ID A0A8C0GSY7_CHEAB Unreviewed; 1199 AA.
AC A0A8C0GSY7;
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=ATP2B4 {ECO:0000313|Ensembl:ENSCABP00000013813.1};
OS Chelonoidis abingdonii (Abingdon island giant tortoise) (Testudo
OS abingdonii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Chelonoidis.
OX NCBI_TaxID=106734 {ECO:0000313|Ensembl:ENSCABP00000013813.1, ECO:0000313|Proteomes:UP000694404};
RN [1] {ECO:0000313|Ensembl:ENSCABP00000013813.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCABP00000013813.1}
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; A0A8C0GSY7; -.
DR Ensembl; ENSCABT00000015145.1; ENSCABP00000013813.1; ENSCABG00000010326.1.
DR GeneTree; ENSGT00940000154527; -.
DR OMA; MINVHDI; -.
DR Proteomes; UP000694404; Unplaced.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:UniProtKB-ARBA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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:000008; 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; 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 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:UP000694404};
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 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 438..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 873..894
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 946..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1025..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1058..1079
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 51..125
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1199
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 131621 MW; 1261EFA2B6EC4BC8 CRC64;
FGNMTNNAAD HHPGNSVAEG SHEGDFGCSL ADLRTLMELR SGEAVARIND TYGGVQNICK
RLKTSPVEGL SGNPADLEKR RQVFGQNFIP PKKAKTFLQL VWEALQDVTL IILEIAAIIS
LGLSFYHPPG GGSELCGQAV AGAEDEGEAQ AGWIEGAAIL FSVIIVVLVT AFNDWSKEKQ
FRGLQSRIEQ EQKFTVIRKG QVIQIPVAEI VVGDIAQIKY GDLLPADGIL IQGNDLKIDE
SSLTGESDHV KKSVDKDLML LSGTHVMEGS GRMLVTAVGI NSQTGIIFTL LGAGEGEEEK
KVKKGFFLSL FPSSISVNGV KSFPPLRLPL THYVSFASWG VAKTQDGVAL EIQPLKSQEG
VENEDKEKKK VKVPKKEKSV LQGKLTRLAV QIGKAGLIMS AITVIILVLY FVIDTFAVQR
RPWLAECTPI YIQYFVKFFI IGVTVLVVAV PEGLPLAVTI SLAYSVKKMM KDNNLVRHLD
ACETMGNATA ICSDKTGTLT MNRMTVVQAY VGDTHYRQIP DPEAILPKVL DLIVNSVAIN
SAYTSKILPP EKEGGLPRQV GNKTECSLLG FVLDLKQDYQ AVRNEVPEEK LYKVYTFNSV
RKSMSTVLKN SDGSFRMYSK GASEIILRKC TKILDKNGDL RVFKVKDRDE MVKKVIEPMA
CQGLRTICLA FRDFPADAEP NWDNENEIMS DLACITVVGI EDPVRPEVPE AILKCQRAGI
TVRMVTGDNI NTARAIATKC GILLPGEDFL CLEGKEFNRL IRNEKGEVEQ EQLDKVWPKL
RVLARSSPTD KHTLVKGIID STVGEQRQVV AVTGDGTNDG PALKKADVGF AMGIAGTDVA
KEASDIILTD DNFTSIVKAV MWGRNVYDSI SKFLQFQLTV NVVAVIVAFT GACITQDSPL
KAVQMLWVNL IMDTFASLAL ATEPPSESLL LRRPYGRNKP LISRTMMKNI LGHAVYQLTI
IFTLLFAGER FFDIDSGRNA PLHSPPSEHY TIVFNTFVMM QLFNEINARK IHGERNVFDA
IFRNPIFCTV VLGTFAAQIL IVEFGGKPFS SSGLTLSQWL WCIFIGVGEL LWGQVRAGVP
TSRLKFLKEA GHGTTKEDIP EEDLPEDMDE IDHAEMELRR GQILWFRGLN RIQTQMDVVY
TFQTGASSLQ GALRRQPSIV SQHHDVKHVS SPTHVALSSV NSTPTTSAAA AASPTAGSE
//
