ID A0A5N5JM08_9ROSI Unreviewed; 1004 AA.
AC A0A5N5JM08;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN ORFNames=DKX38_024588 {ECO:0000313|EMBL:KAB5520269.1};
OS Salix brachista.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Salix.
OX NCBI_TaxID=2182728 {ECO:0000313|EMBL:KAB5520269.1, ECO:0000313|Proteomes:UP000326939};
RN [1] {ECO:0000313|Proteomes:UP000326939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. br00 {ECO:0000313|Proteomes:UP000326939};
RX PubMed=31307060; DOI=10.1093/gigascience/giz085;
RA Yang J., Wariss H.M., Tao L., Zhang R., Yun Q., Hollingsworth P., Dao Z.,
RA Luo G., Guo H., Ma Y., Sun W.;
RT "De novo genome assembly of the endangered Acer yangbiense, a plant species
RT with extremely small populations endemic to Yunnan Province, China.";
RL Gigascience 8:0-0(2019).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB5520269.1}.
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DR EMBL; VDCV01000016; KAB5520269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5JM08; -.
DR Proteomes; UP000326939; Chromosome 16.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR FunFam; 3.40.1110.10:FF:000021; calcium-transporting ATPase, endoplasmic reticulum-type; 1.
DR FunFam; 2.70.150.10:FF:000014; Calcium-transporting ATPase, putative; 1.
DR FunFam; 1.20.1110.10:FF:000077; ECA1 (ER-TYPE CA2+-ATPASE 1); 1.
DR FunFam; 1.20.1110.10:FF:000065; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 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; 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; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000326939};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 928..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 952..975
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..101
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 110480 MW; 0C39A9AFDDFF11A5 CRC64;
MGKGGEDRGK KEKNGIESRN QDNDTFPAWA KDVKECEEKY EVNREVGLSE ADVEKRREIY
GYNELEKHEG VSIFKLILDQ FNDTLVRILL AAAVISFVLA WYDGDEGGEM EITAFVEPLV
IFLILIVNAI VGVWQESNAE KALEALKEIQ SQHATVIRNG KKFSSLPARE LVPGDIVELR
VGDKVPADMR VLHLISSTLR VEQGSLTGES EAVSKTVKAV AEDTDIQGKK CMVFAGTTVV
NGNCICLVME TGMNTEIGKV HSQIHEAAQN EEDTPLKKKL NEFGEVLTML IGIICAVVWL
INVKYFLTWE YVDGWPKNFK FSFEKCTYYF EIAVALAVAA IPEGLPAVIT TCLALGTRKM
AQKNALVRKL PSVETLGCTT VICSDKTGTL TTNQMAVSKL VAMGSRAGTL RAFNVEGTTY
SPFDGEIKDW PVGRMDSNLQ MIAKIAAVCN DADVEQSGNH YVAGGMPTEA ALKVMVEKMG
FPGEHHTESS LGCGDVLACC QKWNKMEQRI ATLEFDRDRK SMGVIVNSIS NKKSLLVKGA
VENLLDRSTS IQLLDGSVVA LDQYSKDLIL HGLHEMSTSA LRCLGFAYKE ALSDFETYNG
DEDHPAHQLL LEPRNYSSIE NNLTFVGLVG LRDPPRKEVR QAIEDCRAAG IRVIVITGDN
KNTAEAICHE IGVFGPYDDI SSQSLTGKEF MDHRDVNSNV NSVLKAISDV KLSSNNAEIA
NWKVTVIFLI LVSWYMISSN IGEVASIFLT AALGIPEGMI PVQLLWVNLV TDGPPATALG
FNPPDGDVMK KPPRRSDDSL INTWILFRYL VIGLYVGIAT VGVFIIWYTS HTFMGIDLSG
DGHSLVTYSQ LANWGQCGSW KDFSVSPFTA GSQVFNFDAN PCEYFQSGKI KASTLSLSVL
VSIEMFNSLN ALSEDCSLLR MPPWVNPWLL IAMSISFGLH ALILYVPFLA QVFGIVPLSF
NEWLLVLAVA LPVILIDEVL KFAGRCTNGL RQSNSTRQSK RKAE
//
