AT1A4_RAT
ID AT1A4_RAT Reviewed; 1028 AA.
AC Q64541;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-4;
DE Short=Na(+)/K(+) ATPase alpha-4 subunit;
DE EC=7.2.2.13 {ECO:0000269|PubMed:20179187};
DE AltName: Full=Sodium pump subunit alpha-4;
GN Name=Atp1a4; Synonyms=Atp1al2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=7809153; DOI=10.1073/pnas.91.26.12952;
RA Shamraj O.I., Lingrel J.B.;
RT "A putative fourth Na+,K(+)-ATPase alpha-subunit gene is expressed in
RT testis.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12952-12956(1994).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20179187; DOI=10.1530/rep-09-0495;
RA Jimenez T., Sanchez G., Wertheimer E., Blanco G.;
RT "Activity of the Na,K-ATPase alpha4 isoform is important for membrane
RT potential, intracellular Ca2+, and pH to maintain motility in rat
RT spermatozoa.";
RL Reproduction 139:835-845(2010).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients. Plays a role in sperm
CC motility. {ECO:0000269|PubMed:20179187}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13; Evidence={ECO:0000269|PubMed:20179187};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354;
CC Evidence={ECO:0000269|PubMed:20179187};
CC -!- ACTIVITY REGULATION: Specifically inhibited by an endogenous cardiac
CC glycoside, ouabain. {ECO:0000250}.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; U15176; AAB81285.1; -; mRNA.
DR RefSeq; NP_001257959.1; NM_001271030.1.
DR RefSeq; NP_074039.1; NM_022848.3.
DR AlphaFoldDB; Q64541; -.
DR SMR; Q64541; -.
DR BioGRID; 247817; 1.
DR STRING; 10116.ENSRNOP00000062079; -.
DR BindingDB; Q64541; -.
DR ChEMBL; CHEMBL2485; -.
DR iPTMnet; Q64541; -.
DR PhosphoSitePlus; Q64541; -.
DR jPOST; Q64541; -.
DR PaxDb; Q64541; -.
DR PRIDE; Q64541; -.
DR GeneID; 29132; -.
DR KEGG; rno:29132; -.
DR UCSC; RGD:61952; rat.
DR CTD; 480; -.
DR RGD; 61952; Atp1a4.
DR VEuPathDB; HostDB:ENSRNOG00000032378; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_3_1; -.
DR InParanoid; Q64541; -.
DR OMA; NSRVKFD; -.
DR OrthoDB; 388324at2759; -.
DR PhylomeDB; Q64541; -.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR SABIO-RK; Q64541; -.
DR PRO; PR:Q64541; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000032378; Expressed in testis and 6 other tissues.
DR Genevisible; Q64541; RN.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0097733; C:photoreceptor cell cilium; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0120200; C:rod photoreceptor outer segment; ISO:RGD.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISO:RGD.
DR GO; GO:0097225; C:sperm midpiece; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:MGI.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; IDA:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; TAS:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0030641; P:regulation of cellular pH; IDA:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 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; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Sodium; Sodium transport;
KW Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1028
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 4"
FT /id="PRO_0000046305"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..807
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..848
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 849..871
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..923
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 924..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 957..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..990
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 991..1011
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1012..1028
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..89
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 382
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 948
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1028 AA; 114005 MW; 858FE008735D06FA CRC64;
MEPGKETAAT SEQKPRPTLR ASNTNRQPKV KRRKKDLEEL KKEVVMDDHK LTLDELSAKY
SVDLTKGLSV TDAQEILTLN GPNVLTPPPT TPEWIKFCKQ LFGGFSLLLW TGSLLCFLAY
GIHVSYYQEN ANKDNLYLGI VLSAVVIITG CFSYYQEAKS SKIMESFKTM VPQQALVIRD
GEKMQINVRD VVLGDLVEVK GGDQVPADIR VIAAQGCKVD NSSLTGESEP QSRCPDCTHE
NPLETRNIIF FSTNCVEGTA RGVVIATGDH TVMGRIASLT SGLTMGKTPI ATEIEHFIHI
ITAVAVFLGV TFFFLSLILG YTWLDAVIFL IGIIVANVPE GLLATVTVCL TLTAKRMARK
NCLVKNLEAV ETLGSTSTIC SDKTGTLTQN RMTVAHLWFD KTVYEADTSE EQTTGKTFPK
SSDTWFYLAR IAGLCNRADF KPHQESLPIT KRTTTGDASE SALLKFIEQS YSPVSEMRQK
NPKVAEIPFN STNKYQMSIH LLEDNSEAHV LLMKGAPERI LDFCSSFLLN GQEYPMDEEM
KTDFQNAYIE LGGLGERVLG FCFLNLPSNF SKGFQFNTEE LNFPMENLCF AGLISMIDPP
RTAVPDAVSK CRSAGIKVIM VTGDHPITAK AIAKSVGIIS EANETAEDIA ARLNISISQV
SNKSIKAIVV HGSELKDMDS GQLDNILKSY KEIVFARTSP QQKLIIVEGC QRLGAIVAVT
GDGVNDSPAL KKADIGIAMG ITGSDVSKQA ADMILLDDNF ASIVTGVEEG RLIFDNLKKS
IAYTLTSNIP EITPFLLFIV LSIPLPLGTI TILCIDLGTD MVPAISLAYE TPESDIMKRL
PRNPKTDNLV NDRLIGMAYG QIGMIQALAG FFTYFVILAE NGFKPLDLLG IRLYWDDTNL
NDLEDTYGQQ WTYEQRKVVE FTCQTAFFIS IVIVQWADLI ICKTRRNSLF KQGMKNKVLI
FGLLEETILA ACLSYIPGMD VALRMYPLKI NWWFCALPYS VLIFIYDEVR KLIIRRRPGG
WLEKETYY
