AT2B1_PIG
ID AT2B1_PIG Reviewed; 1220 AA.
AC P23220;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 1 {ECO:0000250|UniProtKB:P20020};
DE EC=7.2.2.10 {ECO:0000250|UniProtKB:G5E829};
DE AltName: Full=Plasma membrane calcium ATPase isoform 1 {ECO:0000250|UniProtKB:P20020};
DE Short=PMCA1 {ECO:0000250|UniProtKB:P20020};
DE AltName: Full=Plasma membrane calcium pump isoform 1 {ECO:0000303|PubMed:2147100};
GN Name=ATP2B1 {ECO:0000250|UniProtKB:P20020};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach smooth muscle;
RX PubMed=2147100; DOI=10.1042/bj2710655;
RA de Jaegere S., Wuytack F., Eggermont J.A., Verboomen H., Casteels R.;
RT "Molecular cloning and sequencing of the plasma-membrane Ca2+ pump of pig
RT smooth muscle.";
RL Biochem. J. 271:655-660(1990).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium from the cytoplasm to the extracellular space thereby
CC maintaining intracellular calcium homeostasis. Plays a role in blood
CC pressure regulation through regulation of intracellular calcium
CC concentration and nitric oxide production leading to regulation of
CC vascular smooth muscle cells vasoconstriction. Positively regulates
CC bone mineralization through absorption of calcium from the intestine.
CC Plays dual roles in osteoclast differentiation and survival by
CC regulating RANKL-induced calcium oscillations in preosteoclasts and
CC mediating calcium extrusion in mature osteoclasts (By similarity).
CC Regulates insulin sensitivity through calcium/calmodulin signaling
CC pathway by regulating AKT1 activation and NOS3 activation in
CC endothelial cells (By similarity). May play a role in synaptic
CC transmission by modulating calcium and proton dynamics at the synaptic
CC vesicles. {ECO:0000250|UniProtKB:G5E829, ECO:0000250|UniProtKB:P20020}.
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:G5E829};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000250|UniProtKB:G5E829};
CC -!- SUBUNIT: Monomer. Dimer. Oligomer. Calmodulin binding. Interacts with
CC PDZD11. Interacts with SLC35G1 and STIM1. Interacts with YWHAE;
CC interacts with the monomeric and dimeric forms of the YWHAE but prefer
CC the monomer form; this interaction inhibits calcium-transporting ATPase
CC activity (By similarity). Interacts with NPTN; this interaction
CC stabilizes ATP2B1 and increases ATPase activity; this interaction
CC controls T cell calcium homeostasis following T cell activation.
CC Interacts with EPB41; regulates small intestinal calcium absorption
CC through regulation of membrane expression of ATP2B1 (By similarity).
CC {ECO:0000250|UniProtKB:G5E829, ECO:0000250|UniProtKB:P20020}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20020};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:G5E829}. Synapse {ECO:0000250|UniProtKB:G5E829}.
CC Presynaptic cell membrane {ECO:0000250|UniProtKB:G5E829}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:G5E829}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Colocalizes with SV2A in
CC photoreceptor synaptic terminals. Colocalizes with NPTN to the
CC immunological synapse. Colocalizes with EPB41 to the basolateral
CC membrane in enterocyte. Preferentially sorted to recycling synaptic
CC vesicles. {ECO:0000250|UniProtKB:G5E829}.
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; X53456; CAA37536.1; -; mRNA.
DR PIR; S13057; S13057.
DR RefSeq; NP_999517.1; NM_214352.3.
DR AlphaFoldDB; P23220; -.
DR SMR; P23220; -.
DR STRING; 9823.ENSSSCP00000000984; -.
DR PaxDb; P23220; -.
DR PeptideAtlas; P23220; -.
DR PRIDE; P23220; -.
DR GeneID; 397636; -.
DR KEGG; ssc:397636; -.
DR CTD; 490; -.
DR eggNOG; KOG0204; Eukaryota.
DR InParanoid; P23220; -.
DR OrthoDB; 115892at2759; -.
DR BRENDA; 7.2.2.10; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
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:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030320; ATP2B1.
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 PANTHER; PTHR24093:SF245; PTHR24093:SF245; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
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; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT CHAIN 2..1220
FT /note="Plasma membrane calcium-transporting ATPase 1"
FT /id="PRO_0000046210"
FT TOPO_DOM 2..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 127..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 176..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 387..418
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..882
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..927
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 949..971
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 972..991
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 992..1005
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1006..1027
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 1028..1039
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 1061..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 297..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1117
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250"
FT REGION 1118..1220
FT /note="Required for basolateral membrane targeting"
FT /evidence="ECO:0000250|UniProtKB:P11505"
FT REGION 1118..1127
FT /note="Calmodulin-binding subdomain B"
FT /evidence="ECO:0000250"
FT REGION 1160..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 797
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 801
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E829"
FT MOD_RES 1116
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11505"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 1165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
SQ SEQUENCE 1220 AA; 134710 MW; 3372FAF67F82401A CRC64;
MGDMANNSVA YGGVKNSLKE ANHDGDFGIT LADVRALMEL RSTDALRKIQ ESYGDVYGIC
TRLKTSPVEG LSGNPADIER REAVFGKNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAIV
SLGLSFYQPP EGDNALCGEV SVGEEEGEGE TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ
FRGLQSRIEQ EQKFTVIRGG QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE
SSLTGESDHV KKSLDKDPLL LSGTHVMEGS GRMVVTAVGI NSQTGIIFTL LGAGGEEEEK
KDEKKKEKKN KKQDGAIENR NKAKAQDGAA MEMQPLKSEE GGDGDEKDKK KANLPKKEKS
VLQGKLTKLA VQIGKAGLLM SAITVIILVL YFVIDTFWVQ KRPWLAECTP IYIQYFVKFF
IIGVTVLVVA VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL
TMNRMTVVQA YINEKHYKKI PEPEAIPPNI LSYLVTGISV NCAYTSKILP PEKEGGLPRH
VGNKTECALL GLLLDLKRDY QDVRNEIPEE ALYKVYTFNS VRKSMSTVLK NSDGSYRIFS
KGASEIILKK CFKILSANGE AKVFRPRDRD DIVKTVIEPM ASEGLRTICL AFRDFPAGEP
EPEWDNENDI VTGLTCIAVV GIEDPVRPEV PDAIKKCQRA GITVRMVTGD NINTARAIAT
KCGILHPGED FLCLEGKDFN RRIRNEKGEI EQERIDKIWP KLRVLARSSP TDKHTLVKGI
IDSTVSDQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK
AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTLASL
ALATEPPTES LLLRKPYGRN KPLISRTMMK NILGHAFYQL VVVFTLLFAG EKFFDIDSGR
NAPLHAPPSE HYTIVFNTFV LMQLFNEINA RKIHGERNVF EGIFNNAIFC TIVLGTFVVQ
IIIVQFGGKP FSCSELSIEQ WLWSIFLGMG TLLWGQLIST IPTSRLKFLK EAGHGTQKEE
IPEEELAEDV EEIDHAEREL RRGQILWFRG LNRIQTQIRV VNAFRSSLYE GLEKPESRSS
IHNFMTHPEF RIEDSEPHIP LIDDTDAEDD APTKRNCSPP PSPNKNNNAV DSGIYLTIEM
NKSATSSSPG SPLHSLETSL
