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O88751 (CABP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-binding protein 1

Short name=CaBP1
Alternative name(s):
Caldendrin
Gene names
Name:Cabp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Prevents NMDA receptor-induced cellular degeneration. Ref.5

Subunit structure

Interacts ITPR1, ITPR2 and ITPR3. The strength of this interaction inversely correlates with calcium concentration. Interacts with CACNA1A (via C-terminal CDB motif) in the pre- and postsynaptic membranes. Interacts with CACNA1C. Interacts with CACNA1D By similarity. Interacts (via EF-hands 1 and 2) at microtubules with MAP1LC3B. Interacts (via EF-hands 1 and 2) with NSMF (via the central NLS-containing motif region), the interaction occurs in a calcium dependent manner after synaptic NMDA receptor stimulation and prevents nuclear import of NSMF. Interacts with MYO1C and TRPC5 By similarity. Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Occurs in both the cytoplasmic and cytoskeletal compartment of cell somata and dendrites. Ref.6

Tissue specificity

Somatodendritic compartment of neurons. Restricted expression in retina to a subpopulation of amacrine, bipolar, and ganglion cells. According to Ref.2, expression is heterogeneous within brain regions and their major cell types and does not match with those of marker proteins for characterized neuronal subpopulations. Ref.2

Developmental stage

Its expression is regulated differentially in retinal cell types during development.

Domain

EF-1 binds magnesium constitutively under physiological conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds neither calcium nor magnesium By similarity.

Post-translational modification

Phosphorylated. The phosphorylation regulates the activity By similarity. Ref.1

Sequence similarities

Contains 4 EF-hand domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmulticellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell communication by electrical coupling

Inferred from direct assay PubMed 17960496. Source: RGD

negative regulation of protein import into nucleus

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of voltage-gated calcium channel activity

Inferred from direct assay PubMed 17960496. Source: RGD

regulation of synaptic plasticity

Non-traceable author statement Ref.5. Source: RGD

regulation of voltage-gated calcium channel activity

Inferred from direct assay PubMed 17224447. Source: RGD

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 15140941. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 20236386. Source: RGD

cytoskeleton

Inferred from direct assay Ref.1. Source: RGD

cytosol

Inferred from direct assay PubMed 17960496PubMed 20236386. Source: RGD

dendrite

Inferred from direct assay PubMed 15140941. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 15140941. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15140941. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17960496. Source: RGD

plasma membrane

Inferred from direct assay PubMed 17960496. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 15140941. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 17224447. Source: RGD

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.1. Source: RGD

calcium-dependent protein binding

Inferred from direct assay Ref.7. Source: UniProtKB

ion channel binding

Inferred from physical interaction PubMed 17224447. Source: RGD

nuclear localization sequence binding

Inferred from direct assay Ref.7. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 17224447PubMed 21855531. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 20236386. Source: RGD

type 3 metabotropic glutamate receptor binding

Inferred from physical interaction PubMed 21855531. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O88751-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform expressed in the brain.
Isoform 2 (identifier: O88751-2)

Also known as: Caldendrin-S1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: MSSHIAKSES...RPMLSSAFGQ → MGNCVKSPLRNLSRK
Note: Minor isoform expressed in the brain, in the granule cell layer of the cerebellum, at low level. Not developmentally regulated.
Isoform 3 (identifier: O88751-3)

Also known as: Caldendrin-S2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: MSSHIAKSES...RPMLSSAFGQ → MGNCVKSPLR...RKGFAENRQP
Note: Minor isoform expressed in the brain, in the granule cell layer of the cerebellum, at low level. Not developmentally regulated.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Calcium-binding protein 1
PRO_0000073515

Regions

Domain153 – 18836EF-hand 1
Domain189 – 22436EF-hand 2
Domain230 – 26536EF-hand 3
Domain267 – 29832EF-hand 4
Calcium binding166 – 177121 Potential
Calcium binding243 – 254122 Potential
Calcium binding280 – 291123 Potential

Sites

Metal binding1661Magnesium By similarity
Metal binding1681Magnesium By similarity
Metal binding1701Magnesium By similarity
Metal binding1721Magnesium; via carbonyl oxygen By similarity
Metal binding2431Calcium 1 By similarity
Metal binding2451Calcium 1 By similarity
Metal binding2471Calcium 1 By similarity
Metal binding2491Calcium 1; via carbonyl oxygen By similarity
Metal binding2541Calcium 1 By similarity
Metal binding2801Calcium 2 By similarity
Metal binding2811Calcium 2; via amide nitrogen By similarity
Metal binding2821Calcium 2 By similarity
Metal binding2841Calcium 2 By similarity
Metal binding2851Calcium 2; via amide nitrogen By similarity
Metal binding2861Calcium 2; via carbonyl oxygen By similarity
Metal binding2881Calcium 2 By similarity
Metal binding2911Calcium 2 By similarity

