ID Q9FVE8_SOYBN Unreviewed; 1014 AA.
AC Q9FVE8;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=SCA1 {ECO:0000313|EMBL:AAG28435.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:AAG28435.1};
RN [1] {ECO:0000313|EMBL:AAG28435.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10948258; DOI=10.1105/tpc.12.8.1393;
RA Chung W.S., Lee S.H., Kim J.C., Heo W.D., Kim M.C., Park C.Y., Park H.C.,
RA Lim C.O., Kim W.B., Harper J.F., Cho M.J.;
RT "Identification of a calmodulin-regulated soybean Ca(2+)-ATPase (SCA1) that
RT is located in the plasma membrane.";
RL Plant Cell 12:1393-1407(2000).
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|ARBA:ARBA00000363,
CC 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|ARBA:ARBA00006124,
CC 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; AF195028; AAG28435.1; -; mRNA.
DR RefSeq; NP_001238485.1; NM_001251556.1.
DR AlphaFoldDB; Q9FVE8; -.
DR GeneID; 547567; -.
DR KEGG; gmx:547567; -.
DR OrthoDB; 847at2759; -.
DR BioCyc; MetaCyc:MONOMER-14661; -.
DR ExpressionAtlas; Q9FVE8; baseline and differential.
DR GO; GO:0016020; C: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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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; 1.20.5.170; -; 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; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR024750; Ca_ATPase_N_dom.
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:SF474; CALCIUM-TRANSPORTING ATPASE 1; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12515; CaATP_NAI; 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; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 2: Evidence at transcript level;
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|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 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 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 395..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 818..840
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 958..979
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 991..1009
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 113..189
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1014 AA; 110740 MW; B4A16CC78259E8D7 CRC64;
MESYLNENFE VKSKNSPEEV LQRWRRLCGI VKNPRRRFRF TANLSKRDEA AAMRRTIQEK
LRIAILVSKA ALQFIQSVQL SDYKLPEEVK DAGFQICGDE LGSIVEVHDV KKFRHHGGVD
GIAEKLSTST TEGLNSDTEL LNRRQQIYGI NKFTESAATS FWVFVWEAFQ DMTLMILGVC
AIVSLLVGIA TEGWPKGAHD GLGIVASILL VVFVTATSDY RQSLQFRDLD KEKKKISIQV
TRNGYRQKMS IYELLPGDIV HLAIGDQVPA DGLFVSGFSV LIDESSLTGE SEPVMVNSEN
PFLLSGTKVQ DGSCKMLVTS VGMRTQWGKL MATLSEGGDD ETPLQVKLNG VATIIGKIGL
FFAVVTFAVL VQGLVSLKLQ QGSLRSWTGD DALELLEFFA VAVTIVVVAV PEGLPLAVTL
SLAFAMKKMM NDKALLRHYA ACETMGSATT ICSDKTGTLT TNHMTVVKTC FCMNSKEVSN
NNASSLCSEL PEPAVKLLLE SIFNNTGGEV VVNQNGKREI LGTPTEAAIL EFGLSLGGDF
QGEKQACKLV KVEPFNSTKK KMSVVVELPG GGLRAHCKGA SEIILAACDK VLNSNGEVVP
LDEESTSHLK ATINQFASEA LRTLCLAYVE LENGFSPEDP IPVSGYTCIG VIGIKDPVRP
GVKESVAMCR SAGITVRMVT GDNINTAKAI ARECGILTDD GIAIEGPEFR EKSQEELLEL
IPKIQVMARS SPLDKHTLVK HLRTTFGEVV AVTGDGTNDA PALHEADIGL AMGIAGTEVA
KESADVIILD DNFSTIVTVA KWGRSVYINI QKFVQFQLTV NVVALIVNFT SACLTGTAPL
TAVQLLWVNM IMDTLGALAL ATEPPNDDLM KRSPVGRKGN FISNVMWRNI LGQSLYQFMV
IWFLQSRAKS IFLLEGPNSD LVLNTLIFNS FVFCQVFNEI NSREMEKINV FKGILDNYVF
VGVISATVFF QIIIVEYLGT FANTTPLTLS QWFFCLLVGF MGMPIAARLK KIPV
//
