AT133_MOUSE
ID AT133_MOUSE Reviewed; 1219 AA.
AC Q5XF89;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Polyamine-transporting ATPase 13A3;
DE AltName: Full=Putrescine transporting ATPase {ECO:0000250|UniProtKB:Q9H7F0};
DE EC=7.6.2.16 {ECO:0000250|UniProtKB:Q9H7F0};
GN Name=Atp13a3 {ECO:0000312|MGI:MGI:2685387}; Synonyms=Gm542;
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 [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=15381061; DOI=10.1016/j.bbrc.2004.08.156;
RA Schultheis P.J., Hagen T.T., O'Toole K.K., Tachibana A., Burke C.R.,
RA McGill D.L., Okunade G.W., Shull G.E.;
RT "Characterization of the P5 subfamily of P-type transport ATPases in
RT mice.";
RL Biochem. Biophys. Res. Commun. 323:731-738(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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).
CC -!- FUNCTION: ATP-driven pump involved in endocytosis-dependent polyamine
CC transport. Uses ATP as an energy source to transfer polyamine precursor
CC putrescine from the endosomal compartment to the cytosol.
CC {ECO:0000250|UniProtKB:Q9H7F0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + putrescine(out) = ADP + H(+) + phosphate +
CC putrescine(in); Xref=Rhea:RHEA:29995, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:326268, ChEBI:CHEBI:456216; EC=7.6.2.16;
CC Evidence={ECO:0000250|UniProtKB:Q9H7F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29996;
CC Evidence={ECO:0000250|UniProtKB:Q9H7F0};
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9H7F0}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9H7F0};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H7F0}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Mainly targeted to the recycling endosomes and to a
CC lesser extent to the early and late endosomes.
CC {ECO:0000250|UniProtKB:Q9H7F0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XF89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XF89-2; Sequence=VSP_036301;
CC -!- TISSUE SPECIFICITY: Expression is greatest in liver, followed by
CC kidney, colon, stomach, brain and small intestine. Isoform 1 is highly
CC expressed in the kidney while isoform 2 is highly expressed in the
CC brain. {ECO:0000269|PubMed:15381061}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; BK005558; DAA05589.1; -; mRNA.
DR CCDS; CCDS49820.1; -. [Q5XF89-1]
DR CCDS; CCDS49821.1; -. [Q5XF89-2]
DR RefSeq; NP_001121566.1; NM_001128094.1. [Q5XF89-1]
DR RefSeq; NP_001121568.1; NM_001128096.1. [Q5XF89-2]
DR AlphaFoldDB; Q5XF89; -.
DR SMR; Q5XF89; -.
DR BioGRID; 230239; 1.
DR STRING; 10090.ENSMUSP00000051645; -.
DR iPTMnet; Q5XF89; -.
DR PhosphoSitePlus; Q5XF89; -.
DR SwissPalm; Q5XF89; -.
DR EPD; Q5XF89; -.
DR jPOST; Q5XF89; -.
DR MaxQB; Q5XF89; -.
DR PaxDb; Q5XF89; -.
DR PeptideAtlas; Q5XF89; -.
DR PRIDE; Q5XF89; -.
DR ProteomicsDB; 277084; -. [Q5XF89-1]
DR ProteomicsDB; 277085; -. [Q5XF89-2]
DR Antibodypedia; 33892; 65 antibodies from 14 providers.
DR Ensembl; ENSMUST00000061350; ENSMUSP00000051645; ENSMUSG00000022533. [Q5XF89-1]
DR Ensembl; ENSMUST00000100013; ENSMUSP00000128224; ENSMUSG00000022533. [Q5XF89-2]
DR GeneID; 224088; -.
DR KEGG; mmu:224088; -.
DR UCSC; uc012aee.1; mouse. [Q5XF89-2]
DR UCSC; uc012aef.1; mouse. [Q5XF89-1]
DR CTD; 79572; -.
DR MGI; MGI:2685387; Atp13a3.
DR VEuPathDB; HostDB:ENSMUSG00000022533; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000155941; -.
DR HOGENOM; CLU_001828_0_0_1; -.
DR InParanoid; Q5XF89; -.
DR OMA; GFKFYED; -.
DR OrthoDB; 172453at2759; -.
DR TreeFam; TF300331; -.
DR BioGRID-ORCS; 224088; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Atp13a3; mouse.
DR PRO; PR:Q5XF89; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5XF89; protein.
DR Bgee; ENSMUSG00000022533; Expressed in secondary oocyte and 252 other tissues.
DR ExpressionAtlas; Q5XF89; baseline and differential.
DR Genevisible; Q5XF89; MM.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0015417; F:ABC-type polyamine transporter activity; IBA:GO_Central.
DR GO; GO:0015594; F:ABC-type putrescine transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:1902047; P:polyamine transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF12409; P5-ATPase; 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; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endosome; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1219
FT /note="Polyamine-transporting ATPase 13A3"
FT /id="PRO_0000363358"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT INTRAMEM 29..49
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TOPO_DOM 50..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..228
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..444
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..936
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 937..957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 958
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 959..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1066
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1067..1087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1088..1098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1099..1119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1120..1136
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1158..1219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT ACT_SITE 494
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT BINDING 494..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 746
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 879..883
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 879
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1154
FT /note="E -> ESFFLDTVLWKVVFNRDKQGECRFSTTQPPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15381061"
FT /id="VSP_036301"
SQ 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
