ID G5EEK8_CAEEL Unreviewed; 1059 AA.
AC G5EEK8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=sca-1 {ECO:0000313|EMBL:CAB07262.1,
GN ECO:0000313|WormBase:K11D9.2a};
GN Synonyms=mca-4 {ECO:0000313|EMBL:CAA09985.1};
GN ORFNames=CELE_K11D9.2 {ECO:0000313|EMBL:CAB07262.1}, K11D9.2
GN {ECO:0000313|WormBase:K11D9.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB07262.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB07262.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB07262.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000313|EMBL:CAA09985.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA09985.1};
RA Kraev A., Kraev N., Carafoli E.;
RT "Cloning and functional expression of the plasma membrane calcium ATPase
RT gene family from Caenorhabditis elegans.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAA09985.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA09985.1};
RA Kraev A.S.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CAB07262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB07262.1};
RA Sulson J.E., Waterston R.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAB07262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB07262.1};
RG WormBase Consortium;
RA WormBase;
RL Submitted (AUG-2023) 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|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}.
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DR EMBL; AJ012296; CAA09985.1; -; mRNA.
DR EMBL; BX284603; CAB07262.1; -; Genomic_DNA.
DR PIR; T23605; T23605.
DR RefSeq; NP_499386.1; NM_066985.4.
DR SMR; G5EEK8; -.
DR IntAct; G5EEK8; 2.
DR STRING; 6239.K11D9.2a.1; -.
DR PaxDb; 6239-K11D9-2a; -.
DR EnsemblMetazoa; K11D9.2a.1; K11D9.2a.1; WBGene00004736.
DR GeneID; 176512; -.
DR AGR; WB:WBGene00004736; -.
DR WormBase; K11D9.2a; CE18884; WBGene00004736; sca-1.
DR eggNOG; KOG0202; Eukaryota.
DR OMA; PLWNNMM; -.
DR OrthoDB; 203629at2759; -.
DR Reactome; R-CEL-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004736; Expressed in larva and 4 other cell types or tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:WormBase.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
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:0031490; F:chromatin DNA binding; IPI:WormBase.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:WormBase.
DR GO; GO:0070509; P:calcium ion import; IDA:WormBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IGI:WormBase.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:WormBase.
DR GO; GO:0050891; P:multicellular organismal-level water homeostasis; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
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; 2.
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 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:G5EEK8,
KW ECO:0007829|PeptideAtlas:G5EEK8};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
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 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 294..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 761..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 835..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 932..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 965..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..76
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1059 AA; 115511 MW; 921131B6625B5D7B CRC64;
MEDAHAKDAN EVCKFFGTGP EGLTPQQVET LRNKYGENEM PAEEGKSLWE LILEQFDDLL
VKILLLAAII SFVLALFEEH EDQTEAVTAF VEPFVILLIL IANATVGVWQ ERNAESAIEA
LKEYEPEMAK VIRSGHHGIQ MVRAKELVPG DLVEVSVGDK IPADLRLVKI YSTTIRIDQS
ILTGESVSVI KHTDSVPDPR AVNQDKKNCL FSGTNVASGK ARGIVFGTGL TTEIGKIRTE
MAETENEKTP LQQKLDEFGE QLSKVISVIC VAVWAINIGH FNDPAHGGSW VKGAIYYFKI
AVALAVAAIP EGLPAVITTC LALGTRRMAK KNAIVRSLPS VETLGCTSVI CSDKTGTLTT
NQMSVSKMFI AGQASGDNIN FTEFAISGST YEPVGKVSTN GREINPAAGE FESLTELAMI
CAMCNDSSVD YNETKKIYEK VGEATETALI VLAEKMNVFG TSKAGLSPKE LGGVCNRVIQ
QKWKKEFTLE FSRDRKSMSA YCFPASGGSG AKMFVKGAPE GVLGRCTHVR VNGQKVPLTS
AMTQKIVDQC VQYGTGRDTL RCLALGTIDT PVSVSNMNLE DSTQFVKYEQ DITFVGVVGM
LDPPRTEVSD SIKACNHAGI RVIMITGDNK NTAEAIGRRI GLFGENEDTT GKAYTGREFD
DLPPEQQSEA CRRAKLFARV EPSHKSKIVD ILQSQGEITA MTGDGVNDAP ALKKAEIGIS
MGSGTAVAKS ASEMVLADDN FASIVSAVEE GRAIYNNMKQ FIRYLISSNV GEVVSIFMVA
ALGIPEALIP VQLLWVNLVT DGLPATALGF NPPDLDIMDR HPRSANDGLI SGWLFFRYLA
VGTYVGVATV GASMWWFLLY EEGPQITYYQ LTHWMRCEIE PDNFADLDCA VFEDNHPNAM
ALSVLVTIEM LNAINSLSEN QSLLVMPPWK NIWLMAAISL SMSLHFVILY VDIMATIFQI
TPLNWVEWIA VLKISLPVLL LDEILKFIAR NYIDGKPETV GAKARSAISL LAWVSVTLAY
FAWMLGPYAE LINHALVGPS VDPSKFDAVV TPDKLHNEL
//
