LipidDB ID

LipidDB-9606-00505

Entry Name

UniProt Accession

Q9NZU7; O95663; Q8N6H5; Q9NZU8;

Theoretical PI

8.65

Molecular Weight

39837.86

Genbank Protein ID

CAA64361.1; AAF25782.1; AAF25783.1; AAH30201.2;

Genbank Nucleotide ID

X94700; AF169148; AF169149; AC069234; BC030201;

Protein Name

Calcium-binding protein 1

Protein Synonyms/Alias

CaBP1; Calbrain; Caldendrin;

Gene Name

CABP1

Gene Synonyms/Alias

Created Date

27-APR-2001

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Few AP, Lautermilch NJ, Westenbroek RE, Scheuer T, Catterall WA. Differential regulation of CaV2.1 channels by calcium-binding protein 1 and visinin-likeprotein-2 requires N-terminal myristoylation. J Neurosci. 2005 Jul27;25(30):7071-80.[PMID:16049184]

Functional Description

Modulates calcium-dependent activity of inositol 1,4,5- triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor- induced cellular degeneration (By similarity).

Sequence Annotation

Domain: 225 260 EF-hand 1.
Domain: 261 296 EF-hand 2.
Domain: 302 337 EF-hand 3.
Domain: 339 370 EF-hand 4.
Metal binding site: 238 238 Magnesium.
Metal binding site: 240 240 Magnesium.
Metal binding site: 242 242 Magnesium.
Metal binding site: 244 244 Magnesium; via carbonyl oxygen.
Metal binding site: 315 315 Calcium 1.
Metal binding site: 317 317 Calcium 1.
Metal binding site: 319 319 Calcium 1.
Metal binding site: 321 321 Calcium 1; via carbonyl oxygen.
Metal binding site: 326 326 Calcium 1.
Metal binding site: 352 352 Calcium 2.
Metal binding site: 353 353 Calcium 2; via amide nitrogen.
Metal binding site: 354 354 Calcium 2.
Metal binding site: 356 356 Calcium 2.
Metal binding site: 357 357 Calcium 2; via amide nitrogen.
Metal binding site: 358 358 Calcium 2; via carbonyl oxygen.
Metal binding site: 360 360 Calcium 2.
Metal binding site: 363 363 Calcium 2.
Modified residue: 323 323 Phosphoserine.

Protein Length

370 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl
GO:0005829; C:cytosol; IEA:Ensembl
GO:0030425; C:dendrite; IEA:Ensembl
GO:0005615; C:extracellular space; IDA:UniProt
GO:0000139; C:Golgi membrane; IDA:MGI
GO:0043025; C:neuronal cell body; IEA:Ensembl
GO:0005634; C:nucleus; IEA:Ensembl
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:MGI
GO:0014069; C:postsynaptic density; IDA:UniProtKB
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW
GO:0043234; C:protein complex; IEA:Ensembl
GO:0005509; F:calcium ion binding; TAS:ProtInc
GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB
GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc
GO:0008139; F:nuclear localization sequence binding; ISS:UniProtKB
GO:0043086; P:negative regulation of catalytic activity; TAS:GOC
GO:0010651; P:negative regulation of cell communication by electrical coupling; IEA:Ensembl
GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB
GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IEA:Ensembl

Interpro

InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR018247; EF_Hand_1_Ca_BS
InterPro; IPR002048; EF_hand_dom

Pfam

Pfam; PF00036; EF-hand_1;

SMART

SMART; SM00054; EFh;

PROSITE

PROSITE; PS00018; EF_HAND_1;
PROSITE; PS50222; EF_HAND_2;

PRINTS