ID A0A7E4V354_PANRE Unreviewed; 1309 AA.
AC A0A7E4V354;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Panagrellus redivivus (Microworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC Panagrellus.
OX NCBI_TaxID=6233 {ECO:0000313|Proteomes:UP000492821, ECO:0000313|WBParaSite:Pan_g15951.t1};
RN [1] {ECO:0000313|Proteomes:UP000492821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT8872 {ECO:0000313|Proteomes:UP000492821};
RX PubMed=23410827; DOI=10.1534/genetics.112.148809;
RA Srinivasan J., Dillman A.R., Macchietto M.G., Heikkinen L., Lakso M.,
RA Fracchia K.M., Antoshechkin I., Mortazavi A., Wong G., Sternberg P.W.;
RT "The draft genome and transcriptome of Panagrellus redivivus are shaped by
RT the harsh demands of a free-living lifestyle.";
RL Genetics 193:1279-1295(2013).
RN [2] {ECO:0000313|WBParaSite:Pan_g15951.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (OCT-2020) to UniProtKB.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR WBParaSite; Pan_g15951.t1; Pan_g15951.t1; Pan_g15951.
DR Proteomes; UP000492821; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:TreeGrafter.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR FunFam; 1.20.1110.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000033; Calcium-transporting ATPase; 1.
DR FunFam; 2.70.150.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000060; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000007; Calcium-transporting ATPase; 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 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; IPR059000; ATPase_P-type_domA.
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; 3.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF253; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE MCA-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 Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000492821};
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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 430..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 475..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1046..1064
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1117..1139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 110..184
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..410
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1246
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 143609 MW; 2574D5ADD67D3ED3 CRC64;
MRNSQNVTDQ STVCGDSTAG RRSSVGGAGF ELVIDEDDSG TGGICGSKPQ KAHILSEIPL
HGDELKATDG DAKHGSTGQE AGDASSATLD ELKKLMETRG AEAIVQLDNE YNGFEGLCEK
LDVNPIRGLP NDPKVLQRRR QKYGANVIPK GASKPFWRLV LDASKDPTLL ILILSGFVSL
ALSFYEPDQE VTDVIPSVSS LFADKDHHEG DAAAHILLNS TEFLNSTNPH EQRHEDHGTA
WIEGAAILLS VIVVVLVTAV NDYSKERQFQ NLRNKIETGH QFSVIRDGDT FDVPVADLVV
GDIVRVKYGD LIPADGILIQ ANDLKIDESS LTGESDHVRK TVESDPVILS GTYAMEGSGK
MVITAVGVNS QTGIIMMLLT GGKGSDGSSS SSSSSSSSDT DSTGSGSSRS SSEDGDITSK
SVLQTKLSQL ALQIIYCGTT IAVIALIVLV ARYSIQRYAI EKQPFTFADL HSGVKFFIIA
VTILVISIPE GLPLAIALSL TYSVKKMMKD NNLVRHMDAC ETMGNATTIC SDKTGTLTTN
QMTVVQSYVD GQYHNDMQSQ PTATSLPVFT RNILSEALSV NSAYNSMVVP PTKAGERAQQ
VGNKTECGLL GFVTQIGGDY DAIRKSHPEE GMVKVYTFNS SRKSMMSVIE LVENGVKVGY
RVFAKGASEI LLSKCAYFVG QNGVIEAFTA EKCEGIMHNV IKEMAENGLR TICVAYKDYV
YSNVRPAEET EIGIDSDKAI DWDDEEQVAS RFVGIAICGI QDPVRPEVPE AIRRCTRAGI
TVRMVTGDNI NTARAIAIQC GILKPGDDFL VLEGKQFNER IRDEKGQVSQ EKLDAVWPRL
RVLARAQPID KYTLVKGIID SKNSLQREIV AVTGDGTNDG PALKKADVGF AMGVAGTDVA
KEASDIILTD DNFTSIVRAV MWGRNVYDSI SKFLQFQLTV NVVAVFTAFI GACTVSDSPL
KAVHMLWINL IMDTLASLAL ATETPTDELL ERKPYGRKKS LISRTMFKNI AMHALYQLGV
LLVFLFRGPE LFGIPSGLNA PLFSPPSVHF TIVFNTFVMM TLFNEINCRK VHGERNVFKY
LSTNHMFIGI WISTFICQIL IVQFGGPWFS TAPLTPAQWF VCLAFGLSEL AFGQFVATIP
AKKLPKSFRV GRGEAPPSKL RMERVEEHHD RSMQMQAAPS RGMNLWMRAF ELIGLHYRVI
NAFRRNMREK TLGETAPKMT AAAAEQWRQS YKHYRRRKHH DRRMHRAMSM EGDDVPPTAI
EGGKPPRLTT HRERKIHRHI KEIARPHSQD HSIGRNDSTG DGSKNDLNV
//
