ID D1FNM8_MOUSE Unreviewed; 1166 AA. AC D1FNM8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 2. DT 27-MAR-2024, entry version 98. DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146}; DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146}; GN Name=Atp2b4 {ECO:0000313|EMBL:ACC91879.2, ECO:0000313|MGI:MGI:88111}; 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 {ECO:0000313|EMBL:ACC91879.2}; RN [1] {ECO:0000313|EMBL:ACC91879.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6 {ECO:0000313|EMBL:ACC91879.2}; RC TISSUE=Brain {ECO:0000313|EMBL:ACC91879.2}; RA Afroze T., Yang G., Khoshbin A., Tanwir M., Tabish T., Momen A., Elias C., RA Backx P., Husain M.; RT "Regulated Alternative Splicing of a Novel and a Classical Exon-20 of RT PMCA4."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of CC calcium. {ECO:0000256|RuleBase:RU361146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; EC=7.2.2.10; CC Evidence={ECO:0000256|RuleBase:RU361146}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIB subfamily. {ECO:0000256|RuleBase:RU361146}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU361146}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU493094; ACC91879.2; -; mRNA. DR RefSeq; NP_001161421.1; NM_001167949.2. DR AlphaFoldDB; D1FNM8; -. DR PeptideAtlas; D1FNM8; -. DR DNASU; 381290; -. DR GeneID; 381290; -. DR AGR; MGI:88111; -. DR CTD; 493; -. DR MGI; MGI:88111; Atp2b4. DR OrthoDB; 847at2759; -. DR BioGRID-ORCS; 381290; 4 hits in 77 CRISPR screens. DR ChiTaRS; Atp2b4; mouse. DR GO; GO:0005886; C:plasma membrane; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC. DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 3. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR022141; ATP_Ca_trans_C. 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; IPR006408; P-type_ATPase_IIB. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 3. DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1. DR PANTHER; PTHR24093:SF435; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 4; 1. DR Pfam; PF12424; ATP_Ca_trans_C; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 2. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR Genevisible; D1FNM8; MM. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146}; KW Calcium transport {ECO:0000256|ARBA:ARBA00022568, KW ECO:0000256|RuleBase:RU361146}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU361146}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU361146}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}. FT TRANSMEM 369..390 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 410..436 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 844..865 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 917..938 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 958..975 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 996..1017 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 1029..1050 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT DOMAIN 45..121 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" FT REGION 294..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 294..311 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1166 AA; 128548 MW; 1A9DA75973DC88D1 CRC64; MTNPPGQSVS ANTVAESHEG EFGCTLMDLR KLMELRGADA VAQISAHYGG VQEICTRLKT SPIEGLSGNP ADLEKRRLVF GKNVIPPKRP KTFLELVWEA LQDVTLIILE IAAVISLVLS FYRPPGGDNE ICGHIASSPE EEEEGETGWI EGAAILASVI IVVLVTAFND WSKEKQFRGL QSRIELEQKF SIIRNGQLIQ LPVAEIVVGD IAQIKYGDLL PADGILIQGN DLKIDESSLT GESDHVKKTL DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIIFTLLGAS EEEDDDDKKK KGKKQGAPEN RNKAKTQDGV ALEIQPLNSQ EGLDSEDKEK KIARIPKKEK SVLQGKLTRL AVQIGKAGLI MSVLTVVILI LYFVVDNFVI QRREWLPECT PVYIQYFVKF FIIGVTVLVV AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT LTMNRMTVVQ AYIGGTHYRQ IPQPDVFPPK VLELIVNGIS INCAYTSKIQ PPEKEGGLPR QVGNKTECGL LGFVTDLKQD YQAVRNEVPE EKLFKVYTFN SVRKSMSTVI RKPEGGFRMF SKGASEIMLR RCDRILNKEG EIKSFRSKDR DNMVRNVIEP MASEGLRTIC LAYRDFDGTE PSWDIEGEIL TSLICIAVVG IEDPVRPEVP DAIAKCKRAG ITVRMVTGDN VNTARAIATK CGILTPKDDF LCLEGKEFNS LIRNEKGEVE QEKLDKIWPK LRVLARSSPT DKHTLVKGII DSTAGEQRQV VAVTGDGTND GPALKKADVG FAMGIAGTDV AKEASDIILT DDNFTSIVKA VMWGRNVYDS ISKFLQFQLT VNVVAVIVAF TGACITQDSP LKAVQMLWVN LIMDTFASLA LATEPPTESL LRRRPYGRNK PLISRTMMKN ILGHAVYQLL IVFLLVFAGD TLFDIDSGRK APLNSPPSQH YTIVFNTFVL MQLFNEINAR KIHGEKNVFA GVYRNIIFCT VVLGTFFCQI MIVELGGKPF SCTSLTMEQW MWCLFIGIGE LLWGQVISAI PTKSLKFLKE AGHGSDKEDI SRDTEGMDEI DLAEMELRRG QILWVRGLNR IQTQIDVINK FQTEAPLKRV RENMTQHLDV KLVPSSYSAA VASLRTCPSI SSAISSAVTS PPVGSE //