AT2C1_BOVIN
ID AT2C1_BOVIN Reviewed; 953 AA.
AC P57709;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
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; Synonyms=SPCA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Prapong S., Reinhardt T.A.;
RT "Bos taurus mRNA encoding putative secretory pathway Ca2+-transporting
RT ATPase (SPCA).";
RL Submitted (FEB-2000) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF230532; AAF64433.1; -; mRNA.
DR RefSeq; NP_786979.1; NM_175785.2.
DR AlphaFoldDB; P57709; -.
DR SMR; P57709; -.
DR STRING; 9913.ENSBTAP00000015441; -.
DR PaxDb; P57709; -.
DR PRIDE; P57709; -.
DR Ensembl; ENSBTAT00000068713; ENSBTAP00000072313; ENSBTAG00000011626.
DR GeneID; 327663; -.
DR KEGG; bta:327663; -.
DR CTD; 27032; -.
DR VEuPathDB; HostDB:ENSBTAG00000011626; -.
DR VGNC; VGNC:26296; ATP2C1.
DR eggNOG; KOG0202; Eukaryota.
DR GeneTree; ENSGT00940000156421; -.
DR HOGENOM; CLU_002360_3_1_1; -.
DR InParanoid; P57709; -.
DR OMA; GVHRMAK; -.
DR OrthoDB; 100699at2759; -.
DR TreeFam; TF354251; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000011626; Expressed in oviduct epithelium and 108 other tissues.
DR ExpressionAtlas; P57709; baseline and differential.
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; 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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
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: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; 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..953
FT /note="Calcium-transporting ATPase type 2C member 1"
FT /id="PRO_0000046222"
FT TOPO_DOM 1..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..125
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..138
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..157
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 158..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 297..316
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 317..328
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 329..346
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 347..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 734..753
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 754..763
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 764..784
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 785..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 805..824
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 825..842
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 843..862
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 863..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 876..894
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 895..909
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 910..930
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 931..953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ACT_SITE 384
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 678
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 772
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 776
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 953 AA; 104780 MW; 2412EEB45AFB000F CRC64;
MDNLLPQSRF SYFKKYPIHA IRKYLSMLRN QKEEEQVARF QKIPNAENET MIPVLTSKKA
SELPVSEVAS ILQADLQNGL NKCEVSHRRA FHGWNEFDIS EDEPLWKKYI SQFKNPLIML
LLASAVISVL MHQFDDAVSI TVAILIVVTV AFVQEYRSEK SLEELSKLMP PECHCVREGK
LEHTLARDLV PGDTVCLSVG DRVPADLRLF EAVDLSVDES SLTGETTPCS KVTAPQPAAT
NGDLASRSNI AFMGTLVRCG KAKGIVIGTG ENSEFGEVFK MMQAEEAPKT PLQKSMDLLG
KQLSFYSFGI IGIIMLVGWL LGKDILEMFT ISVSLAVAAI PEGLPIVVTV TLALGVMRMV
KKRAIVKKLP IVETLGCCNV ICSDKTGTLT KNEMTVTHIF TSDGLRAEVT GVGYNPFGEV
IVDGDVVHGF YNPSVSRIVE AGCVCNDAVI RNNTLMGKPT EGALIALAMK MGLDGLQQDY
IRKAEYPFSS EQKWMAVKCV HRTQQDRPEI CFMKGAYEQV IKYCTTYHSK GQTLTLTQQQ
RDLYQQEKAQ MGSAGLRVLA LASGPELGQL TFLGLVGIID PPRTGVKEAV TTLIASGVSI
KMITGDSQET AVAIASRLGL YSKTSQSVSG EEIDAMDVQQ LSQIVPKVAV FYRASPRHKM
KIIKSLQKNG SVVAMTGDGV NDAVALKAAD IGVAMGQTGT DVCKEAADMI LVDDDFQTIM
SAIEEGKGIY NNIKNFVRFQ LSTSIAALTL ISLATLMNFP NPLNAMQILW INIIMDGPPA
QSLGVEPVDK DVIRKPPRNW KDSILTKNLI LKILVSSIII VCGTLFVFWR ELRDNVITPR
DTTMTFTCFV FFDMFNALSS RSQTKSVFEI GLCSNKMFCY AVLGSIMGQL LVIYFPPLQK
VFQTESLSIL DLLFLLGLTS SVCIVAEIIK KVERSREKIQ KPVSSTSSSF LEV
