AT2C2_RAT
ID AT2C2_RAT Reviewed; 944 AA.
AC Q8R4C1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Calcium-transporting ATPase type 2C member 2;
DE Short=ATPase 2C2;
DE EC=7.2.2.10 {ECO:0000250|UniProtKB:O75185};
DE AltName: Full=Ca(2+)/Mn(2+)-ATPase 2C2 {ECO:0000250|UniProtKB:O75185};
DE AltName: Full=Secretory pathway Ca(2+)-transporting ATPase type 2;
DE Short=SPCA2 {ECO:0000303|Ref.1};
GN Name=Atp2c2; Synonyms=Spca2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Duodenum;
RA Kostina M.B., Pestov N.B., Korneenko T.V., Shakhparonov M.I.;
RT "Second isoform of mammalian secretory pathway Ca-ATPase, SPCA2.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:A7L9Z8, ECO:0000250|UniProtKB:O75185}.
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:O75185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000250|UniProtKB:O75185};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
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:0000250|UniProtKB:O75185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC Evidence={ECO:0000250|UniProtKB:O75185};
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:0000250|UniProtKB:O75185}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:O75185}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O75185}; Multi-pass
CC membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:A7L9Z8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; AF484685; AAL91565.1; -; mRNA.
DR RefSeq; NP_604457.1; NM_134462.1.
DR AlphaFoldDB; Q8R4C1; -.
DR SMR; Q8R4C1; -.
DR STRING; 10116.ENSRNOP00000066506; -.
DR PRIDE; Q8R4C1; -.
DR Ensembl; ENSRNOT00000074753; ENSRNOP00000066506; ENSRNOG00000049334.
DR GeneID; 171496; -.
DR KEGG; rno:171496; -.
DR CTD; 9914; -.
DR RGD; 620647; Atp2c2.
DR eggNOG; KOG0202; Eukaryota.
DR GeneTree; ENSGT00940000160275; -.
DR InParanoid; Q8R4C1; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; Q8R4C1; -.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q8R4C1; -.
DR Proteomes; UP000002494; Chromosome 19.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140613; F:P-type manganese transporter activity; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0061180; P:mammary gland epithelium development; ISO:RGD.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030334; ATP2C2.
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; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR42861:SF23; PTHR42861:SF23; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
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; TIGR01522; ATPase-IIA2_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Calcium transport; Cell membrane; Golgi apparatus;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..944
FT /note="Calcium-transporting ATPase type 2C member 2"
FT /id="PRO_0000356157"
FT TOPO_DOM 1..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..835
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..853
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 873..893
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..903
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..924
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..944
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 69..93
FT /note="Interaction with ORAI1"
FT /evidence="ECO:0000250|UniProtKB:O75185"
FT ACT_SITE 377
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 672
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 766
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75185"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75185"
SQ SEQUENCE 944 AA; 103020 MW; EA1CF6891B3218B5 CRC64;
MGRRFKFLQK LAFLGQNHRY KALERDEVDT LIDEQYELKA IEREKAVAAL PPREACKCSK
EELARTFHVD LDSGLSEFAV AQRRLVHGWN EFVTDNTEPV WKKYLDQFRN PLILLLLGSS
VVSVLTKEYE DAISIALAVL IVVTVGFIQE YRSEKSLEEL TKLVPPECNC LRDGKLRHML
ARDLVPGDVV SLSMGDRIPA DIRLTEVTDL LVDESSFTGE VEPCSKTDSP LAGGGDLSTL
SNVVFMGTLV QCGKGQGVVI GTGEQSQFGE VFKMMRAEET PKTPLQKSMD KLGKQLTVFS
FGIIGLLMLV GWVQGKPLLS MFTIGVSLAV AAIPEGLPIV VMVTLVLGVL RMAKKRVIVK
KLPIVETLGC CNVICSDKTG TLTANEMTAT QLVTSDGFHA EVSGIGYSGE GTVCLLPSKE
VIKEFSNVSV GKLVEAGCVA NNAVVRKNAV MGQPTEGALV VLAMKMNLGS IKDSYIRKKE
IPFSSEQKWM AVRCSLKNED EEDVYFMKGA FEEVIHHCST YNNGGIPLPL TPQQKSYCQQ
EEKKMGSLGL RVLALASGPE LGRLTFLGLV GIIDPPRAGV KEAVQALSES DVSVKMVTGD
ALETALAIGR TIGLCDEKLK AMSGEEVEGM EQDALAARVR QVSVFFRTSP KHKVKIIKAL
QESGAIVAMT GDGVNDSVAL KSADIGIAMG QTGTDVSKEA ADMILVDDDF SAIMSAVEEG
KGIFYNIKNF VRFQLSTSIA ALSLITLSTV CNLPNPLNAM QILWVNIIMD GPPAQSLGVE
PVDRDALKRP PRSVKDTILN RALILKILMS AAVILGGTLF IFWREIPENR TSTPRTTTMA
FTCFVFFDLF NALSCRSQTK LIFEIGFFRN RMFLYSILGS LLGQLAVIYA PPLQKVFQTE
NLSALDLLLL TGLASSVFIL SELLKLCEKF CSRAKADQML PEAV
