ID A0A852IDA6_9PICI Unreviewed; 905 AA.
AC A0A852IDA6;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Calcium-transporting ATPase type 2C member 2 {ECO:0000256|ARBA:ARBA00070963};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE AltName: Full=Ca(2+)/Mn(2+)-ATPase 2C2 {ECO:0000256|ARBA:ARBA00083166};
DE AltName: Full=Secretory pathway Ca(2+)-transporting ATPase type 2 {ECO:0000256|ARBA:ARBA00077949};
DE Flags: Fragment;
GN Name=Atp2c2 {ECO:0000313|EMBL:NXX40102.1};
GN ORFNames=TRILEU_R05173 {ECO:0000313|EMBL:NXX40102.1};
OS Tricholaema leucomelas (pied barbet).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC Piciformes; Lybiidae; Tricholaema lacrymosa.
OX NCBI_TaxID=240729 {ECO:0000313|EMBL:NXX40102.1, ECO:0000313|Proteomes:UP000627253};
RN [1] {ECO:0000313|EMBL:NXX40102.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-002-37 {ECO:0000313|EMBL:NXX40102.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXX40102.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (FEB-2020) 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:0000256|ARBA:ARBA00054616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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:ARBA00047282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000256|ARBA:ARBA00047282};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Mn(2+)(in) + ATP + H2O = Mn(2+)(out) + ADP + phosphate + H(+);
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:ARBA00047330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC Evidence={ECO:0000256|ARBA:ARBA00047330};
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:0000256|ARBA:ARBA00062966}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004554}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004166}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXX40102.1}.
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DR EMBL; WAAF01003471; NXX40102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A852IDA6; -.
DR OrthoDB; 3352408at2759; -.
DR Proteomes; UP000627253; Unassembled WGS sequence.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-ARBA.
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; IEA:UniProtKB-EC.
DR CDD; cd02085; P-type_ATPase_SPCA; 1.
DR FunFam; 2.70.150.10:FF:000008; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000006; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 1.
DR FunFam; 3.40.50.1000:FF:000001; Phospholipid-transporting ATPase IC; 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; 1.
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; IPR059000; ATPase_P-type_domA.
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; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 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; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000627253};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 263..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..95
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXX40102.1"
FT NON_TER 905
FT /evidence="ECO:0000313|EMBL:NXX40102.1"
SQ SEQUENCE 905 AA; 99479 MW; 29884D9358F7C0F7 CRC64;
EECELKIIEQ EKEVTVLPPK EACKCHKEDL AKALRVDLQT GLSELSVLQR RSKHGWNEFS
VENTEPIWKK YLDQFKNPLI LLLLASALVS VITKEYEDAA SITVAVLIVV TVAFIQEYRS
EKSLEELNKL VPPECNCLRE GKLQHLLARE LVPGDIIYLS VGDRVPADLR LIEVTDLLVD
ESSFTGEAEP CNKTDSVLLE ARDITTLSNI VFMGTLVRYG KGKGIVIGTG EKSQFGEVFK
MMQAEETPKT PLQKSMDRLG KQLTLFSFGI IGLIMLIGWL QGKRLLSMFT IGVSLAVAAI
PEGLPIVVTV TLVLGVLRMA KKKVIVKKLP IVETLGCCNV ICSDKTGTLT ANEMTVTRLV
TSDGFQAEVS GVGYNGNGNV YLLPSKEVLK EFSNISVGKL VEAGCVVNNA IIRKNSVIGQ
PTEGALIALA MKMDLADIKD IYVRKKEIPF SSEQKWMAVK CMLKTQDQED IYFMKGAFEE
VIQYCTLYNS SGISLSITPQ QRAFYQQEEK RMGSSGLRVL ALASGPELGK LTFLGLVGII
DPPRAGVREA VQVLLESGVS VKMITGDALE TAVAIGQNIG LCNGKLKTMS GEELDQLAEA
ELSSTIKNVS IFFRTSPKHK LKIIKALQRA GAIVSMTGDG VNDAVALKSA DIGIAMGQAG
TDVSKEAANM ILVDDDFSKV MNAIEEGKGI FYNIKNFVRF QLSTSISALS LITLSTVLNL
PNPLNAMQIL WINIIMDGPP AQSLGVEPVD RDTIKQPPRC ITDTILSKSL ILKIFMSAII
IISGTLFVFW KENPKSVITP RTTTMTFTCF VFFDLFNALT CRSQTKLIFE IGFFRNRMFL
YSVLGSFLGQ LAVIYIPPLQ KIFQTENLGA LDLLFLTGLA SSVFIVSELV KLCEKHYCPP
KHTKR
//
