ID A0A3Q1JAR2_ANATE Unreviewed; 1031 AA.
AC A0A3Q1JAR2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000028249.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000028249.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- 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; A0A3Q1JAR2; -.
DR Ensembl; ENSATET00000028690.2; ENSATEP00000028249.2; ENSATEG00000019480.2.
DR GeneTree; ENSGT00940000164922; -.
DR InParanoid; A0A3Q1JAR2; -.
DR Proteomes; UP000265040; 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; 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:SF92; CALCIUM-TRANSPORTING ATPASE; 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; 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|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};
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:UP000265040};
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 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 292..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 751..772
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 824..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 922..941
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..71
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1031 AA; 112974 MW; 6ACF3B51BF604535 CRC64;
MENAHTKAPA ECLAHFGVNE NTGLTPDQFK KNLDKFGYNG KSIWELVIEQ FEDLLVRILL
LAACISFVLA WFEEGEETVT AFVEPFVILL ILIANAVVGV WQERNAESAI EALKEYEPEM
GKVYRSDRKS VQRIKAREIV PGDIVEVSVG DKVPADIRIV SIKSTTLRVD QSILTGESVS
VIKHTDPVPD PRAVNQDKKN MLFSGTNIAA GKAIGVAVAT GVSTEIGKIR DQMAATEQEK
TPLQAKLDEF GEQLSKVISL ICVAVWAINI GHFNDPVHGG SWIRGAVYYF KIAVALAVAA
IPEGLPAVIT TCLALGTRRM AKKNAIVRSL PSVETLGCTS VICSDKTGTL TTNQMCVTKM
FIVKTVDGDH VDLDAFDISG SKYTPEGEVT QGGAKVVCSA YDGLVELSTI CALCNDSSLD
YNESKKIYEK VGEATETALC CLVEKMNVFN SNVKNLSRIE RANACCTVIK QLMRKNFTLE
FSRDRKSMSV YCTPSKGDGG PKMFVKGAPE GVIERCAYVR VGTTRVPLTN AIKEKIMAVI
RDWGTGRDTL RCLALATRDT PLKLEEMNLE DSTKFADYET DLTFVGCVGM LDPPRKEVTG
SIELCRAAGI RVIMITGDNK GTAIAICRRI GIFSEDEDVS GRAYTGREFD DLPIHEQAEA
VRRACCFARV EPSHKSKIVE FLQGFDDITA MTGDGVNDAP ALKKAEIGIA MGSGTAVAKS
ASEMVLADDN FSSIVAAVEE GRAIYNNMKQ FIRYLISSNV GEVVCIFLTA ALGLPEALIP
VQLLWVNLVT DGLPATALGF NPPDLDIMGK PPRSPKEPLI SGWLFFRYMA IGGYVGAATV
GGAAWWFLYD QTGPGVTYYQ LSHFMQCHEE NEDFAGLDCE IFEAAPPMTM ALSVLVTIEM
CNALNSLSEN QSLVRMPPWS NFWLLAAMTL SMSLHFMIIY VDPLPMIFKL THLSTEQWLM
VLKLSFPVIL IDEVLKFVAR NYVEGIPQLV VASGYCHAHI CIFCVCSCTY ACSFTAYYVE
LWDLLVNEGH K
//
