ID A0A3B3Q1V5_9TELE Unreviewed; 1049 AA.
AC A0A3B3Q1V5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000000272.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000000272.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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=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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004326}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
CC 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 AlphaFoldDB; A0A3B3Q1V5; -.
DR STRING; 1676925.ENSPKIP00000000272; -.
DR Ensembl; ENSPKIT00000024160.1; ENSPKIP00000000272.1; ENSPKIG00000018942.1.
DR GeneTree; ENSGT00940000164922; -.
DR Proteomes; UP000261540; Unplaced.
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; 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:SF24; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 1; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 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 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|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {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 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 99..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 130..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 806..827
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 879..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 977..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 830..1033
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
SQ SEQUENCE 1049 AA; 115678 MW; 74D91F4D83962E93 CRC64;
MKHAGLNVNK LHYAHNHDIQ TAVKQRRGYS LGMKTCPIIR NISLKTRPLD RSIYPCNATG
HNYLGLGAIF MQSIHRRIQK QQSWTEHHRK QKSYVPHGLL CLTLAVHFDL VLLDVCFTQV
LAWFEEGEET VTAFVEPFVI LLILIANAVV GVWQERNAES AIEALKEYEP EMGKVYRADR
KSVQRIKARE IVPGDIVEVS VGDKVPSDIR ITSIRSTTLR VDQSILTGES VSVIKHTDPV
PDPRAVNQDK KNMLFSGTNI AAGKAIGVAV ATGVSTEIGK IRDQMAATEQ EKTPLQQKLD
EFGEQLSKVI SLICVAVWMI NIGHFNDPVH GGSWIRGAVY YFKIAVALAV AAIPEGLPAV
ITTCLALGTR RMAKKNAIVR SLPSVETLGC TSVICSDKTG TLTTNQMCVT KMFVIDKVEG
DHVALEEFNI SGSKYTPEGE VTKAGARVNC SIYDGLVELA TICALCNDSS LDFNEAKGIY
EKVGEATETA LCCLVEKMNV FSTDVRNLSK VERANACCTV IKQLMKKEFT LEFSRDRKSM
SVYCSPAKSS KAPVGNKMFV KGAPEGVIER CAYVRVGTTR VPLTGPVKDK IMAVIKEWGT
GRDTLRCLAL ATRDTPLKKE EMNLEDSTKF ADYEMDLTFV GCVGMLDPPR KEVTGSIELC
REAGIRVIMI TGDNKGTAVA ICRRIGIFGE DEDVLGRAFT GREFDDLSVM DQREAVRIAC
CYARVEPSHK SKIVEYLQSY DEITAMTGDG VNDAPALKKA EIGIAMGSGT AVAKSASEMV
LADDNFSSIV AAVEEGRAIY NNMKQFIRYL ISSNVGEVVC IFLTAALGLP EALIPVQLLW
VNLVTDGLPA TALGFNPPDL DIMGRPPRSP KEPLISGWLF FRYMAIGGYV GAATVGAAAW
WFLYCDEGPM ITYYQLSHFM QCSPENEDFN GIDCEVFESP EPMTMALSVL VTIEMCNALN
SLSENQSLVR MPPWSNGWLI AAMTLSMSLH FLIIYVDPLP MVFKLTHLNV EQWMVVLKLS
FPVILIDEVL KFVARNYLEG TDKTLLQKK
//
