ID A0A662YZ04_ACIRT Unreviewed; 1212 AA.
AC A0A662YZ04;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=EOD39_7862 {ECO:0000313|EMBL:RXN01122.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXN01122.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXN01122.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXN01122.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXN01122.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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:RXN01122.1}.
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DR EMBL; SCEB01000082; RXN01122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A662YZ04; -.
DR Proteomes; UP000289886; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 2.
DR InterPro; IPR022141; ATP_Ca_trans_C.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF245; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 1; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00122; E1-E2_ATPase; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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|RuleBase:RU361146};
KW Calcium {ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|RuleBase:RU361146};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000289886};
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 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 405..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 918..935
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 955..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 993..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1026..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 866..1044
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT DOMAIN 1089..1135
FT /note="Plasma membrane calcium transporting P-type ATPase
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12424"
FT REGION 227..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 133579 MW; 51BD6237ECF626B6 CRC64;
MANNSYSGVK NSVAEANHDG EFGVTVKDLR DLMELRGTEG LRKIEDCYGD VSGLCSRLKT
QPVGVCGTAA GGVEDEGESH AGWIEGVAIL LSVVCVVLVT AFNDWSKEKQ FRGLQNRIEQ
EQKFTVVRGG QVIQIPVAEI VVGDIAQVKY GDLLPADGVL IQGNDLKIDE SSLTGESDHV
KKTLDKDPLL LSGTHVMEGS GKVLVTAVGV NSQTGIIFTL LGAGEDEDKD KEEKQKKKDK
KNKKQDGSVE NRNKAKAQDG AGMEMQPLKS EEGLDGDAQE KRKANMSKKE KSVLQGKLTK
LAVQIGKAAK AQDGAGMEMQ PLKSEEGLDG DAQEKRKANM SKKEKSVLQG KLTKLAVQIG
KAGLVMSAIT VIILVLYFVI NTFWVQNISW ITECTPIYIQ YFVKFFIIGV TVLVVAVPEG
LPLAVTISLA YSVKKMMKDN NLVRHLDACE TMGNATAICS DKTGTLTMNR MTVVQVFIGE
NHYRKVPEPE AVPEKCLDLL VTGIGVNCAY TTKILSPEKE GGLPRHVGNK TECALLGFAL
DLKRDYQAVR NEIPEEKLYK VYTFNSVRKS MSTVLKNADG SYRMFSKGAS EILLKKCYRI
LNADGEAKLF RPRDRDDMVK KVIEPMASEG LRTICLAYRD FPAGDSEPEW DNENDILTSL
TCICVVGIED PVRPEVPDAI KKCQRAGITV RMVTGDNINT ARAIAIKCGI LLPGDDFLCI
EGKEFNRRIR NEKGEIEQER IDKIWPKLRV LARSSPTDKH TLVKGIIDST IVEQRQVVAV
TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN FSSIVKAVMW GRNVYDSISK
FLQFQLTVNI VAVIVAFTGA CITQDSPLKA VQMLWVNLIM DTFASLALAT EPPTESLLLR
KPYGRNKPLI SRTMMKNILG HGVYQLTVIF TLLFAGEKIF DIDSGRNAPL HAPPSEHYTI
VFNTFVMMQL FNEINARKIH GERNVFEGIF NNLIFCSIVF GTFVIQIVIV QFGGKPFSCI
GLGIDHWLWC VFLGIGALLW GQLISSIPTS RLKFLKEAGH GTQKDDYPDE ELEEDMEEID
HGERELRRGQ ILWFRGLNRI QTQIRVVNAF RSSLYEGLEK PESRNSIHNF MNQPEFQIED
SEPHIPLIDD TDAEDDAPTK RNSSPPRNSS PPPSPNKNNN AVDSGIHLTL DTSKSATSSS
PGSPLHSLET SL
//
