ID A0A669B5J7_ORENI Unreviewed; 1257 AA.
AC A0A669B5J7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=atp2b2 {ECO:0000313|Ensembl:ENSONIP00000029748.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000029748.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000029748.1}
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: 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_013132528.1; XM_013277074.2.
DR AlphaFoldDB; A0A669B5J7; -.
DR Ensembl; ENSONIT00000037388.1; ENSONIP00000029748.1; ENSONIG00000014357.2.
DR GeneID; 100690326; -.
DR KEGG; onl:100690326; -.
DR CTD; 491; -.
DR GeneTree; ENSGT00940000166500; -.
DR InParanoid; A0A669B5J7; -.
DR OMA; IQHCKRA; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000005207; Linkage group LG5.
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:SF377; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 2; 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 PRINTS; PR00121; NAKATPASE.
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 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:UP000005207};
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 414..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 457..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 892..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 969..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1007..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1077..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 49..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 298..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 138160 MW; 0FAC73441F1701B9 CRC64;
MGDMSNSDFY AKNQRNEGNH AAAFGCSVME LRSLMELRGT EAVVKLQEDY GGVEGLCKRL
KTSPTEGLAG AQTDLDKRKE IFGKNLIPPK KPKTFLQLVW EALQDVTLII LEIAALISLG
LSFYHPPGET GGESCGAAAG GVEDEGEADA GWIEGAAILL SVVCVVLVTA FNDWSKEKQF
RGLQSRIEQE QKFQVVRGSQ VIQLPVADIV VGDIAQIKYG DLLPADGVLI QGNDLKIDES
SLTGESDHVK KSADKDPMLL SGTHVMEGSG RMVVTAVGVN SQTGIIFTLL GAGVEEEEKK
EKKGGAVEDG HQNTDCSHPP IHPIATIATD GAAGINAPGS ASLINGKMQD GNMESNQIKV
KKQDGAAAME MQPLKSAEGG EADEKERKKV SAPKKEKSVL QGKLTKLAVQ IGKAGLLMSA
ITVIILVLYF AIDNFVMQKH PWMPECTPIY IQYFVKFFII GVTVLVVAVP EGLPLAVTIS
LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT NRMTAVQLYV GDVHYKEIPD
PGVLPPKSLD LLVNAISINS AYTTKILPPD KEGGLPKQVG NKTECGLLGL VLELKRDYQP
IRNQIPEEKL YKVYTFNSVR KSMSTVIKLP DGSFRMYSKG ASEIVLKKCS HILNEVGEPR
VFRPRDKDEM VKKVIEPMAC DGLRTICVAY RDFSSNPEPN WDDENNILND LTAICVVGIE
DPVRPEVPDA IQKCQRAGIT VRMVTGDNIN TARAIAIKCG IIHPGEDFLC IDGKEFNRRI
RNEKGEVEQE RIDKVWPKLR VLARSSPTDK HTLVKGIIDS TMADQRQVVA VTGDGTNDGP
ALKKADVGFA MGIAGTDVAK EASDIILTDD NFSSIVKAVM WGRNVYDSIS KFLQFQLTVN
VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA TEPPTESLLK RKPYGRNKPL
ISSTMTKNIL GHGVYQLIII FTLLFVGEQI FDIDSGRNAP LHSPPSEHYT IIFNTFVMMQ
LFNEINARKI HGERNVFDGI FRNPIFCSIV FGTFAVQIVI VQFGGKPFSC QPLDLEKWMW
CVFLGLGELV WGQVIATIPN SRLRFLRRAG QLTQKDELPE EDVNEENEEI DHAERELRRG
QILWFRGLNR IQTQIRVVNA FRSSLYEGLE KPDSRTSIHN FMTHPEFRIE DSTPNIPLID
DTDDDSARRR MKYSSQPSSP NKNNNAIDSG INLTIDTSKS AASSSPASPL HSLETSL
//
