AT2C1_RAT
ID AT2C1_RAT Reviewed; 919 AA.
AC Q64566; Q64567;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calcium-transporting ATPase type 2C member 1;
DE Short=ATPase 2C1;
DE EC=7.2.2.10 {ECO:0000250|UniProtKB:P98194};
DE AltName: Full=ATP-dependent Ca(2+) pump PMR1;
DE AltName: Full=Ca(2+)/Mn(2+)-ATPase 2C1 {ECO:0000250|UniProtKB:P98194};
DE AltName: Full=Secretory pathway Ca(2+)-transporting ATPase type 1;
DE Short=SPCA1 {ECO:0000250|UniProtKB:P98194};
GN Name=Atp2c1;
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] (ISOFORMS LONG AND SHORT), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Stomach, and Testis;
RX PubMed=1380825; DOI=10.1021/bi00148a023;
RA Gunteski-Hamblin A.-M., Clarke D.M., Shull G.E.;
RT "Molecular cloning and tissue distribution of alternatively spliced mRNAs
RT encoding possible mammalian homologues of the yeast secretory pathway
RT calcium pump.";
RL Biochemistry 31:7600-7608(1992).
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 (By
CC similarity). Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions
CC on the cytoplasmic side of the membrane and delivers them to the
CC lumenal side. The transfer of ions across the membrane is coupled to
CC ATP hydrolysis and is associated with a transient phosphorylation that
CC shifts the pump conformation from inward-facing to outward-facing state
CC (By similarity). Plays a primary role in the maintenance of Ca(2+)
CC homeostasis in the trans-Golgi compartment with a functional impact on
CC Golgi and post-Golgi protein sorting as well as a structural impact on
CC cisternae morphology. Responsible for loading the Golgi stores with
CC Ca(2+) ions in keratinocytes, contributing to keratinocyte
CC differentiation and epidermis integrity (By similarity). Participates
CC in Ca(2+) and Mn(2+) ions uptake into the Golgi store of hippocampal
CC neurons and regulates protein trafficking required for neural polarity
CC (By similarity). May also play a role in the maintenance of Ca(2+) and
CC Mn(2+) homeostasis and signaling in the cytosol while preventing
CC cytotoxicity (By similarity). {ECO:0000250|UniProtKB:P98194,
CC ECO:0000250|UniProtKB:Q80XR2}.
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:P98194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000250|UniProtKB:P98194};
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:P98194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC Evidence={ECO:0000250|UniProtKB:P98194};
CC -!- SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P98194}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:P98194}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P98194}; Multi-pass membrane protein
CC {ECO:0000255}. Note=During neuron differentiation, shifts from
CC juxtanuclear Golgi position to multiple Golgi structures distributed
CC over the neural soma with a predominance in the apical dendritic trunk.
CC {ECO:0000250|UniProtKB:Q80XR2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Short;
CC IsoId=Q64566-1; Sequence=Displayed;
CC Name=Long;
CC IsoId=Q64566-2; Sequence=VSP_000411;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. The long isoform is only
CC found in testis. {ECO:0000269|PubMed:1380825}.
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; M93017; AAA73341.1; -; mRNA.
DR EMBL; M93018; AAA73342.1; -; mRNA.
DR PIR; A42764; A42764.
DR AlphaFoldDB; Q64566; -.
DR SMR; Q64566; -.
DR STRING; 10116.ENSRNOP00000018175; -.
DR iPTMnet; Q64566; -.
DR PhosphoSitePlus; Q64566; -.
DR SwissPalm; Q64566; -.
DR jPOST; Q64566; -.
DR PaxDb; Q64566; -.
DR PRIDE; Q64566; -.
DR UCSC; RGD:621311; rat. [Q64566-1]
DR RGD; 621311; Atp2c1.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; Q64566; -.
DR PhylomeDB; Q64566; -.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q64566; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:RGD.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140613; F:P-type manganese transporter activity; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0070509; P:calcium ion import; IC:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:RGD.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0032468; P:Golgi calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0032472; P:Golgi calcium ion transport; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006828; P:manganese ion transport; ISS:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030336; ATP2C1.
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:SF2; PTHR42861:SF2; 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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Golgi apparatus; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..919
FT /note="Calcium-transporting ATPase type 2C member 1"
FT /id="PRO_0000046225"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..728
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 753..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 648
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 919
FT /note="V -> FYPKI (in isoform Long)"
FT /evidence="ECO:0000303|PubMed:1380825"
FT /id="VSP_000411"
FT CONFLICT 538
FT /note="L -> F (in Ref. 1; AAA73342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 100500 MW; D26C8C95C14DFB8A CRC64;
MKVARFQKIP NVENETMIPV LTSKRASELA VSEVAGLLQA DLQNGLNKSE VSHRRAFHGW
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVLMRQF DDAVSITVAI LIVVTVAFVQ
EYRSEKSLEE LSKLVPPECH CVREGKLEHT LARDLVPGDT VCLSVGDRVP ADLRLFEAVD
LSIDESSLTG ETTPCSKVTA PQPAATNGDL ASRSNIAFMG TLVRCGKAKG IVIGTGENSE
FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS FYSFGIIGII MLVGWLLGKD ILEMFTISVS
LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET LGCCNVICSD KTGTLTKNEM
TVTHILTSDG LHAEVTGVGY NQFGEVIVDG DVVHGFYNPA VSRIVEAGCV CNDAVIRNNT
LMGKPTEGAL IALAMKMGLD GLQQDYIRKA EYPFSSEQKW MAVKCVHRTQ QDRPEICFMK
GAYEQVIKYC TTYNSKGQTL ALTQQQRDLY QQEKAQMGSA GLRVLALASG PDLGQLTLLG
LVGIIDPPRT GVKEAVTTLI ASGVSIKMIT GDSQETAIAI ASRLGLYSKT SQSVSGEEVD
TMEVQHLSQI VPKVAVFYRA SPRHKMKIIK SLQKNGSVVA MTGDGVNDAV ALKAADIGVA
MGQTGTDVCK EAADMILVDD DFQTIMSAIE EGKGIYNNIK NFVRFQLSTS IAALTLISLA
TLMNFPNPLN AMQILWINII MDGPPAQSLG VEPVDKDVIR KPPRNWKDSI LTKNLILKIL
VSSIIIVCGT LFVFWRELRD NVITPRDTTM TFTCFVFFDM FNALSSRSQT KSVFEIGLCS
NKMFCYAVLG SIMGQLLVIY FPPLQKVFQT ESLSILDLLF LLGLTSSVCI VSEIIKKVER
SREKTQKNTT STPSSFLEV