Amino acid modifications

Modified residue2511Phosphoserine By similarity

Natural variations

Alternative sequence1 – 146146MSSHI…SAFGQ → MGNCVKSPLRNLSRK in isoform 2.
VSP_026157
Alternative sequence1 – 146146MSSHI…SAFGQ → MGNCVKSPLRNLSRKMRQEE KTSYMAVQTSEDGLADGGEL PGPLMMLAQNCAVMHNLLGP ACIFLRKGFAENRQP in isoform 3.
VSP_026158

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 8A9B74CD6B9F6875

FASTA29833,017
        10         20         30         40         50         60 
MSSHIAKSES KTSLLKAAAA SGGSRAPRHS SARDPGLRGR RLPGPCPDSP ATCGDPSSRR 

        70         80         90        100        110        120 
PLCRPVPRDE GARGSRRGLP QAHCRPRETL PPARGRDGEE RGLAPALSLR GSLRSRGRGD 

       130        140        150        160        170        180 
PAPAGTPEAD PFLHQLRPML SSAFGQDRSL RPEEIEELRE AFREFDKDKD GYINCRDLGN 

       190        200        210        220        230        240 
CMRTMGYMPT EMELIELSQQ INMNLGGHVD FDDFVELMGP KLLAETADMI GVKELRDAFR 

       250        260        270        280        290 
EFDTNGDGEI STSELREAMR KLLGHQVGHR DIEEIIRDVD LNGDGRVDFE EFVRMMSR 

« Hide

Isoform 2 (Caldendrin-S1) [UniParc].

Checksum: 3C65D1F2C4338AF3
Show »

FASTA16719,354
Isoform 3 (Caldendrin-S2) [UniParc].

Checksum: C0BCC66C8FF0C88F
Show »

FASTA22725,903

References

[1]"Caldendrin, a novel neuronal calcium-binding protein confined to the somato-dendritic compartment."
Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M., Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.
J. Biol. Chem. 273:21324-21331(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
Strain: Sprague-Dawley.
[2]"The neuron-specific Ca2+-binding protein caldendrin: gene structure, splice isoforms, and expression in the rat central nervous system."
Laube G., Seidenbecher C.I., Richter K., Dieterich D.C., Hoffmann B., Landwehr M., Smalla K.H., Winter C., Boeckers T.M., Wolf G., Gundelfinger E.D., Kreutz M.R.
Mol. Cell. Neurosci. 19:459-475(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
Tissue: Brain.
[3]Seidenbecher C.I.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 290-291.
[4]"Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels."
Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F., Foskett J.K.
Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITPR1; ITPR2 AND ITPR3.
[5]"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1."
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A.
Nat. Neurosci. 5:210-217(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CACNA1A.
[6]"Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an association with the microtubule cytoskeleton highlighting exclusive binding partners for neuronal Ca(2+)-sensor proteins."
Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M., Gundelfinger E.D., Kreutz M.R.
J. Mol. Biol. 336:957-970(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3B, SUBCELLULAR LOCATION.
[7]"Caldendrin-Jacob: a protein liaison that couples NMDA receptor signalling to the nucleus."
Dieterich D.C., Karpova A., Mikhaylova M., Zdobnova I., Konig I., Landwehr M., Kreutz M., Smalla K.H., Richter K., Landgraf P., Reissner C., Boeckers T.M., Zuschratter W., Spilker C., Seidenbecher C.I., Garner C.C., Gundelfinger E.D., Kreutz M.R.
PLoS Biol. 6:E34-E34(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NSMF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y17048 mRNA. Translation: CAD20347.1.
AJ315761 mRNA. Translation: CAC43037.1.
AJ315657 mRNA. Translation: CAC42417.1.
RefSeqNP_001028847.1. NM_001033675.1.
NP_001028848.1. NM_001033676.1.
NP_598213.1. NM_133529.2.
UniGeneRn.23560.

3D structure databases

ProteinModelPortalO88751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO88751. 1 interaction.

Proteomic databases

PaxDbO88751.
PRIDEO88751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001551; ENSRNOP00000001551; ENSRNOG00000001173. [O88751-1]
ENSRNOT00000001552; ENSRNOP00000001552; ENSRNOG00000001173. [O88751-3]
ENSRNOT00000039281; ENSRNOP00000033685; ENSRNOG00000001173. [O88751-2]
GeneID171051.
KEGGrno:171051.
UCSCRGD:620385. rat. [O88751-1]

Organism-specific databases

CTD9478.
RGD620385. Cabp1.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00740000114946.
HOGENOMHOG000233018.
HOVERGENHBG012180.
InParanoidO88751.
OMAMRQEEKT.
OrthoDBEOG7XM303.
PhylomeDBO88751.

Gene expression databases

ArrayExpressO88751.
GenevestigatorO88751.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR015754. Ca_binding_pro.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERPTHR23050:SF21. PTHR23050:SF21. 1 hit.
PfamPF00036. EF-hand_1. 3 hits.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio621595.

Entry information

Entry nameCABP1_RAT
AccessionPrimary (citable) accession number: O88751
Secondary accession number(s): Q711K8, Q91WZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families