Lipid Modification Database
Tag
Content
LipidDB ID
LipidDB-3702-01253
Entry Name
ACA11_ARATH
UniProt Accession
Q9M2L4
;
Theoretical PI
5.97
Molecular Weight
111944.81
Genbank Protein ID
CAB68139.1
;
AEE79642.1
;
Genbank Nucleotide ID
AL137080
;
CP002686
;
Protein Name
Putative calcium-transporting ATPase 11, plasma membrane-type
Protein Synonyms/Alias
3.6.3.8; Ca(2+)-ATPase isoform 11;
Gene Name
ACA11
Gene Synonyms/Alias
At3g57330; F28O9.180;
Created Date
11-JAN-2001
Lipid Modification Sites
Position
Sequence Form
Peptide
References
Modification Type
619
Canonical
SEALRTL
C
LVYTDLD
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
Functional Description
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell or into organelles.
Sequence Annotation
Topological domain: 1 157 Cytoplasmic.
Transmembrane: 158 178 Helical.
Topological domain: 179 196 Lumenal.
Transmembrane: 197 217 Helical.
Topological domain: 218 345 Cytoplasmic.
Transmembrane: 346 365 Helical.
Topological domain: 366 395 Lumenal.
Transmembrane: 396 413 Helical.
Topological domain: 414 801 Cytoplasmic.
Transmembrane: 802 820 Helical.
Topological domain: 821 831 Lumenal.
Transmembrane: 832 852 Helical.
Topological domain: 853 872 Cytoplasmic.
Transmembrane: 873 895 Helical.
Topological domain: 896 907 Lumenal.
Transmembrane: 908 929 Helical.
Topological domain: 930 947 Cytoplasmic.
Transmembrane: 948 969 Helical.
Topological domain: 970 979 Lumenal.
Transmembrane: 980 1001 Helical.
Topological domain: 1002 1025 Cytoplasmic.
Region: 19 30 Interaction with calmodulin.
Active site: 451 451 4-aspartylphosphate intermediate.
Metal binding site: 746 746 Magnesium.
Metal binding site: 750 750 Magnesium.
Protein Length
1025 AA.
Protein Sequence
(Canonical)
MSNLLKDFEV ASKNPSLEAR QRWRSSVGLV KNRARRFRMI SNLDKLAENE KKRCQIQEKI 60
RVVFYVQKAA FQFIDAGARP EYKLTDEVKK AGFYVEADEL ASMVRNHDTK SLTKIGGPEG 120
IAQKVSVSLA EGVRSSELHI REKIYGENRY TEKPARSFLT FVWEALQDIT LIILMVCAVV 180
SIGVGVATEG FPKGMYDGTG ILLSIILVVM VTAISDYKQS LQFRDLDREK KKIIIQVTRD 240
GSRQEVSIHD LVVGDVVHLS IGDQVPADGI FISGYNLEID ESSLSGESEP SHVNKEKPFL 300
LSGTKVQNGS AKMLVTTVGM RTEWGKLMDT LSEGGEDETP LQVKLNGVAT IIGKIGLGFA 360
VLTFVVLCIR FVVEKATAGS ITEWSSEDAL TLLDYFAIAV TIIVVAVPEG LPLAVTLSLA 420
FAMKQLMSDR ALVRHLAACE TMGSSTCICT DKTGTLTTNH MVVNKVWICE NIKERQEENF 480
QLNLSEQVKN ILIQAIFQNT GSEVVKDKEG KTQILGSPTE RAILEFGLLL GGDVDTQRRE 540
HKILKIEPFN SDKKKMSVLT SHSGGKVRAF CKGASEIVLK MCEKVVDSNG ESVPLSEEKI 600
ASISDVIEGF ASEALRTLCL VYTDLDEAPR GDLPNGGYTL VAVVGIKDPV RPGVREAVQT 660
CQAAGITVRM VTGDNISTAK AIAKECGILT AGGVAIEGSD FRNLPPHEMR AILPKIQVMA 720
RSLPLDKHTL VNNLRKMGEV VAVTGDGTND APALHEADIG LAMGIAGTEV AKENADVIIM 780
DDNFATIVNV AKWGRAVYIN IQKFVQFQLT VNVVALIINF VSACITGSAP LTAVQLLWVN 840
