Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01078
Entry Name
UniProt Accession
Theoretical PI
6.3
Molecular Weight
100500.17
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcium-transporting ATPase type 2C member 1
Protein Synonyms/Alias
ATPase 2C1; 3.6.3.8; ATP-dependent Ca(2+) pump PMR1;
Gene Name
Atp2c1
Gene Synonyms/Alias
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
344
Canonical
IVETLGCCNVICSDK
[1]
S-Palmitoylation
889
Canonical
LGLTSSVCIVSEIIK
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Predicted from GPS-Lipid
Functional Description
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium.
Sequence Annotation
Topological domain: 1 78 Cytoplasmic.
Transmembrane: 79 95 Helical.
Topological domain: 96 99 Extracellular.
Transmembrane: 100 121 Helical.
Topological domain: 122 263 Cytoplasmic.
Transmembrane: 264 283 Helical.
Topological domain: 284 295 Extracellular.
Transmembrane: 296 317 Helical.
Topological domain: 318 700 Cytoplasmic.
Transmembrane: 701 723 Helical.
Topological domain: 724 728 Extracellular.
Transmembrane: 729 752 Helical.
Topological domain: 753 776 Cytoplasmic.
Transmembrane: 777 795 Helical.
Topological domain: 796 802 Extracellular.
Transmembrane: 803 828 Helical.
Topological domain: 829 843 Cytoplasmic.
Transmembrane: 844 863 Helical.
Topological domain: 864 876 Extracellular.
Transmembrane: 877 893 Helical.
Topological domain: 894 919 Cytoplasmic.
Active site: 350 350 4-aspartylphosphate intermediate.
Metal binding site: 644 644 Magnesium.
Metal binding site: 648 648 Magnesium.
Protein Length
919 AA.
Protein Sequence
(Canonical)
MKVARFQKIP NVENETMIPV LTSKRASELA VSEVAGLLQA DLQNGLNKSE VSHRRAFHGW  60
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVLMRQF DDAVSITVAI LIVVTVAFVQ  120
EYRSEKSLEE LSKLVPPECH CVREGKLEHT LARDLVPGDT VCLSVGDRVP ADLRLFEAVD  180
LSIDESSLTG ETTPCSKVTA PQPAATNGDL ASRSNIAFMG TLVRCGKAKG IVIGTGENSE  240
FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS FYSFGIIGII MLVGWLLGKD ILEMFTISVS  300
LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET LGCCNVICSD KTGTLTKNEM  360
TVTHILTSDG LHAEVTGVGY NQFGEVIVDG DVVHGFYNPA VSRIVEAGCV CNDAVIRNNT  420
LMGKPTEGAL IALAMKMGLD GLQQDYIRKA EYPFSSEQKW MAVKCVHRTQ QDRPEICFMK  480
GAYEQVIKYC TTYNSKGQTL ALTQQQRDLY QQEKAQMGSA GLRVLALASG PDLGQLTLLG  540
LVGIIDPPRT GVKEAVTTLI ASGVSIKMIT GDSQETAIAI ASRLGLYSKT SQSVSGEEVD  600
TMEVQHLSQI VPKVAVFYRA SPRHKMKIIK SLQKNGSVVA MTGDGVNDAV ALKAADIGVA  660
MGQTGTDVCK EAADMILVDD DFQTIMSAIE EGKGIYNNIK NFVRFQLSTS IAALTLISLA  720
TLMNFPNPLN AMQILWINII MDGPPAQSLG VEPVDKDVIR KPPRNWKDSI LTKNLILKIL  780
VSSIIIVCGT LFVFWRELRD NVITPRDTTM TFTCFVFFDM FNALSSRSQT KSVFEIGLCS  840
NKMFCYAVLG SIMGQLLVIY FPPLQKVFQT ESLSILDLLF LLGLTSSVCI VSEIIKKVER  900
SREKTQKNTT STPSSFLEV                                               919
FASTA
(Canonical)
>LipidDB-10116-01078|Q64566
MKVARFQKIPNVENETMIPVLTSKRASELAVSEVAGLLQADLQNGLNKSEVSHRRAFHGW
NEFDISEDEPLWKKYISQFKNPLIMLLLASAVISVLMRQFDDAVSITVAILIVVTVAFVQ
EYRSEKSLEELSKLVPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVD
LSIDESSLTGETTPCSKVTAPQPAATNGDLASRSNIAFMGTLVRCGKAKGIVIGTGENSE
FGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVS
LAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEM
TVTHILTSDGLHAEVTGVGYNQFGEVIVDGDVVHGFYNPAVSRIVEAGCVCNDAVIRNNT
LMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMK
GAYEQVIKYCTTYNSKGQTLALTQQQRDLYQQEKAQMGSAGLRVLALASGPDLGQLTLLG
LVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAIAIASRLGLYSKTSQSVSGEEVD
TMEVQHLSQIVPKVAVFYRASPRHKMKIIKSLQKNGSVVAMTGDGVNDAVALKAADIGVA
MGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLA
TLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKIL
VSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCS
NKMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVSEIIKKVER
SREKTQKNTTSTPSSFLEV
Gene Ontology
GO:0005794; C:Golgi apparatus; ISS:UniProtKB
GO:0000139; C:Golgi membrane; ISS:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD
GO:0005886; C:plasma membrane; IDA:RGD
GO:0030141; C:secretory granule; IDA:RGD
GO:0005802; C:trans-Golgi network; ISS:UniProtKB
GO:0030133; C:transport vesicle; IDA:RGD
GO:0005524; F:ATP binding; ISS:UniProtKB
GO:0005509; F:calcium ion binding; ISS:UniProtKB
GO:0005388; F:calcium-transporting ATPase activity; ISS:UniProtKB
GO:0030145; F:manganese ion binding; ISS:UniProtKB
GO:0015410; F:manganese-transporting ATPase activity; ISS:UniProtKB
GO:0004871; F:signal transducer activity; ISS:UniProtKB
GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB
GO:0070509; P:calcium ion import; IC:RGD
GO:0070588; P:calcium ion transmembrane transport; IDA:GOC
GO:0006816; P:calcium ion transport; ISS:UniProtKB
GO:0016339; P:calcium-dependent cell-cell adhesion; ISS:UniProtKB
GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB
GO:0030026; P:cellular manganese ion homeostasis; ISS:UniProtKB
GO:0008544; P:epidermis development; ISS:UniProtKB
GO:0032468; P:Golgi calcium ion homeostasis; ISS:UniProtKB
GO:0032472; P:Golgi calcium ion transport; ISS:UniProtKB
GO:0071421; P:manganese ion transmembrane transport; ISS:GOC
GO:0006828; P:manganese ion transport; ISS:UniProtKB
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB
GO:0007165; P:signal transduction; ISS:GOC
Interpro
InterPro; IPR006413; ATPase_P-typ_Ca-transp_PMR1
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; IPR001757; Cation_transp_P_typ_ATPase
InterPro; IPR023214; HAD-like_dom
Pfam
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;