ID A0A0L9T6J0_PHAAN Unreviewed; 1056 AA.
AC A0A0L9T6J0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Calcium-transporting ATPase {ECO:0000313|EMBL:KAG2380174.1};
GN ORFNames=HKW66_Vig0169530 {ECO:0000313|EMBL:KAG2380174.1},
GN LR48_Vigan181s000700 {ECO:0000313|EMBL:KOM25729.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM25729.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM25729.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM25729.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2380174.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2380174.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JABFOF010000009; KAG2380174.1; -; Genomic_DNA.
DR EMBL; KQ258286; KOM25729.1; -; Genomic_DNA.
DR RefSeq; XP_017405823.1; XM_017550334.1.
DR RefSeq; XP_017405824.1; XM_017550335.1.
DR RefSeq; XP_017405825.1; XM_017550336.1.
DR STRING; 3914.A0A0L9T6J0; -.
DR EnsemblPlants; KOM25729; KOM25729; LR48_Vigan181s000700.
DR GeneID; 108319262; -.
DR Gramene; KOM25729; KOM25729; LR48_Vigan181s000700.
DR KEGG; var:108319262; -.
DR OMA; GIVDWGC; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000053144; Unassembled WGS sequence.
DR Proteomes; UP000743370; Unassembled WGS sequence.
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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02083; P-type_ATPase_SERCA; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF102; CALCIUM-TRANSPORTING ATPASE 2, ENDOPLASMIC RETICULUM-TYPE; 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; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..85
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1056 AA; 116623 MW; F35557257E56EC30 CRC64;
MKVPMEEKPF PAWSWSVEQC LKEYGVKLDK GLSTHEVQKR REKYGWNELA KEKGKPLWEL
VLEQFDDMLV KILLAAAFLS FLLAYFHGSD SGKSGFDAYV EPLVIILILV LNAIVGVWQE
NNAEKALEAL KELQSESGKV LRDGYFVPDL PARELIPGDI VELHVGDKVP ADMRVAALKT
STLRVEQSSL TGEAMPVLKG TSPVFLEDCE LQAKENMVFA GTTVVNGSCV CIVITTGMDT
EIGKIQKQIH EASQEDSDTP LKKKLDEFGN RLTTAIGLVC LIVWAINYKN FISWDVVDGW
PSNVKFSFQK CTYYFKIAVA LAVAAIPEGL PAVITTCLAL GTRKMAQKNA IVRKLPSVET
LGCTTVICSD KTGTLTTNQM AVTQFFTLGG KTTASRLISV EGTTYDPKDG GIVDWGCYNM
DANLQVMAEI CAVCNDAGIY FDGRLFRATG LPTEAALKVL VEKMGVPDVK SRSKTCDNAQ
LAASNLMDVN TVVKLGCCEW WNKRSKRVAT LEFDRIRKSM SVIVREPNGQ NRLLVKGAVE
SLLERSSHVQ LADGSLVPID NQCRELLLQR LQEMSSKGLR CLGFSYKDEL GEFSDYYADT
HPAHKKLLDP TYYSSIESDL IFVGIVGLRD PPREEVHKAI EDCKEAGIRV MVITGDNKST
AEAICREIRL FSEDEDLKGQ SLTGKEFITL PRSEQVKILL RPGGKVFSRA EPRHKQEIVR
LLKEMGEIVA MTGDGVNDAP ALKLADIGIA MGIAGTEVAK EASDMVLADD NFSTIVSAVA
EGRSIYNNMK SFIRYMISSN VGEVISIFLT AALGIPECMI PVQLLWVNLV TDGPPATALG
FNPADVDIMQ KPPRRSDDAL ISSWVLFRYL VIGSYVGLAT VGIFVLWYTQ ASFLGINLVS
DGHTIIEFSQ LRNWGECPSW SNFTVAPFNV GGGRLITFSN PCDYFSVGKV KAMTLSLSVL
VAIEMFNSLN ALSEDNSLRK LPPWRNPWLL VAMSISFGLH CLILYTPFLA EVFGVIPLTF
NEWFMVLLIS APVILIDEIL KLVARSQRRL TKEKKA
//
