ID A0A4W2FRY0_BOBOX Unreviewed; 1171 AA.
AC A0A4W2FRY0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 33.
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|Ensembl:ENSBIXP00005008511.1};
OS Bos indicus x Bos taurus (Hybrid cattle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00005008511.1, ECO:0000313|Proteomes:UP000429181};
RN [1] {ECO:0000313|Proteomes:UP000314981, ECO:0000313|Proteomes:UP000429181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT "Haplotype-resolved cattle genomes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBIXP00005008511.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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|ARBA:ARBA00048694,
CC ECO:0000256|RuleBase:RU361146};
CC -!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
CC Interacts with calmodulin. {ECO:0000256|ARBA:ARBA00062373}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000256|ARBA:ARBA00060429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00060429}. Membrane
CC {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {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|ARBA:ARBA00006124,
CC ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR RefSeq; XP_027419981.1; XM_027564180.1.
DR AlphaFoldDB; A0A4W2FRY0; -.
DR Ensembl; ENSBIXT00000022523.1; ENSBIXP00000034574.1; ENSBIXG00000017601.1.
DR Ensembl; ENSBIXT00005044213.1; ENSBIXP00005008511.1; ENSBIXG00005000259.1.
DR GeneID; 113906280; -.
DR CTD; 493; -.
DR GeneTree; ENSGT00940000154527; -.
DR Proteomes; UP000314981; Chromosome 16.
DR Proteomes; UP000429181; Chromosome 16.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0036126; C:sperm flagellum; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0030165; F:PDZ domain binding; IEA:TreeGrafter.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:UniProtKB-ARBA.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:TreeGrafter.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR FunFam; 1.20.1110.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000002; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000011; Calcium-transporting ATPase; 1.
DR FunFam; 2.70.150.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000022; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000007; Calcium-transporting ATPase; 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; 2.
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; IPR059000; ATPase_P-type_domA.
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; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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.
PE 3: Inferred from homology;
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 Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Flagellum {ECO:0000256|ARBA:ARBA00022846};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314981};
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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 368..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 409..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 843..864
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 920..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 957..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 995..1016
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1028..1049
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..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 129189 MW; 42788B22CDF259F5 CRC64;
MTNPTEHTLP SNSILESREG EFGCTVMDLR KLMELRSSDA IDQINVHYGG VMNLCSRLKT
NPVEGLSGNP ADLEKRKQVF GQNLIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
FYRPPGGENE QCGLAVTSPE DEGEAEAGWI EGAAILFSVI IVVLVTAFND WSKEKQFRGL
QNRIEKEQKF SVIRNGHIIQ LPVAEIVVGD IAQIKYGDLL PADGILIQGN DLKIDESSLT
GESDHVKKSL ERDPMLLSGT HVMEGSGRMV VTAVGINSQT GIIFTLLGAS EGEEEEKKKK
GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GIDSEEKEKK AAKLPKKEKS VLQGKLTRLA
VQIGKAGLIM SAITVLILIL YFVIDNFVIQ RRPWLAECTP IYVQYFVKFF IIGVTVLVVA
VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMSVVQA
YIGDTRYHQI PSPDDLVPKV LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGNKTECALL
GFVSDLKQDY HAVRSEVPEE KLYKVYTFNS VRKSMSTVIE KPGGGYRMYS KGASEIILRK
CNRILDKKGE AVPFKNKDRD EMVRTVIEPM ACEGLRTLCI AYRDFNDGEP PWDNESEILT
ELTCIAVVGI EDPVRPEVPE AIAKCKRAGI TVRMVTGDNI NTARAIATKC GIVTPGDDFL
CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL RVLARSSPTD KHTLVKGIID STVGDQRQVV
AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
SKFLQFQLTV NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTDSLL
KRRPYGRNKP LISRTMMKNI LGHAVYQLTV IFFLVFAGEK FFDIDSGRRA PLHSPPSQHY
TIIFNTFVLM QLFNEINSRK IHGERNVFSG IFRNLIFCSV VLGTFISQII IVEFGGKPFS
CTKLTLSQWF WCLFIGIGEL LWGQVISTIP TQSLKFLKEA GHGTTKEEIT KDAEGLDEID
HAEMELRRGQ ILWFRGLNRI QTQIDVINTF QTGASFKGVL KRQTMGQHLD VKHVPSSSYV
TVAPVKSPPT TSVAAAVSSP TLGNQSGQSV P
//