AT135_MOUSE
ID AT135_MOUSE Reviewed; 1216 AA.
AC Q3TYU2; Q14BM0; Q8BUP1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable cation-transporting ATPase 13A5;
DE EC=7.2.2.-;
DE AltName: Full=P5-ATPase isoform 5;
GN Name=Atp13a5;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Inner ear;
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 MRNA] (ISOFORM 2).
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 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).
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TYU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TYU2-2; Sequence=VSP_033924;
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain and stomach.
CC {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; AK083121; BAC38770.1; -; mRNA.
DR EMBL; AK158355; BAE34470.1; -; mRNA.
DR EMBL; BC115739; AAI15740.1; -; mRNA.
DR CCDS; CCDS28095.1; -. [Q3TYU2-1]
DR RefSeq; NP_001271304.1; NM_001284375.1.
DR RefSeq; NP_783581.2; NM_175650.4. [Q3TYU2-1]
DR AlphaFoldDB; Q3TYU2; -.
DR SMR; Q3TYU2; -.
DR STRING; 10090.ENSMUSP00000075204; -.
DR GlyGen; Q3TYU2; 2 sites.
DR iPTMnet; Q3TYU2; -.
DR PhosphoSitePlus; Q3TYU2; -.
DR PaxDb; Q3TYU2; -.
DR PRIDE; Q3TYU2; -.
DR ProteomicsDB; 281866; -. [Q3TYU2-1]
DR ProteomicsDB; 281867; -. [Q3TYU2-2]
DR Antibodypedia; 65947; 10 antibodies from 6 providers.
DR DNASU; 268878; -.
DR Ensembl; ENSMUST00000075806; ENSMUSP00000075204; ENSMUSG00000048939. [Q3TYU2-1]
DR GeneID; 268878; -.
DR KEGG; mmu:268878; -.
DR UCSC; uc007yvy.2; mouse. [Q3TYU2-1]
DR CTD; 344905; -.
DR MGI; MGI:2444068; Atp13a5.
DR VEuPathDB; HostDB:ENSMUSG00000048939; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000160327; -.
DR HOGENOM; CLU_001828_0_1_1; -.
DR InParanoid; Q3TYU2; -.
DR OMA; KMEDCNV; -.
DR OrthoDB; 172453at2759; -.
DR PhylomeDB; Q3TYU2; -.
DR TreeFam; TF300331; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 268878; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q3TYU2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3TYU2; protein.
DR Bgee; ENSMUSG00000048939; Expressed in vestibular membrane of cochlear duct and 87 other tissues.
DR ExpressionAtlas; Q3TYU2; baseline and differential.
DR Genevisible; Q3TYU2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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: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: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; 1.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Glycoprotein; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1216
FT /note="Probable cation-transporting ATPase 13A5"
FT /id="PRO_0000337123"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 933..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1113..1133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 486
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 852
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033924"
FT CONFLICT 1072
FT /note="A -> T (in Ref. 2; AAI15740)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="L -> V (in Ref. 1; BAE34470)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130
FT /note="E -> V (in Ref. 1; BAC38770)"
FT /evidence="ECO:0000305"
FT CONFLICT 1214
FT /note="T -> A (in Ref. 1; BAE34470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 136760 MW; 184884C18414B47A CRC64;
MEKSKKDGHQ AVLNEGEENE LEVFGYHTQN LRRALCLVTA ILTLGAVQLM FYWRPEWWVW
TSCIPCPLQE ADTILLRTTD EFRRYMRKKV FCLHLSTLKF PISKNPEEPL VADHHSVINQ
AVMKPELKLR CIQVQKIRYV WDFLKKRFQK VGLLEDSNSC FDIHHTFGLG LTNEEQEVRR
LVCGPNSIEV EIQPIWKLLV KQVLNPFYVF QAFTLTLWLS QGYIEYSVAI IILTVISIVL
SVYDLRQQSV KLHKLVEEHN KVQVTITVRD KGLQELESRL LVPGDILILP GKISLPCDAI
LIDGSCVVNE GMLTGESIPV TKTPLPQTEN TMPWKSHSLE DYRKHVLFCG TEVIQVKPSA
QGLVRAVVLQ TGYNTAKGDL VRSILYPRPL NFKLYNDAFK FMVFLACVGV VGFFYALGVY
MYHEVPPRET ATMALILLSA TVPPVLPAAL TIGNVYAQKR LKKEKIFCIS PQRINMCGQI
NLVCFDKTGT LTEDGLDLWG TVPTAGNCFQ AVHSFASGEA VPWGPLCAAM TSCHSLILLD
GTIQGDPLDL KMFEGTGWNM EDSQVASCKF GMADSSTVIK PGPKASQSPV DSITILRQFP
FSSGLQRMSV IAQLAGDLHL HVYMKGAPEM VARFCRSETV PKNFSQELRN YTVQGFRVIA
LAHKTLKMER LSDMDHLARE KVESELAFLG LLIMENRLKK ETRPVLKELS EARIRTVMVT
GDNLQTAITV AKNSEMIPVG SQVVIVEANE PGDLVPASVT WQLVGTQEPG SGKKDTYIDI
GNSSVPAGKG YHFAMSGKSY QVLFHHFYSM LPQILVNGTI FARMSPGQKS SLVEEFQKLN
YYVGMCGDGA NDCGALKMAH AGISLSEQEA SVASPFTSKT ANIECVPHLI REGRAALVSS
FGVFKYLTMY GIIQFIGTSL LYWQLQLFGN YQYLLQDVAI TLMVSLTMSI NHAYPKLAPY
RPAGQLLSPQ LLLSVFMNSC FTCIVQVCTF LTVKQQPWYC EVYKYSECFL VNQSNLSANV
SLDRNWTGNA TLVPASVLSF EGTTLWPIVT FNCISAAFIF SKGKPFRKPI YANYLFSLLL
ASAAGLTIFI LFCDFQDLYR KMEFIPTPTS WRVSILIAAF VQFCVAFFVE DAVLQNRELW
LFIKKEFGFY SKSQYRILQR KLAEDSTWPP VNRTDYAVNG KNGFYVNRAY ESPEEVPKGK
LKLEEQASEQ HFWTRL
