ID A0A8C4YD48_9SAUR Unreviewed; 1172 AA.
AC A0A8C4YD48;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2B2 {ECO:0000313|Ensembl:ENSGEVP00005023869.1};
OS Gopherus evgoodei (Goodes thornscrub tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=1825980 {ECO:0000313|Ensembl:ENSGEVP00005023869.1, ECO:0000313|Proteomes:UP000694390};
RN [1] {ECO:0000313|Ensembl:ENSGEVP00005023869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Murphy B., Edwards T., Rhie A., Koren S., Phillippy A., Fedrigo O.,
RA Haase B., Mountcastle J., Lewin H., Damas J., Howe K., Formenti G.,
RA Myers G., Durbin R., Jarvis E.D.;
RT "G10K-VGP Goodes thornscrub tortoise genome, primary haplotype.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGEVP00005023869.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGEVP00005023869.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. 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 AlphaFoldDB; A0A8C4YD48; -.
DR Ensembl; ENSGEVT00005025099.1; ENSGEVP00005023869.1; ENSGEVG00005015471.1.
DR GeneTree; ENSGT00940000161461; -.
DR OrthoDB; 116380at2759; -.
DR Proteomes; UP000694390; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:TreeGrafter.
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:1905059; F:P-type calcium transporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:TreeGrafter.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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; 2.70.150.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000032; 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; 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; 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 NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF377; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 2; 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 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.
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 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:UP000694390};
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 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 393..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 434..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 884..902
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 992..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 47..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 318..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1140
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 129471 MW; 23DF5E84AF291B5B CRC64;
MGDMTNSDFY TKNQRNEANR AGEFGCSLEE LRSLMELRGT EAVVKIKETY GDTEGLCRHL
KTSPTEGLPG TAADLEKRKL IFGKNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
LSFYQPPGEG NEGCATVSGG AEDEGEAEAG WIEGAAILLS VVCVVLVTAF NDWSKEKQFR
GLQSRIEQEQ KFTVVRGAQV IQIPVAEIVV GDIAQVKYGD LLPSDGIFIQ GNDLKIDESS
LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MLVTAVGVNS QTGIIFTLLG AGGEEEEKKD
KKGNSLIAHL TTDGAAGANA TDNANASLVN GMSRTPTKQQ DGAAAMEMQP LKSAEGGEGD
EKEKKKSSMH KKEKSVLQGK LTKLAVQIGK AGLVMSAITV IILVLYFAVD TFVINKKQWL
PECTPVYVQY FVKFFIIGVT VLVVAVPEGL PLAVTISLAY SVKKMMKDNN RMTVVAYTTK
ILPPEKEGGL PRQVGNKTEC GLLGFVLQLK QDYQPVRNLI PEEKLYKVYT FNSVRKSMST
VVKMPDGSFR MYSKGASEIV LKKCSRIINA TGEIRVFRPR DRDEMVKKVI EPMACDGLRT
ICIAYRDFSS NPEPDWDSEN DILTDLTCIC VVGIEDPVRP EVPEAIRKCQ RAGITVRMVT
GDNINTARAI AIKCGIIHPG EDFLCIEGKE FNRRIRNEKG EIEQERIDKI WPKLRVLARS
SPTDKHTLVK GIIDSTQVEQ RQVVAVTGDG TNDGPALKKA DVGFAMGIAG TDVAKEASDI
ILTDDNFSSI VKAVMWGRNV YDSISKFLQF QLTVNVVAVI VAFTGACITQ DSPLKAVQML
WVNLIMDTFA SLALATEPPT ESLLLRRPYG RNKPLISRTM MKNILGHAVY QLTLIFTLLF
VGEKMFKIDS GRNAPLHSPP SEHYTIIFNT FVMMQLFNEI NARKIHGERN VFDGIFRNPI
FCTIVLGTFA VQIVIVQFGG KPFSCSPLQL DQWMWCVFIG LGELVWGQVI ATIPTSRLKF
LKEAGRLTEK EEVPEEDLNE DVEEIDHAER ELRRGQILWF RGLNRIQTQI RVVKAFRSSL
YEGLEKPESR TSIHNFMTHP EFRIEDSQPH IPLIDDTDLE EDPALKQNSS PPSSLNKNNS
AIDSGINLTT DTSKSATSSS PGSPIHSLET SL
//
