ID A0A093KCI5_STRCA Unreviewed; 860 AA.
AC A0A093KCI5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Calcium-transporting ATPase type 2C member 1 {ECO:0000256|ARBA:ARBA00022187};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE AltName: Full=ATP-dependent Ca(2+) pump PMR1 {ECO:0000256|ARBA:ARBA00030859};
DE AltName: Full=Ca(2+)/Mn(2+)-ATPase 2C1 {ECO:0000256|ARBA:ARBA00031856};
DE AltName: Full=Secretory pathway Ca(2+)-transporting ATPase type 1 {ECO:0000256|ARBA:ARBA00030666};
DE Flags: Fragment;
GN ORFNames=N308_03625 {ECO:0000313|EMBL:KFV87984.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV87984.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV87984.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV87984.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR EMBL; KL206987; KFV87984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093KCI5; -.
DR STRING; 441894.ENSSCUP00000019510; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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 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; 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; 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; PR00120; HATPASE.
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:ARBA00022568};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
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:ARBA00022568}.
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 804..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..59
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV87984.1"
FT NON_TER 860
FT /evidence="ECO:0000313|EMBL:KFV87984.1"
SQ SEQUENCE 860 AA; 93878 MW; 09D165EF54AEAE7D CRC64;
NLQNGLKNCE VCHRRAFHGW NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVVMHQF
DDAVSITVAI LIVVTVAFVQ EYRSEKSLEE LSKLVPPECH CVREGRVEHT LARDLVPGDT
VCLSVGDRVP ADLRLFEAVD LSVDESSLTG ETAPCSKSTA PQPAATNGDL TSRSNIAFMG
TLVRCGKAKG IVIGTGENSE FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS LYSFGIIGII
MVVGWLQGKH ILDMFTIGVS LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET
LGCCNVICSD KTGTLTKNEM TVTHIFTSDG QHAEVTGVGY NRFGEVILDG DVIHGYNNPS
ISKIVEAGCV CNDALIRNNT LMGKPTEGAL IALAMKMGLD GLQEDYIRKA EYPFSSEQKW
MAVKCVHRTQ QDKPEVCFMK GAYEQVIKYC TSYNCKGQAL PLVQQQREQY QQEKTSMGCA
GLRVLALASG PELGQLTFLG LVGIIDPPRS GVKEAVTTLI TSGVAIKMIT GDSQETAVAI
ASRLGLYSKN SQALSGEEID GLDIQQLSQI TPKVAVFYRA SPRHKLKIIK SLQNNGAVVA
MTGDGVNDAV ALKAADIGVA MGQTGTDVCK EAADMILVDD DFQTIMSAIE EGKGIYNNIK
NFVRFQLSTS IAALTLISLA TLMNFPNPLN AMQILWINII MDGPPAQSLG VEPVDKDVIQ
KPPRNLKDSI LTKNLIVKIL VSSIIIVCGT LFVFWRELRD NVITPRDTTM TFTCFVFFDM
FNALSSRSQA KSVFEIGLCS NKMFCYAVLG SIMGQLLVIY FPPLQKVFQT ESLSVLDLLF
LLGLTSSVCI VTEIIKKFER
//
