ID A0A2K5CGS9_AOTNA Unreviewed; 992 AA.
AC A0A2K5CGS9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=Calcium-transporting ATPase type 2C member 2 {ECO:0000256|ARBA:ARBA00070963};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE AltName: Full=Ca(2+)/Mn(2+)-ATPase 2C2 {ECO:0000256|ARBA:ARBA00083166};
DE AltName: Full=Secretory pathway Ca(2+)-transporting ATPase type 2 {ECO:0000256|ARBA:ARBA00077949};
GN Name=ATP2C2 {ECO:0000313|Ensembl:ENSANAP00000007831.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000007831.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000007831.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+)
CC and Mn(2+) ions, both essential cofactors for processing and
CC trafficking of newly synthesized proteins in the secretory pathway.
CC Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the
CC cytoplasmic side of the membrane and delivers them to the lumenal side.
CC The transfer of ions across the membrane is coupled to ATP hydrolysis
CC and is associated with a transient phosphorylation that shifts the pump
CC conformation from inward-facing to outward-facing state. Induces Ca(2+)
CC influx independently of its ATP-driven pump function. At the
CC basolateral membrane of mammary epithelial cells, interacts with Ca(2+)
CC channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+)
CC content of endoplasmic reticulum or Golgi stores. May facilitate
CC transepithelial transport of large quantities of Ca(2+) for milk
CC secretion via activation of Ca(2+) influx channels at the plasma
CC membrane and active Ca(2+) transport at the Golgi apparatus.
CC {ECO:0000256|ARBA:ARBA00054616}.
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 -!- SUBUNIT: Interacts (via N-terminus) with ORAI1 (via N- and C-termini);
CC this interaction regulates Ca(2+) influx at the plasma membrane.
CC {ECO:0000256|ARBA:ARBA00062966}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004554}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004166}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR AlphaFoldDB; A0A2K5CGS9; -.
DR STRING; 37293.ENSANAP00000007831; -.
DR Ensembl; ENSANAT00000025610.1; ENSANAP00000007831.1; ENSANAG00000021932.1.
DR Ensembl; ENSANAT00000025646.1; ENSANAP00000007867.1; ENSANAG00000021932.1.
DR GeneTree; ENSGT00940000160275; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0140613; F:P-type manganese transporter activity; IEA:Ensembl.
DR GO; GO:0061180; P:mammary gland epithelium development; IEA:Ensembl.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR CDD; cd02085; P-type_ATPase_SPCA; 1.
DR FunFam; 1.20.1110.10:FF:000051; Calcium-transporting ATPase; 1.
DR FunFam; 2.70.150.10:FF:000008; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000006; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
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; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..130
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 992 AA; 108195 MW; E6E89830FB3A2A85 CRC64;
MVEGRVSKFL KKLGFSGGDR EYQALEKDEE EALIDEQIEL KAIEKEKKVT ALPPKEACKC
HKEDLANVFC VDLHTGLSEF SVTQRRLVHG WNEFVAETTE PVWKKYLDQF KNPLILLLLG
SALVSVLTRE YEDAVSIATA VLIVVTVAFI QEYRSERSLE ELTKLVPPEC NCLREGKLQH
LLARELVPGD VVSLSIGDRI PADIRLTEVT DLLVDESSFT GEAEPCSKTD SPLAGGGDLT
TLSNIVFMGT LVQYGRGQGV VIGTGESSQF GEVFKMMQSE ETPKTPLQKS MDRLGKQLTL
FSFGIIGLIM LIGWLQGKQL LSMFTIGVSL AVAAIPEGLP IVVMVTLVLG VLRMAKKRVI
VKKLPIVETL GEGLWPVEFR HLELNGSLAV RAVQPGGFTN LRVAISLFYK LMLIVPGCCS
VLCSDKTGTL TANEMTVTQL VTSDGLHAEV SGVGYDGQGT VCLLPSKEVI KEFSNVSVGK
LVEAGCVANN AVIRKNAVIG QPTEGALMAL AMKMDLNDIK NSYVRKKEIA FSSEQKWMAV
QCSPKTEDQE DIYFMKGALE EVIRYCTTYN NGGIPLPLTP QQRSFCLREE KRMGSLGLRV
LALASGPELG RLTFLGLVGI IDPPRAGVKE AVQVLSESGV SVKMITGDAL ETALAIGRNI
GLCIGKLQAM SGEEVDSMEK GELADRVGKV SVFFRTSPKH KLKIIKALQE SGAIVAMTGD
GVNDAVALKS ADIGIAMGQT GTDVSKEAAN MILVDDDFSA IMNAVEEGKG IFYNIKNFVR
FQLSTSISAL SLITLSTVFN LPSPLNAMQI LWINIIMDGP PAQSLGVEPV DKDALRQPPR
SVGDTILSRA LILKILMSAA VIISGTLFIF WKEMPEDRAS TPRTTTMTFT CFVFFDLFNA
LTCRSQTKLI FEIGFLRNRM FLYSVLGSIL GQLVVIYIPP LQRVFQTENL GALDLLFLIG
LASSVFILSE LLKLCERYCC SPGRVQTPHE AV
//
