AT134_MOUSE
ID AT134_MOUSE Reviewed; 1193 AA.
AC Q5XF90; Q80V28; Q8C105; Q8C184;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable cation-transporting ATPase 13A4;
DE EC=7.2.2.-;
DE AltName: Full=P5-ATPase isoform 4;
GN Name=Atp13a4;
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 [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION, 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 [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=29505581; DOI=10.1371/journal.pone.0193228;
RA Soerensen D.M., Holemans T., van Veen S., Martin S., Arslan T.,
RA Haagendahl I.W., Holen H.W., Hamouda N.N., Eggermont J., Palmgren M.,
RA Vangheluwe P.;
RT "Parkinson disease related ATP13A2 evolved early in animal evolution.";
RL PLoS ONE 13:e0193228-e0193228(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:29505581};
CC Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5XF90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XF90-2; Sequence=VSP_031263;
CC Name=3;
CC IsoId=Q5XF90-3; Sequence=VSP_031262;
CC Name=4;
CC IsoId=Q5XF90-4; Sequence=VSP_031264, VSP_031265;
CC -!- TISSUE SPECIFICITY: Expressed in brain and stomach.
CC {ECO:0000269|PubMed:15381061}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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; AK028776; BAC26113.1; -; mRNA.
DR EMBL; AK029303; BAC26383.1; -; mRNA.
DR EMBL; AC175464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048410; AAH48410.1; -; mRNA.
DR EMBL; BK005557; DAA05588.1; -; mRNA.
DR CCDS; CCDS49816.1; -. [Q5XF90-1]
DR CCDS; CCDS49817.1; -. [Q5XF90-4]
DR CCDS; CCDS59623.1; -. [Q5XF90-2]
DR RefSeq; NP_001158085.1; NM_001164613.1.
DR RefSeq; XP_017172445.1; XM_017316956.1.
DR AlphaFoldDB; Q5XF90; -.
DR SMR; Q5XF90; -.
DR STRING; 10090.ENSMUSP00000138479; -.
DR iPTMnet; Q5XF90; -.
DR PhosphoSitePlus; Q5XF90; -.
DR PaxDb; Q5XF90; -.
DR PRIDE; Q5XF90; -.
DR ProteomicsDB; 277051; -. [Q5XF90-1]
DR ProteomicsDB; 277052; -. [Q5XF90-2]
DR ProteomicsDB; 277053; -. [Q5XF90-3]
DR ProteomicsDB; 277054; -. [Q5XF90-4]
DR DNASU; 224079; -.
DR GeneID; 224079; -.
DR KEGG; mmu:224079; -.
DR UCSC; uc007ywd.2; mouse. [Q5XF90-4]
DR CTD; 84239; -.
DR MGI; MGI:1924456; Atp13a4.
DR eggNOG; KOG0208; Eukaryota.
DR InParanoid; Q5XF90; -.
DR PhylomeDB; Q5XF90; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 224079; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Atp13a4; mouse.
DR PRO; PR:Q5XF90; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5XF90; protein.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IDA: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:0005388; F:P-type calcium transporter activity; IC:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
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 SMART; SM00831; Cation_ATPase_N; 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; 1.
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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1193
FT /note="Probable cation-transporting ATPase 13A4"
FT /id="PRO_0000318676"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT INTRAMEM 33..53
FT /evidence="ECO:0000305|PubMed:29505581"
FT TOPO_DOM 54..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..224
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..437
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 902..922
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 923..933
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 955..973
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 974..994
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 995..1036
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1071
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1072..1092
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1093..1105
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT ACT_SITE 487
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 853
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..295
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031262"
FT VAR_SEQ 407..425
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031263"
FT VAR_SEQ 815..878
FT /note="ILINGTIFARMSPGQKSSLVEEFQKLDYFVGMCGDGANDCGALKMAHVGISL
FT SEQEASVASPFT -> LVMNNFLGSSCVFAFSWVLLYVSIVIPRIPLVQLSVKLKIFQD
FT MAEKAVFSMAAGFNYTGHLKK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031264"
FT VAR_SEQ 879..1193
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031265"
FT CONFLICT 568
FT /note="L -> F (in Ref. 1; BAC26113/BAC26383)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="G -> A (in Ref. 1; BAC26113/BAC26383)"
FT /evidence="ECO:0000305"
FT CONFLICT 790
FT /note="R -> G (in Ref. 1; BAC26113/BAC26383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1193 AA; 132804 MW; 69C30D087163A24A CRC64;
MGDHLEKSQH ALLNEGDENE MEIFGYRTQG CRKALCLIGS IFSLGMLPLV FYWRPAWRVW
ANCVPCSLQE ADVVLLKTTD EFKIYSWKKV IWISLSALSS TSGLTPDHPL ITDEGYIINR
AIRKPDLKVR YIKVQKIRYV WNNLEGQFQK IGSLEDWLSS AKIHQKFGLG LTSEEQEIRR
LICGPNAIDV EITPIWKLLI KEVLNPFYIF QLFSVCLWFS EDYKEYALAI ILMSVISIAL
TVYDLRQQSV KLHHLVESHN SITVSVYERK AGAQDLESRL LVPGDLLILT GSRVQMPCDA
ILIDGSCVVD EGMLTGESIP VTKTPLSQTA SSVPWKMQSE ADPRRHVLFC GTEVIQAKAA
GSGAVRAVVL QTGFNTAKGD LVRSILYPKP MNFKLYRDAI RFLLCLVGTA TIGMVYTLCV
YVLSGEPPEE VVRKALDVIT IAVPPALPAA LTTGIIYAQR RLKKKGIFCI SPQRINVCGQ
LNLVCFDKTG TLTRGGLDPW GVVPCDQNGF QAVHSFASGK ALPQGPLCAA MASCHSLILL
DGTIQGDPLD LKMFEATKWE MTASGDDLHI KEMLAHTIVV KPTDMVGQVP AEGLAIVHQF
PFSSALQRMT VIVQEMGGGR LAFMKGAPER VASFCQPDTV PTSFISELQI YTTQGFRVIA
LAYKKLEMDC PTTALMREKV ESDLVFLGLL ILENRLKEET KPVLEELISA RIRTVMITGD
NLQTAITVAR KSGMVSEGQK VILVEANEAT GSSSASISWK LVEEKKPGPF GSQDTYINIR
EEVPENGRDR SYHFALSGKS FHVISQYFSS LLPKILINGT IFARMSPGQK SSLVEEFQKL
DYFVGMCGDG ANDCGALKMA HVGISLSEQE ASVASPFTSK TPNIECVPHL IKEGRAALVT
SFCMFKYMAL YSMIQYVGVL LLYWKTNSLS NYQFLFQDLA ITTLIGVTMN LNGANPKLVP
FRPAGRLISP PLLLSVVLNI LLSLAMHIVG FILVQKQPWY IMDYHSVCPV RNESASALAA
SPSVPEKTRS NSTFASFENT TIWFLGTINC IFVALVFSKG KPFRQPTYTN YIFVLVLILQ
MGVCLFILFA DIPEMHRRLD LLCTPVLWRV YILIMISSNF VVSLAVEKAI IENRALWIAV
KRCFGYQSKS QYRIWQRNLA NDSSWPPLNQ TSYSDMQGVS YSNPVFESNE EQL
