ID A0A6J3QS35_TURTR Unreviewed; 1172 AA.
AC A0A6J3QS35;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2B3 {ECO:0000313|RefSeq:XP_033705325.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033705325.1};
RN [1] {ECO:0000313|RefSeq:XP_033705325.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033705325.1};
RG RefSeq;
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: 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. 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}.
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DR RefSeq; XP_033705325.1; XM_033849434.1.
DR AlphaFoldDB; A0A6J3QS35; -.
DR Proteomes; UP000245320; Chromosome X.
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; 3.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF284; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 3; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000245320};
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 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 416..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 932..950
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 970..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 999..1024
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1036..1057
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 50..126
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 299..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1075..1102
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 336..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 128463 MW; F68F9B595B63412B CRC64;
MGDVANSSVE FHPKPRQQRE APHAGGFGCT LAELRSLMEL RGAEALQKVQ ETYGDVGGLC
RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAIV
SLGLSFYAPP GEESEACGNV SAGAEDEGEA EAGWIEGAAI LLSVICVVLV TAFNDWSKEK
QFRGLQSRIE QEQKFTVIRN GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQGNDLKID
ESSLTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEK
KEKKGKQQDG AMESSQTKAK KQDGAVAMEM QPLKSAEGGE TEEREKKKAN VPKKEKSVLQ
GKLTKLAVQI GKAGLVMSAV TVIILALYFV IETFVVEGRA WLAECTPVYV QYFVKFFIIG
VTVLVVAVPE GLPLAVTISL AYSVKKMMRD NNLVRHLDAC ETMGNATAIC SDKTGTLTTN
RMTVVQSYLG DTHYKEVPAP SALTPKILDL LVHAISINSA YTTKILPPEK EGALPRQVGN
KTECALLGFV LDLKQDFQPV REQIPEDKLY KVYTFNSVRK SMSTVIRMPD SGFRLFSKGA
SEILLKKCTN ILNSNGELRS FRPRDRDDMV QKIIEPMACD GLRTICIAYR DFSAAQEPDW
DNENEVVGDL TCIAVVGIED PVRPEVPEAI RKCQRAGITV RMVTGDNINT ARAIAAKCGI
IQPGEDFLCL EGKEFNRRIR NEKGEIEQER LDKVWPKLRV LARSSPTDKH TLVKGIIDSN
TGEQRQVVAV TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN FTSIVKAVMW
GRNVYDSISK FLQFQLTVNV VAVIVAFTGA CITQDSPLKA VQMLWVNLIM DTFASLALAT
EPPTESLLLR KPYGRDKPLI SRTMMKNILG HAAYQLTTIF TLLFVGELFF DIDSGRNAPL
HSPPSEHYTI IFNTFVMMQL FNEINARKIH GERNVFHGIF GNPIFCTIVL GTFVIQIVIV
QFGGKPFSCS PLSTEQWLWC LFVGVGELVW GQVIATIPTS QLKCLKEAGH GPGKDEMTDE
ELAEGEEEID HAERELRRGQ ILWFRGLNRI QTQMEVVSTF KRSGSFQGAV RRRSSVLSQL
HDVTNLSTPT HVILSAANPT SAAGNPGGES IP
//
