ID A0A3Q1ITU0_ANATE Unreviewed; 1257 AA.
AC A0A3Q1ITU0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 25.
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:ENSATEP00000025437.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000025437.2}
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1ITU0; -.
DR Ensembl; ENSATET00000025855.2; ENSATEP00000025437.2; ENSATEG00000017529.2.
DR GeneTree; ENSGT00940000154527; -.
DR InParanoid; A0A3Q1ITU0; -.
DR Proteomes; UP000265040; Unplaced.
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; 2.
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; 3.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF245; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 1; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 2.
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; 2.
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 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};
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 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 379..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 420..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 856..877
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 933..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 971..989
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1041..1062
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 45..121
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 286..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 139029 MW; 89A62C7BC9D3F8A5 CRC64;
MANNSYSGVK NSMVEANHDG EFGCTLNELR SLMELRGADA LGKIGETYGD VQRLCNRLKT
SPTDGLSGQP GDIEKRKTVF GQNFIPPKKP KTFLQLVWEA LQDVTLIILE VAAIVSLCLS
FYRPPDTERE NCGRAAGGVE DENESEAGWI EGAAILLSVI CVVVVTAFND WSKEKQFRGL
QSRIEQEQKF TVVRGGQVIQ IPVAEIVVGD IAQIKYGDLL PADGVLIQGN DLKIDESSLT
GESDHVKKTQ EKDPMLLSGT HVMEGSGKMV VTAVGVNSQT GIIFTLLGGG DDDDDEEEEK
KKEKEEKKKQ RKNKKQDGSV ENRKKAKAQD GAAMEMQPLN SDEGADAEEK KKANLPKKEK
SVLQGKLTKL AVQIGKAGLV MSAITVIILV VLFVVDTFWI QKLEWTKDCT PIYIQFFVKF
FIIGVTVLVV AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT
LTMNRMTVVQ AYVAEKHYKK VPEPENIPSS TLDILILGIA VNCAYTTKIM PPEKEGGLPR
QVGNKTECAL LGFANDLKRD YQAIRNEIPE EKLYKVYTFN SVRKSMSTVL KMADGSYRMF
SKGASEILLK KCYKILTANG EPKVFRPRDR DDMVKKVIEP MASEGLRTIC LGYRDFPASE
GEPDWENEND ILTGLTCVCV VGIEDPVRPE VPDAIRKCQR AGITVRMVTG DNINTARAIA
TKCGILQPGD DFLCLEGKEF NRRIRNEKGE IEQERIDKIW PKLRVLARSS PTDKHTLVKG
IIDSTVAEQR QVVAVTGDGT NDGPALKKAD VGFAMGIAGT DVAKEASDII LTDDNFSSIV
RAVMWGRNVY DSISKFLQFQ LTVNVVAVIV AFTGACITQD SPLKAVQMLW VNLIMDTFAS
LALATEPPTE ALLLRKPYGR NKPLISRTMM KNILGHGVYQ LIIIFSLLFA GEKMFDIDSG
RNAPLHAPPS EHYTIVFNTF VMMQLFNEIN ARKIHGERNV FDGIFNNPIF CSIVFGTFII
QIVIVQFGGK PFSCVSLSID QWLWCTFLGF GSLLWGQVIS SIPTSRLKFL KTAGHGTQKE
EIPDEELEEL EDMDEIDHAE RELRRGQILW FRGLNRIQTQ MDVVSAFQSG TSFQGALRRQ
ASNSSQQQHD IRVVNAFRSS ISLYEGLEKP ESRSSIHNFM THPEFRIEDS EPHIPLIDDT
DAEDDAPTKR NSASPLSPSP NQNNNAVESS NHLLPEGPKS GTPSAPGSPL HSLETSL
//