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Database: UniProt
Entry: G0P8B4_CAEBE
LinkDB: G0P8B4_CAEBE
Original site: G0P8B4_CAEBE 
ID   G0P8B4_CAEBE            Unreviewed;      1229 AA.
AC   G0P8B4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=CAEBREN_01621 {ECO:0000313|EMBL:EGT47678.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) 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: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; GL380130; EGT47678.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0P8B4; -.
DR   STRING; 135651.G0P8B4; -.
DR   EnsemblMetazoa; CBN01621.1; CBN01621.1; WBGene00140346.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_0_1; -.
DR   InParanoid; G0P8B4; -.
DR   OMA; QWGYSIV; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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; 3.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
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; 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; 2.
DR   PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 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; 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, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000008068};
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        86..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        123..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        334..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        372..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        823..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        854..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        900..918
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        938..956
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        976..996
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1008..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          29..103
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1143..1229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1180..1222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1229 AA;  134042 MW;  ABB6E71EA0D7EE72 CRC64;
     MPEYGASLEE LRALMEYRSA EAKEKIDTDY GGTAGLCEKL RTDPNNGLPN SESELETRRN
     VFGANEIPPH PPKCFLQLVW EALQDVTLVI LLVSAIVSLA LSFYRPPGED TAGTDDSEHD
     AGWIEGVAIL ISVIVVVLVT ALNDYTKERQ FRGLQAKIET EHRFFVLRGG QSVQVVVNEL
     VVGDIAQIKY GDLIPADGVL IQSNDLKMDE SSLTGESDQI RKSPEHDPII LSGTHVMEGS
     GKMLVTAVGV NSQTGIIMTL LGAAKTVAEE ERKTAKREGG DGASGAEEGT AQALLDSKGD
     EAMANGKAVP APEADGKKER SVLQAKLTRL AIQIGYAGSF VAGCTVLILI IRFCISRYAI
     DGKSFSLADF QYFINFLIIG VTVLVVAVPE GLPLAVTLSL AYSVKKMMLD NNLVRHLDAC
     ETMGNATSIC SDKTGTLTTN RMTVVQSFIN DVHHKDTPKI ESLDQNTAKL MMDCISVNSS
     YSSQVIPPKQ IGEQATQLGN KTECGMLGFV LALGKSYQEI RDRHPEETIP KVYTFNSVRK
     SMSTVINLPD GGFRVFSKGA SEIVTKRCKY FLGKNGALNK FSSKDAENLV RDVIEPMASD
     GLRTICVAYK DYVPSSKKTA DNQIAYSSEP DWENEEAIVG DMTAIAILGI QDPVRPEVPA
     AITRCQEAGI TVRMVTGDNI NTARSIATAC GILKPGEDFI ALEGKEFNAR IRDENGEVSQ
     EKLDLIWPKL RVLARAQPSD KYTLVKGIID SRVTDSREVV AVTGDGTNDG PALKKADVGF
     AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI AKFLQFQLTV NVVAVVVAFV
     GACAIQDTPL KAVQMLWVNL IMDTLASLAL ATEMPTEELL KRKPYGRTSP LISRTMSKNI
     LGHAVYQLVV LFTLIFYGEQ CFNIPNGRWA PLHSPPSKHF TIVFNTFVMM TLFNEINARK
     IHGERNIFKG LFSNPIYYVI WIATMISQVI IVQFGGRWFS TAALNTSEWL WCLAFGVGTL
     LWGQIVTSIP TGSLPANMTI GSGEAPTNDP LMPDYEDSDT HEKRSGQILW VRGLTRLQTQ
     LRVVKAFRSS LEEFDERRSI ASTHSVQSIR GGFWGGGRHT TTAASPDPAN ARNAMAAISH
     RQSPQPYPYY HHQQPRTPSP QPHIVVENGN AGGNGAATGA PPKQESNGKT EKVPLVQQWS
     PDTNSSYTQT QRSINKSMSL DTPVSVAHV
//
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