ID A0A553NZ60_TIGCA Unreviewed; 1024 AA.
AC A0A553NZ60;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
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 ORFNames=TCAL_09675 {ECO:0000313|EMBL:TRY70707.1};
OS Tigriopus californicus (Marine copepod).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus.
OX NCBI_TaxID=6832 {ECO:0000313|EMBL:TRY70707.1, ECO:0000313|Proteomes:UP000318571};
RN [1] {ECO:0000313|EMBL:TRY70707.1, ECO:0000313|Proteomes:UP000318571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Diego {ECO:0000313|EMBL:TRY70707.1,
RC ECO:0000313|Proteomes:UP000318571};
RX PubMed=29988158; DOI=.1038/s41559-018-0588-1;
RA Barreto F.S., Watson E.T., Lima T.G., Willett C.S., Edmands S., Li W.,
RA Burton R.S.;
RT "Genomic signatures of mitonuclear coevolution across populations of
RT Tigriopus californicus.";
RL Nat. Ecol. Evol. 2:1250-1257(2018).
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:ARBA00000363,
CC ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {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:TRY70707.1}.
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DR EMBL; VCGU01000009; TRY70707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553NZ60; -.
DR STRING; 6832.A0A553NZ60; -.
DR EnsemblMetazoa; TCAL_09675-PA_mrna; TRY70707.1; TCAL_09675.
DR OMA; PLWNNMM; -.
DR Proteomes; UP000318571; Chromosome 9.
DR GO; GO:0033017; C:sarcoplasmic reticulum 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; cd02083; P-type_ATPase_SERCA; 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; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 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, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|RuleBase:RU361146};
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:UP000318571};
KW Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
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 60..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 292..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 755..778
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 829..852
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 923..945
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 8..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1024 AA; 113223 MW; 35023813BC9F8DC3 CRC64;
MEDAFMCSWE ECCERFQVKV DRGLSKEQVD QNLEKYGHNE LPAEEGKSIW RLILEQFDDL
LVKILLLAAI ISFVLAFFED DEDSITAFVE PFVILLILIA NAIVGVWQER NAESAIEALK
EYEPEMGKVI RSDKDGVQKI RARDIVPGDI VEISVGDKAP ADLRLINILS TTLRIDQSIL
TGESVSVIKH NEPVPDPKSV NQDKKNLVFS GTNVAAGKAV GIVIGTGLNT AIGRIRTEMT
QTEEIRTPLQ QKLDEFGEQL SKVITLICIA VWAINIGHFN DPAHGGSWMK GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNM
MSVCKMFAFK SESNFEEFEI SGSTYEPIGE IFQSGRKVKG QDFVSLEELS TISIMCNDSA
IDFNDYKNAF EKVGEATETA LIVLAEKINP YGVSKSGGRL DSAKAVRKDM ESKWNKEFTL
EFSRDRKSMS SYCTPKKPTR IGSGSKLFVK GAPEGVLDRC SHYRVGTEKR EMTREIRHKI
MERAVAYGTG RDTLRCLALA TGDNPVNPKD MDMADATKFV RYEVNLTFVG VVGMLDPPRM
EVTPSIQLCR EAGIRVIMIT GDNKNTAEAI CRRIGIFGED ENTEGLAFSG REFDALSIPE
QRKAVSKAKM FARVEPFHKS KIIEYLQSMK EVSAMTGDGV NDAPALKKAE IGIAMGSGTA
VAKSASEMVL ADDNFASIVA AVEEGRAIYN NMKQFIRYLI SSNIGEVVSI FLTAALGLPE
ALIPVQLLWV NLVTDGLPAT ALGFNPPDLD IMTKPPRSSE ETLITPWLFF RYMAIGLYVG
IATVGGAAYW FLMDPTGPQM SYYQLSHFMQ CTVEPEKFKG ISCDIFQAPE PMTMALSILV
TIEMANAINS LSENQSLMVM PPWINPILLA AMALSFSLHF MILYVDVLAT VFQITPLSFE
QWITVMKFSL PVILLDELLK FVARNYTDGK RGLKIKWGEL FAILAVFVAY GYGWYLHELS
ILAR
//
