burke C.R.,
McGill D.L., Okunade G.W., Shull G.E.;
"Characterization of the P5 subfamily of P-type transport ATPases in
mice.";
Biochem. Biophys. Res. Commun. 323:731-738(2004).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, 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).
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5XF89-1; Sequence=Displayed;
Name=2;
IsoId=Q5XF89-2; Sequence=VSP_036301;
-!- TISSUE SPECIFICITY: Expression is greatest in liver, followed by
kidney, colon, stomach, brain and small intestine. Isoform 1 is
highly expressed in the kidney while isoform 2 is highly expressed
in the brain. {ECO:0000269|PubMed:15381061}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type V subfamily. {ECO:0000305}.
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EMBL; BK005558; DAA05589.1; -; mRNA.
CCDS; CCDS49820.1; -. [Q5XF89-1]
CCDS; CCDS49821.1; -. [Q5XF89-2]
RefSeq; NP_001121566.1; NM_001128094.1. [Q5XF89-1]
RefSeq; NP_001121568.1; NM_001128096.1. [Q5XF89-2]
UniGene; Mm.8924; -.
ProteinModelPortal; Q5XF89; -.
STRING; 10090.ENSMUSP00000128224; -.
iPTMnet; Q5XF89; -.
PhosphoSitePlus; Q5XF89; -.
SwissPalm; Q5XF89; -.
EPD; Q5XF89; -.
PaxDb; Q5XF89; -.
PeptideAtlas; Q5XF89; -.
PRIDE; Q5XF89; -.
Ensembl; ENSMUST00000061350; ENSMUSP00000051645; ENSMUSG00000022533. [Q5XF89-1]
Ensembl; ENSMUST00000100013; ENSMUSP00000128224; ENSMUSG00000022533. [Q5XF89-2]
GeneID; 224088; -.
KEGG; mmu:224088; -.
UCSC; uc012aee.1; mouse. [Q5XF89-2]
UCSC; uc012aef.1; mouse. [Q5XF89-1]
CTD; 79572; -.
MGI; MGI:2685387; Atp13a3.
eggNOG; KOG0208; Eukaryota.
eggNOG; ENOG410XRCA; LUCA.
GeneTree; ENSGT00530000063001; -.
HOGENOM; HOG000171813; -.
HOVERGEN; HBG065757; -.
InParanoid; Q5XF89; -.
KO; K14951; -.
OMA; DYYYYAF; -.
OrthoDB; EOG091G01IL; -.
TreeFam; TF300331; -.
PRO; PR:Q5XF89; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022533; -.
Genevisible; Q5XF89; MM.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005388; F:calcium-transporting ATPase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006544; P-type_TPase_V.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00690; Cation_ATPase_N; 1.
Pfam; PF12409; P5-ATPase; 1.
SUPFAM; SSF56784; SSF56784; 3.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 2.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR01657; P-ATPase-V; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Hydrolase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 1219 Probable cation-transporting ATPase 13A3.
/FTId=PRO_0000363358.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TRANSMEM 202 222 Helical. {ECO:0000255}.
TRANSMEM 229 249 Helical. {ECO:0000255}.
TRANSMEM 406 426 Helical. {ECO:0000255}.
TRANSMEM 445 465 Helical. {ECO:0000255}.
TRANSMEM 937 957 Helical. {ECO:0000255}.
TRANSMEM 959 979 Helical. {ECO:0000255}.
TRANSMEM 996 1016 Helical. {ECO:0000255}.
TRANSMEM 1067 1087 Helical. {ECO:0000255}.
TRANSMEM 1099 1119 Helical. {ECO:0000255}.
TRANSMEM 1137 1157 Helical. {ECO:0000255}.
COMPBIAS 227 230 Poly-Tyr.
ACT_SITE 494 494 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 879 879 Magnesium. {ECO:0000250}.
METAL 883 883 Magnesium. {ECO:0000250}.
MOD_RES 813 813 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 1154 1154 E -> ESFFLDTVLWKVVFNRDKQGECRFSTTQPPQ (in
isoform 2).
{ECO:0000303|PubMed:15381061}.
/FTId=VSP_036301.
SEQUENCE 1219 AA; 137469 MW; 186F60AE9CEAA82E CRC64;
MDKEERKTIN KGQEDEMEIH GYNLCRWKLA MVFVGVICTG GFLLLLLYWL PEWRVKATCV
RAAVKDCEVV LLRTTDEFRV WFCAKIHFLP VENQPNLNAK CLVNEVSNGH AVHLTEENRC
EMNKYSQSQS QQMRYFTHHS IRYFWNDAIH NFDFLKGLDE GVSCASLYEK HSAGLTQGMH
AYRKLIYGVN EIAVKVPSVF KLLIKEVLNP FYIFQLFSVI LWSVDEYYYY ALAIVIMSVV
SIISSLYSIR KQYVMLHDMV ATHSTVRVSV CRENEEIEEI FSTDLVPGDV MIIPLNGTVM
PCDAVLINGT CIVNESMLTG ESVPVTKTNL PNPSVDVKGM GEEQYSPETH KRHTLFCGTT
VIQTRFYTGE LVKAIVVRTG FSTSKGQLVR SILYPKPTDF KLYRDAYLFL LCLVVVAGIG
FIYTIINSIL NEKEVQEIII KSLDIITITV PPALPAAMTA GIVYAQRRLK KVGIFCISPQ
RINICGQLNL VCFDKTGTLT EDGLDLWGIQ RVENTRFLLP EDNVCSEMLV KSQFVACMAT
CHSLTKIEGV LSGDPLDLKM FEAIGWILEE ATEEETALHN RIMPTVVRPS KQLLPEPTTA
GNQEMELFEL PAIYEIGIVR QFPFSSALQR MSVVARTLGE KRMDAYMKGA PEVVASLCKP
ETVPVDFEKV LEDYTKQGFR VIALAHRKLE SKLTWHKVQH ISRDAIENNM DFMGLIIMQN
KLKQETPAVL EDLHKANIRT VMVTGDNMLT AVSVARDCGM ILPQDKVIIA EALPPKDGKV
AKINWHYTDS LSQCSESSAI DSEAIPIKLA HDSLEDLEVT RYHFAMNGKS FSVILEHFQD
LVPKLMLHGT VFARMAPDQK TQLVEALQNV DYFVGMCGDG ANDCGALKRA HGGISLSELE
ASVASPFTSK TPSISCVPNL IREGRAALMT SFCVFKFMAL YSIIQYFSVT LLYSILSNLG
DFQFLFIDLA IILVVVFTMS LNPAWKELVA QRPPSGLISG ALLFSVLSQI VISVGFQSLG
FFWVKQYKVC DPNSDVCNTT RSACWNSSHL YNGTELDSCK IQNYENTTVF FISSFQYLTV
AVAFSKGKPF RQPCYKNYFF VISVIILYVF ILFIMLHPVA SVDQVLEIMC VPYQWRIYML
IIVLINAFVS ITVEESVDRW GKCCLSWALS CRKKTPKAKY MYLAQELRFD PEWPPKPQTT
TEAKAVVKEN GSCQIITIA


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