ID A0A022S0E9_ERYGU Unreviewed; 1178 AA.
AC A0A022S0E9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Cation-transporting ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MIMGU_mgv1a000407mg {ECO:0000313|EMBL:EYU45726.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU45726.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU45726.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR EMBL; KI630177; EYU45726.1; -; Genomic_DNA.
DR RefSeq; XP_012839401.1; XM_012983947.1.
DR AlphaFoldDB; A0A022S0E9; -.
DR STRING; 4155.A0A022S0E9; -.
DR GeneID; 105959791; -.
DR KEGG; egt:105959791; -.
DR eggNOG; KOG0209; Eukaryota.
DR OMA; QKTKYVW; -.
DR OrthoDB; 6047at2759; -.
DR PhylomeDB; A0A022S0E9; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd07543; P-type_ATPase_cation; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
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 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 982..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1133..1155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 830..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 131764 MW; 80EF50D666999C96 CRC64;
MSRFHVGGKV VDTVDLLQKR HWAWRLDMWP FTILYGVWLS AGVPSLDFGD ASIVLGCILA
FHVLVFLFTV WAVDFKCFVQ YSKVNDIHRA DACKITPAKF SGSKEVVPLH FRKLAASSTS
PDTEEIYFDF RKQRFIYSTE NHTFFKLPYP SKETIGYYLK NSGYGTEAKI LTATENWGRN
VFEYPHPTFQ KLMKEQCMEP FFVFQVFCVG LWCLDEYWYY SLFTLFMLFM FESTMAKSRL
KTLSELRRVK VDTQILMVYR CGKWNKLSGT ELLPGDVVSI GRSIASDGEE KSVPADMLIL
AGSAIVNEAI LTGESTPQWK VSVVGRRSDE KLSARRDKSH VLFGGTKILQ HTPDKTFHLK
APDGGCVAVV LRTGFETSQG KLMRTILFST ERVTANSWES GLFILFLVVF ALIAAGYVLM
KGLEDPTRSR YKLLLSCSLI ITSVIPPELP MELSIAVNTS LIALARRGIF CTEPFRIPFA
GKVDICCFDK TGTLTSDDME FTGVRGLTDS DTETEISEVP ERTLEILATC HALVFVDNKL
VGDPLEKAAL KGIDWTYKSD EKAMPKRGGA NLVQIVQRHH FASHLKRMAV VVRVQEQFFA
FVKGAPETIE ERLIDVPEWY VKTYKKHTRQ GSRVLALAYK SLQDMTVSEA RSLDRDTVES
GLTFAGFAIF NCPIREDSAS VLSGLKESSH DLVMITGDQA LTACHVAGQV NIISKPALIL
GRTKDNDGYE WVSPDETYTI SYRENEVEDL SEAHDLCISG DCIEMLQQTS STLKVIPYVK
VFARVAPEQK ELIITTFKSV GRVTLMCGDG TNDVGALKQA QVGVALLNAI PPPAQKDKSS
SEASSKNETE KSAKSKKQDN QSKTRAVSKS VSTSSNQAAN RHMTAAEIQS QKLKKMMEEM
NEDGDGRSAP VVKLGDASMA SPFTAKHASV APTTDIIRQG RSTLVTTLQM FKILGLNCLA
TAYVLSVMYL DGVKLGDVQA TISGVFTAAF FLFISHASPL PNLSAERPHP NIFCSYVLLS
LLGQFSVHIF FLISSVKEAE KYMPDVCIEP DSEFHPNLVN TVSYMVGLML QVATFAVNYM
GHPFNQSISQ NKPFRYALVA AVGFFTVITS DLFRDLNDWL RLVPMPRPLR NKIMLWAFLT
FAICYTWESF LRWAFPGKMP AWRKKQRLVA ANEEKKKV
//