MIMDTLGALA LATEPPNEGL MKRQPIGRTA SFITRAMWRN IIGQSIYQLI VLGILNFAGK 900
QILNLNGPDS TIVLNTIIFN SFVFCQVFNE VNSREIEKIN VFEGMFKSWV FVAVMTATVG 960
FQVIIVEFLG AFASTVPLSW QHWLLCILIG SVSMILAVGL KCIPVESNRH HDGYELLPSG 1020
PSDSA 1025
FASTA
(Canonical)
>LipidDB-3702-01253|Q9M2L4
MSNLLKDFEVASKNPSLEARQRWRSSVGLVKNRARRFRMISNLDKLAENEKKRCQIQEKI
RVVFYVQKAAFQFIDAGARPEYKLTDEVKKAGFYVEADELASMVRNHDTKSLTKIGGPEG
IAQKVSVSLAEGVRSSELHIREKIYGENRYTEKPARSFLTFVWEALQDITLIILMVCAVV
SIGVGVATEGFPKGMYDGTGILLSIILVVMVTAISDYKQSLQFRDLDREKKKIIIQVTRD
GSRQEVSIHDLVVGDVVHLSIGDQVPADGIFISGYNLEIDESSLSGESEPSHVNKEKPFL
LSGTKVQNGSAKMLVTTVGMRTEWGKLMDTLSEGGEDETPLQVKLNGVATIIGKIGLGFA
VLTFVVLCIRFVVEKATAGSITEWSSEDALTLLDYFAIAVTIIVVAVPEGLPLAVTLSLA
FAMKQLMSDRALVRHLAACETMGSSTCICTDKTGTLTTNHMVVNKVWICENIKERQEENF
QLNLSEQVKNILIQAIFQNTGSEVVKDKEGKTQILGSPTERAILEFGLLLGGDVDTQRRE
HKILKIEPFNSDKKKMSVLTSHSGGKVRAFCKGASEIVLKMCEKVVDSNGESVPLSEEKI
ASISDVIEGFASEALRTLCLVYTDLDEAPRGDLPNGGYTLVAVVGIKDPVRPGVREAVQT
CQAAGITVRMVTGDNISTAKAIAKECGILTAGGVAIEGSDFRNLPPHEMRAILPKIQVMA
RSLPLDKHTLVNNLRKMGEVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKENADVIIM
DDNFATIVNVAKWGRAVYINIQKFVQFQLTVNVVALIINFVSACITGSAPLTAVQLLWVN
MIMDTLGALALATEPPNEGLMKRQPIGRTASFITRAMWRNIIGQSIYQLIVLGILNFAGK
QILNLNGPDSTIVLNTIIFNSFVFCQVFNEVNSREIEKINVFEGMFKSWVFVAVMTATVG
FQVIIVEFLGAFASTVPLSWQHWLLCILIGSVSMILAVGLKCIPVESNRHHDGYELLPSG
PSDSA
Gene Ontology
GO:0009507
; C:chloroplast; IDA:TAIR
GO:0005794
; C:Golgi apparatus; IDA:TAIR
GO:0016021
; C:integral component of membrane; IEA:UniProtKB-KW
GO:0009705
; C:plant-type vacuole membrane; IDA:TAIR
GO:0005886
; C:plasma membrane; IDA:TAIR
GO:0005774
; C:vacuolar membrane; IDA:TAIR
GO:0005773
; C:vacuole; IDA:TAIR
GO:0005524
; F:ATP binding; IEA:UniProtKB-KW
GO:0005388
; F:calcium-transporting ATPase activity; ISS:TAIR
GO:0046872
; F:metal ion binding; IEA:UniProtKB-KW
GO:0055081
; P:anion homeostasis; IMP:TAIR
GO:0042742
; P:defense response to bacterium; IGI:TAIR
GO:0043069
; P:negative regulation of programmed cell death; IGI:TAIR
Interpro
InterPro;
IPR006408
; ATPase_P-typ_Ca-transp_plasma
InterPro;
IPR006068
; ATPase_P-typ_cation-transptr_C
InterPro;
IPR004014
; ATPase_P-typ_cation-transptr_N
InterPro;
IPR023299
; ATPase_P-typ_cyto_domN
InterPro;
IPR018303
; ATPase_P-typ_P_site
InterPro;
IPR023298
; ATPase_P-typ_TM_dom
InterPro;
IPR008250
; ATPase_P-typ_transduc_dom_A
InterPro;
IPR024750
; Ca_ATPase_N_dom
InterPro;
IPR001757
; Cation_transp_P_typ_ATPase
InterPro;
IPR023214
; HAD-like_dom
Pfam
Pfam;
PF12515
; CaATP_NAI;
Pfam;
PF00689
; Cation_ATPase_C;
Pfam;
PF00690
; Cation_ATPase_N;
Pfam;
PF00122
; E1-E2_ATPase;
Pfam;
PF00702
; Hydrolase;
SMART
SMART;
SM00831
; Cation_ATPase_N;
PROSITE
PROSITE;
PS00154
; ATPASE_E1_E2;
PRINTS
PRINTS;
PR00119
; CATATPASE;
PRINTS;
PR00120
; HATPASE;