ID W5Q292_SHEEP Unreviewed; 1222 AA.
AC W5Q292;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2B1 {ECO:0000313|Ensembl:ENSOARP00000016830.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016830.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000016830.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016830.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000016830.1}
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: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004187}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004124}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}. Presynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034107}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034107}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
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 EMBL; AMGL01079965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01079966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01079967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01079968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01079969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5Q292; -.
DR Ensembl; ENSOART00000017068.1; ENSOARP00000016830.1; ENSOARG00000015680.1.
DR HOGENOM; CLU_002360_9_0_1; -.
DR Proteomes; UP000002356; Chromosome 3.
DR Bgee; ENSOARG00000015680; Expressed in cerebellum and 55 other cell types or tissues.
DR ExpressionAtlas; W5Q292; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic 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; 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:SF245; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 1; 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 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:UP000002356};
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 934..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 971..988
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1009..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1042..1063
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 50..127
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 298..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 134799 MW; 6298C9817F683630 CRC64;
MGDMANNSVA YGGVKNSLKE ANHDGDFGIT LAELRALMEL RSTDALRKIQ ESYGDVSGIC
ARLKTSPNEV GLSGNPADIE RREAVFGKNF IPPKKPKTFL QLVWEALQDV TLIILEIAAI
VSLGLSFYQP PEGDNALCGD VSVGEEEGEG ETGWIEGAAI LLSVVCVVLV TAFNDWSKEK
QFRGLQSRIE QEQKFTVIRG GQVIQIPVAD ITVGDIAQVK YGDLLPADGI LIQGNDLKID
ESSLTGESDH VKKSLDKDPL LLSGTHVMEG SGRMVVTAVG INSQTGIIFT LLGAGGEEEE
KKDEKKKEKK NKKQDGAIEN RNKAKAQDGA AMEMQPLKSE EGGDGDEKDK KKANLPKKEK
SVLQGKLTKL AVQIGKAGLL MSAITVIILV LYFVIDTFWV QKRPWLAECT PIYIQYFVKF
FIIGVTVLVV AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT
LTMNRMTVVQ AYINEKHYKK IPDPEAIPPN ILSYLVTGIS VNCAYTSKIL PPEKEGGLPR
HVGNKTECAL LGLLLDLKRD YQDVRNEIPE EALYKVYTFN SVRKSMSTVL KNADGSYRIF
SKGASEIILK KCFKILSANG EAKVFRPRDR DDIVKTVIEP MASEGLRTIC LAFRDFPAGE
PEPEWDNEND IVTGLTCIAV VGIEDPVRPE VVPDAIKKCQ RAGITVRMVT GDNINTARAI
ATKCGILHPG EDFLCLEGKD FNRRIRNEKG EIEQERIDKI WPKLRVLARS SPTDKHTLVK
GIIDSTVSEQ RQVVAVTGDG TNDGPALKKA DVGFAMGIAG TDVAKEASDI ILTDDNFTSI
VKAVMWGRNV YDSISKFLQF QLTVNVVAVI VAFTGACITQ DSPLKAVQML WVNLIMDTLA
SLALATEPPT ESLLLRKPYG RNKPLISRTM MKNILGHAFY QLVVVFTLLF AGEKFFDIDS
GRNAPLHAPP SEHYTIVFNT FVLMQLFNEI NARKIHGERN VFEGIFNNAI FCTIVLGTFV
VQIIIVQFGG KPFSCSELSI EQWLWSIFLG MGTLLWGQLI STIPTSRLKF LKEAGHGTQK
EEIPEEELAE DVEEIDHAER ELRRGQILWF RGLNRIQTQI RVVNAFRSSL YEGLEKPESR
SSIHNFMTHP EFRIEDSEPH IPLIDDTDAE DDAPTKRNSS PPPSPNKNNN AVDSGIYLTI
EMNKSATSSS PGSPLHSLET SL
//
