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Entry: A0A5F4WBN8_CALJA
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ID   A0A5F4WBN8_CALJA        Unreviewed;       960 AA.
AC   A0A5F4WBN8;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=ATP2C1 {ECO:0000313|Ensembl:ENSCJAP00000075108.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000075108.2, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000075108.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000075108.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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:0000256|ARBA:ARBA00024147};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC         Evidence={ECO:0000256|ARBA:ARBA00024147};
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:0000256|ARBA:ARBA00024272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC         Evidence={ECO:0000256|ARBA:ARBA00024272};
CC   -!- SUBUNIT: Monomer. Homodimer. {ECO:0000256|ARBA:ARBA00024380}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004205}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004205}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR   AlphaFoldDB; A0A5F4WBN8; -.
DR   Ensembl; ENSCJAT00000098165.2; ENSCJAP00000075108.2; ENSCJAG00000003182.5.
DR   GeneTree; ENSGT00940000156421; -.
DR   Proteomes; UP000008225; Chromosome 17.
DR   Bgee; ENSCJAG00000003182; Expressed in frontal cortex and 6 other cell types or tissues.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0140613; F:P-type manganese transporter activity; IEA:RHEA.
DR   CDD; cd02085; P-type_ATPase_SPCA; 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; 3.
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; 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   NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF2; CALCIUM-TRANSPORTING ATPASE TYPE 2C MEMBER 1; 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; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        113..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        137..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        303..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        328..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        786..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        818..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        855..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        884..906
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          59..133
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   960 AA;  105592 MW;  6C5D9C636CE1DF56 CRC64;
     MDSLLPPSRF SYFKKYPLHT IRRYLSTLRN QRAEEQVARF QKIPNGENET MIPVLTSKKA
     SELPVSEVAS ILQADLQNGL NKCEVNHRRA FHGWNEFDIS EDEPLWKKYI SQFKNPLIML
     LLASAVISVL MHQFDDAVSI TVAILIVVTV AFVQEYRSEK SLEELSKLVP PECHCVREGK
     LEHTLARDLV PGDTVCLSVG DRVPADLRLF EAVDLSIDES SLTGETTPCS KVTAPQPATT
     NGDLASRSNI AFMGTLVRCG KAKGVVIGTG ENSEFGEVFK MMQAEEAPKT PLQKSMDLLG
     KQLSFYSFGI IGIIMLVGWL LGKDILEMFT ISVSLAVAAI PEGLPIVVTV TLALGVMRMV
     KKRAIVKKLP IVETLGCCNV ICSDKTGTLT KNEMTVTHIF TSDGLHAEVT GVGYNQFGEV
     IVDGDVVHGF YNPAVSRIVE AGCVCNDAVI RNNTLMGKPT EGALIALAMK MGLDGLQQDY
     IRKAEYPFSS EQKWMAVKCV HRTQQDRPEI CFMKGAYEQV IKYCTTYQSK GQTLTLTQQQ
     RDVYQQEKAR MGSAGLRVLA LASGPELGQL TFLGLVGIID PPRTGVKEAV TTLIASGVSI
     KMITGDSQET AVAIASRLGL YSKTSQSVSG EEIDGMDVQQ LSQIVPKVAV FYRASPRHKM
     KIIKSLQKNG SVVAMTGDGV NDAVALKAAD IGVAMGQTGT DVCKEAADMI LVDDDFQTIM
     SIAALTLISL ATLMNFPNPL NAMQILWINI IMDGPPAQSL GVEPVDKDVI RKPPRNWKDS
     ILTKNLILKI LVSSIIIVCG TLFVFWRELR DNVITPRDTT MTFTCFVFFD MFNALSSRSQ
     TKSVFEIGLC SNKMFCYAVL GSIMGQLLVI YFPPLQKVFQ TESLSILDLL FLLGLTSSVC
     IVAEIIKKVE RSREKIQKHV SSTSSSFLEV WLWQRSGQQL VEIQPHLETG LPLTEDVSCV
//
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