AT2C1_PONAB
ID AT2C1_PONAB Reviewed; 918 AA.
AC Q5R5K5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 (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 -!- 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; CR860853; CAH92961.1; -; mRNA.
DR AlphaFoldDB; Q5R5K5; -.
DR SMR; Q5R5K5; -.
DR STRING; 9601.ENSPPYP00000015772; -.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_1_1; -.
DR InParanoid; Q5R5K5; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0005802; C:trans-Golgi network; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0006816; P:calcium ion transport; ISS:UniProtKB.
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; ISS:UniProtKB.
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: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; 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 ATP-binding; Calcium; Calcium transport; Golgi apparatus; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..918
FT /note="Calcium-transporting ATPase type 2C member 1"
FT /id="PRO_0000326150"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..732
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..842
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 895..918
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 643
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 918 AA; 100400 MW; 96C2EE903944AD83 CRC64;
MKVARFQKIP NGENETMIPV LTSKKASELP VSEVASILQA DLQNGLNKCE VSHRRAFHGW
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVLMHQF DDAVSITVAI LIVVTVAFVQ
EYRSEKSLEE LSKLVPPECH CVREGKLEHT LARDLVPGDT VCLSVGDRVP ADLRLFEAVD
LSIDESSLTG ETTPCSKVTA PQPAATNGDL ASRSNIAFMG TLVRCGKAKG VVIGTGENSE
FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS FYSFGIIGII MLVGWLLGKD ILEMFTISVS
LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET LGCCNVICSD KTGTLTKNEM
TVTHIFTSDG LHAEVTGVGY NQFGEVIVDG DVVHGFYNPA VSRIVEAGCV CNDAVIRNNT
LMGKPTEGAL IALAMKMGLD GLQQDYIRKA EYPFSSEQKW MAVKCVHRTQ QDRPEICFMK
GAYEQVIKYC TTYQSKGQTL TLTQQQRDVQ QEKARMGSAG LRVLALASGP ELGQLTFLGL
VGIIDPPRTG VKEAVTTLIA SGVSIKMITG DSQETAIAIA SRLGLYSKTS QSVSGEEIDA
MDVQQLSQIV PKVAVFYRAS PRHKMKIIKS LQKNGSVVAM TGDGVNDAVA LKAADIGVAM
GQTGTDVCKE AADMILVDDD FQTIMSAIEE GKGIYNNIKN FVRFQLSTSI AALTLISLAT
LMNFPNPLNA MQILWINIIM DGPPAQSLGV EPVDKDVIRK PPRNWKDSIL TKNLILKILV
SSIIIVCGTL FVFWRELRDN VITPRDTTMT FTCFVFFDMF NALSSRSQTK SVFEIGLCSN
KMFCYAVLGS IMGQLLVIYF PPLQKVFQTE SLSILDLLFL LGLTSSVCIV AEIIKKVERS
REKIQKHVSS TSSSFLEV
