ID A0A2I3GBG8_NOMLE Unreviewed; 457 AA.
AC A0A2I3GBG8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2C1 {ECO:0000313|Ensembl:ENSNLEP00000028669.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000028669.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000028669.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000028669.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSNLEP00000028669.1}
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|ARBA:ARBA00047282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000256|ARBA:ARBA00047282};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Mn(2+)(in) + ATP + H2O = Mn(2+)(out) + ADP + phosphate + H(+);
CC Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00047330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC Evidence={ECO:0000256|ARBA:ARBA00047330};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004127}. 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 IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
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 EMBL; ADFV01027832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01027833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01027834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3GBG8; -.
DR Ensembl; ENSNLET00000041887.1; ENSNLEP00000028669.1; ENSNLEG00000002211.3.
DR GeneTree; ENSGT00940000156421; -.
DR Proteomes; UP000001073; Chromosome 8.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0140613; F:P-type manganese transporter activity; IEA:RHEA.
DR FunFam; 3.40.50.1000:FF:000017; Calcium-transporting ATPase; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
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 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 345..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 382..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 411..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 264..435
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
SQ SEQUENCE 457 AA; 50147 MW; 782AEB4A58C8BBAD CRC64;
MINGQGAYID RPEICFMKGA YEQVIKYCTT YQSKGQTLPL TQQQRDVYQQ EKARMGSAGL
RVLALASGPE LGQLTFLGLV GIIDPPRTGV KEAVTTLIAS GVSIKMITGD SQETAVAIAS
RLGLYSKTSQ SVSGEEIDAM DVQQLSQIVP KVAVFYRASP RHKMKIIKSL QKNGSVVAMT
GDGVNDAVAL KAADIGVAMG QTGTDVCKEA ADMILVDDDF QTIMSAIEEG KGIYNNIKNF
VRFQLSTSIA ALTLISLATL MNFPNPLNAM QILWINIIMD GPPAQSLGVE PVDKDVIRKP
PRNWKDSILT KNLILKILVS SIIIVCGTLF VFWRELRDNV ITPRDTTMTF TCFVFFDMFN
ALSSRSQTKS VFEIGLCSNK MFCYAVLGSI MGQLLVIYFP PLQKVFQTES LSILDLLFLL
GLTSSVCIVA EIIKKVERSR EKIQKHVSST SSSFLEV
//
