ID AT2B4_BOVIN Reviewed; 1207 AA.
AC D3K0R6; D3K0R5; Q28059;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 4 {ECO:0000305};
DE Short=PMCA4 {ECO:0000303|PubMed:21187283};
DE EC=7.2.2.10 {ECO:0000250|UniProtKB:P23634};
GN Name=ATP2B4 {ECO:0000250|UniProtKB:P23634};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-1175 (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=21187283; DOI=10.1074/jbc.m110.142836;
RA Brandenburger T., Strehler E.E., Filoteo A.G., Caride A.J., Aumuller G.,
RA Post H., Schwarz A., Wilhelm B.;
RT "Switch of PMCA4 splice variants in bovine epididymis results in altered
RT isoform expression during functional sperm maturation.";
RL J. Biol. Chem. 286:7938-7946(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1137-1207 (ISOFORM 1).
RX PubMed=2966397; DOI=10.1073/pnas.85.9.2914;
RA Brandt P., Zurini M., Neve R.L., Rhoads R.E., Vanaman T.C.;
RT "A C-terminal, calmodulin-like regulatory domain from the plasma membrane
RT Ca2+-pumping ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2914-2918(1988).
CC -!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme
CC that catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium out of the cell (By similarity). By regulating sperm cells
CC calcium homeostasis, may play a role in sperm motility (By similarity).
CC {ECO:0000250|UniProtKB:P23634, ECO:0000250|UniProtKB:Q6Q477}.
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:0000250|UniProtKB:P23634};
CC -!- ACTIVITY REGULATION: Activated by calcium/calmodulin.
CC {ECO:0000250|UniProtKB:P23634}.
CC -!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
CC Interacts with calmodulin. {ECO:0000250|UniProtKB:P23634}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21187283};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium,
CC flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PMCA4b;
CC IsoId=D3K0R6-1; Sequence=Displayed;
CC Name=2; Synonyms=PMCA4a;
CC IsoId=D3K0R6-2; Sequence=VSP_058016, VSP_058017;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in brain, heart, liver,
CC testis and epididymis. Isoform 2 is detected in brain (at protein
CC level), heart, seminal vesicle and epididymis. There is a shift in
CC expression from isoform 1 to isoform 2 along the length of the
CC epididymis from caput to cauda (at protein level).
CC {ECO:0000269|PubMed:21187283}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
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DR EMBL; GU353069; ADB79572.1; -; mRNA.
DR EMBL; GU353070; ADB79573.1; -; mRNA.
DR EMBL; DAAA02041902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02041903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02041904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02041905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02041906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J03649; AAA30393.1; -; mRNA.
DR PIR; A31332; A31332.
DR RefSeq; NP_001166065.1; NM_001172594.1.
DR AlphaFoldDB; D3K0R6; -.
DR SMR; D3K0R6; -.
DR STRING; 9913.ENSBTAP00000057551; -.
DR PaxDb; 9913-ENSBTAP00000018688; -.
DR Ensembl; ENSBTAT00000071315.1; ENSBTAP00000057551.1; ENSBTAG00000014059.6. [D3K0R6-1]
DR GeneID; 282146; -.
DR KEGG; bta:282146; -.
DR CTD; 493; -.
DR VEuPathDB; HostDB:ENSBTAG00000014059; -.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000154527; -.
DR InParanoid; D3K0R6; -.
DR Reactome; R-BTA-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-BTA-5578775; Ion homeostasis.
DR Reactome; R-BTA-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000014059; Expressed in cardiac ventricle and 110 other cell types or tissues.
DR ExpressionAtlas; D3K0R6; baseline and differential.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IBA:GO_Central.
DR GO; GO:1905145; P:cellular response to acetylcholine; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISS:UniProtKB.
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 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Calmodulin-binding; Cell membrane; Cell projection; Cilium; Flagellum;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1207
FT /note="Plasma membrane calcium-transporting ATPase 4"
FT /id="PRO_0000435123"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..147
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..408
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..871
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 893..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..957
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 958..977
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 978..994
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1028
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1029..1049
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1050..1207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 294..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1103
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250|UniProtKB:P20020,
FT ECO:0000250|UniProtKB:P23634"
FT REGION 1104..1113
FT /note="Calmodulin-binding subdomain B"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT REGION 1159..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23634"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23634"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64542"
FT MOD_RES 1102
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT VAR_SEQ 300..311
FT /note="Missing (in isoform 2)"
FT /id="VSP_058016"
FT VAR_SEQ 1105..1207
FT /note="KVVKAFHSSLHESIQKPKNQNSIHNFMTHPEFTIDEEGPRTPLLDEQEEEIF
FT EKVSKPGTKTSSLDGEVTPQTNKNNNTVDCCQVQIVASHSDSPLHSLETSV -> DVIN
FT TFQTGASFKGVLKRQTMGQHLDVKHVPSSSYVTVAPVKSPPTTSVAAAVSSPTLGNQSG
FT QSV (in isoform 2)"
FT /id="VSP_058017"
FT CONFLICT 180
FT /note="L -> P (in Ref. 1; ADB79572)"
FT CONFLICT 972
FT /note="L -> F (in Ref. 1; ADB79573)"
SQ SEQUENCE 1207 AA; 133792 MW; 8811E298B456F5A2 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 QTQIKVVKAF HSSLHESIQK PKNQNSIHNF MTHPEFTIDE
EGPRTPLLDE QEEEIFEKVS KPGTKTSSLD GEVTPQTNKN NNTVDCCQVQ IVASHSDSPL
HSLETSV
//
