ID U3IES5_ANAPP Unreviewed; 1256 AA.
AC U3IES5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 72.
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:ENSAPLP00000005747.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000005747.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000005747.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000005747.2}
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: 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 AlphaFoldDB; U3IES5; -.
DR Ensembl; ENSAPLT00000006379.2; ENSAPLP00000005747.2; ENSAPLG00000006083.2.
DR GeneTree; ENSGT00940000161461; -.
DR HOGENOM; CLU_002360_9_0_1; -.
DR Proteomes; UP000016666; Chromosome 13.
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:UP000016666};
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 415..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 456..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 891..912
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 968..986
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1006..1024
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1076..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 47..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 295..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 138276 MW; DBDB361C0ECB9B2A CRC64;
MGDMTNSDFY SKNQRNEANH AGEFGCTLQE LRSLMELRGT EAVVKIKETY GETEGLCRHL
KTSPTEGLAG TAADLEKRKL IFGKNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
LSFYQPPGEG NEGCGTATGG AEDEGEAEAG WIEGAAILLS VICVVLVTAF NDWSKEKQFR
GLQSRIEQEQ KFTVVRGGQV IQIPVAEIVV GDIAQVKYGD LLPADGIFIQ GNDLKIDESS
LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MLVTAVGVNS QTGIIFTLLG AGGEEEEKKD
KKGVKQDDGH QLPDSSHPSS HPPSATDGAA GANATDNANA SLVNGKMQDG NMENSQNKAK
QQDGAAAMEM QPLKSAEGGE GDDKDKKKSN MHKKEKSVLQ GKLTKLAVQI GKAGLVMSAI
TVIILVLYFA IDTFVVKKKQ WLPECTPVYV QYFVKFFIIG VTVLVVAVPE GLPLAVTISL
AYSVKKMMKD NNLVRHLDAC ETMGNATAIC SDKTGTLTTN RMTVVQAYVG DVHYKEIPDP
DSVPAKTLEL LVNAIAINSA YTTKILPPEK EGGLPRQVGN KTECGLLGFV LDLKQDYEPV
RNLIPEEKLY KVYTFNSVRK SMSTVIKMPD GSFRMYSKGA SEIVLKKCSR ILNAAGEPRV
FRPRDRDEMV KKVIEPMACD GLRTICVAFR DFNSSPEPDW DNENDILSDL TCICVVGIED
PVRPEVPEAI RKCQRAGITV RMVTGDNINT ARAIAIKCGI IHPGEDFLCL EGKEFNRRIR
NEKGEIEQER IDKIWPKLRV LARSSPTDKH TLVKGIIDST QVEQRQVVAV TGDGTNDGPA
LKKADVGFAM GIAGTDVAKE ASDIILTDDN FSSIVKAVMW GRNVYDSISK FLQFQLTVNI
VAVIVAFTGA CITQDSPLKA VQMLWVNLIM DTFASLALAT EPPTEALLLR KPYGRNKPLI
SRTMMKNILG HAVYQLTLIF TLLFVGEKMF KIDSGRNAPL HSPPSEHYTI IFNTFVMMQL
FNEINARKIH GERNVFDGIF RNPIFCTIVL GTFAIQIVIV QFGGKPFSCS PLQLDQWMWC
VFIGLGELVW GQVIATIPTS RLKFLKEAGR LTEKEEVPEE ELNEDVEEID HAERELRRGQ
ILWFRGLNRI QTQIRVVKAF RSSLYEGLEK PESRTSIHNF MTHPEFRIED SQPHIPLIDD
TDLEEDSALK KNSSPPSSLN KNNSAIDSGI NLTTDTSKSA TSSSPGSPIH SLETSL
//
