Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calcium-binding protein 4

Gene

Cabp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in normal synaptic function through regulation of Ca2+ influx and neurotransmitter release in photoreceptor synaptic terminals and in auditory transmission. Modulator of CACNA1D and CACNA1F, suppressing the calcium-dependent inactivation and shifting the activation range to more hyperpolarized voltages.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi138 – 149121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi215 – 226122PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi252 – 263123PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • photoreceptor cell morphogenesis Source: MGI
  • phototransduction Source: MGI
  • retinal bipolar neuron differentiation Source: MGI
  • retinal cone cell development Source: MGI
  • visual perception Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-binding protein 4
Short name:
CaBP4
Gene namesi
Name:Cabp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1920910. Cabp4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371S → A: Decreased phosphorylation. 1 Publication
Mutagenesisi46 – 461S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi50 – 512SS → AA: No effect on phosphorylation. 1 Publication
Mutagenesisi149 – 1491E → Q: Loss of calcium binding; when associated with Q-226 and Q-263. 1 Publication
Mutagenesisi223 – 2231T → A: No effect on phosphorylation. 1 Publication
Mutagenesisi226 – 2261E → Q: Loss of calcium binding; when associated with Q-149 and Q-263. 1 Publication
Mutagenesisi263 – 2631E → Q: Loss of calcium binding; when associated with Q-149 and Q-226. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Calcium-binding protein 4PRO_0000073522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Phosphoserine; by PKC/PRKCZ1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation levels change with the light conditions and regulate the activity, but has no effect on calcium binding.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8VHC5.
PRIDEiQ8VHC5.

PTM databases

iPTMnetiQ8VHC5.
PhosphoSiteiQ8VHC5.

Expressioni

Tissue specificityi

Expressed in retina and in the inner hair cells (IHC) of the cochlea.4 Publications

Gene expression databases

BgeeiQ8VHC5.
CleanExiMM_CABP4.
GenevisibleiQ8VHC5. MM.

Interactioni

Subunit structurei

Interacts with CACNA1F and CACNA1D (via IQ domain) in a calcium independent manner. Interacts (via N-terminus) with UNC119.4 Publications

Protein-protein interaction databases

DIPiDIP-60739N.
STRINGi10090.ENSMUSP00000025761.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi124 – 13714Combined sources
Helixi148 – 1503Combined sources
Helixi151 – 1555Combined sources
Turni156 – 1583Combined sources
Helixi164 – 1718Combined sources
Beta strandi174 – 1774Combined sources
Helixi183 – 1908Combined sources
Helixi204 – 21411Combined sources
Helixi224 – 2307Combined sources
Turni233 – 2353Combined sources
Helixi242 – 25110Combined sources
Beta strandi256 – 2594Combined sources
Helixi261 – 2688Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M28NMR-A101-271[»]
2M29NMR-A101-271[»]
ProteinModelPortaliQ8VHC5.
SMRiQ8VHC5. Positions 119-271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 16036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini161 – 19636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini202 – 23736EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini239 – 27133EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ8VHC5.
OMAiRELGDCM.
OrthoDBiEOG7XM303.
PhylomeDBiQ8VHC5.
TreeFamiTF334804.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR033014. CABP4.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERiPTHR23050:SF196. PTHR23050:SF196. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VHC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEHNVQLV PGSQKIPKGV VSPRSAAEGP ALTRRRSKKE SWHPGSQKAS
60 70 80 90 100
SGDQSSSQGS EASGSSKHPP RTKVGQEEPS SAPARPASHR HSHRHRSDPQ
110 120 130 140 150
QDAAQRTYGP LLNRMFGKDR ELGPEELEEL QAAFEEFDTD QDGYIGYREL
160 170 180 190 200
GDCMRTLGYM PTEMELLEVS QHVKMRMGGF VDFEEFVELI SPKLREETAH
210 220 230 240 250
MLGVRELRIA FREFDKDRDG RITVAELRQA APALLGEPLE GTELDEMLRE
260 270
MDLNGDGTID FDEFVMMLST G
Length:271
Mass (Da):30,268
Last modified:March 1, 2002 - v1
Checksum:i3B6C7883C3DB8C1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY039218 mRNA. Translation: AAK83463.1.
BC049263 mRNA. Translation: AAH49263.1.
CCDSiCCDS29416.1.
RefSeqiNP_653115.1. NM_144532.2.
UniGeneiMm.379226.

Genome annotation databases

EnsembliENSMUST00000025761; ENSMUSP00000025761; ENSMUSG00000024842.
ENSMUST00000181080; ENSMUSP00000137950; ENSMUSG00000097687.
GeneIDi73660.
KEGGimmu:73660.
UCSCiuc008fyw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY039218 mRNA. Translation: AAK83463.1.
BC049263 mRNA. Translation: AAH49263.1.
CCDSiCCDS29416.1.
RefSeqiNP_653115.1. NM_144532.2.
UniGeneiMm.379226.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M28NMR-A101-271[»]
2M29NMR-A101-271[»]
ProteinModelPortaliQ8VHC5.
SMRiQ8VHC5. Positions 119-271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60739N.
STRINGi10090.ENSMUSP00000025761.

PTM databases

iPTMnetiQ8VHC5.
PhosphoSiteiQ8VHC5.

Proteomic databases

PaxDbiQ8VHC5.
PRIDEiQ8VHC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025761; ENSMUSP00000025761; ENSMUSG00000024842.
ENSMUST00000181080; ENSMUSP00000137950; ENSMUSG00000097687.
GeneIDi73660.
KEGGimmu:73660.
UCSCiuc008fyw.1. mouse.

Organism-specific databases

CTDi57010.
MGIiMGI:1920910. Cabp4.

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ8VHC5.
OMAiRELGDCM.
OrthoDBiEOG7XM303.
PhylomeDBiQ8VHC5.
TreeFamiTF334804.

Miscellaneous databases

PROiQ8VHC5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHC5.
CleanExiMM_CABP4.
GenevisibleiQ8VHC5. MM.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR033014. CABP4.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERiPTHR23050:SF196. PTHR23050:SF196. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function."
    Haeseleer F., Imanishi Y., Maeda T., Possin D.E., Maeda A., Lee A., Rieke F., Palczewski K.
    Nat. Neurosci. 7:1079-1087(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CACNA1F, FUNCTION.
    Tissue: Retina.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina.
  3. Cited for: FUNCTION, TISSUE SPECIFICITY.
  4. "Switching of Ca2+-dependent inactivation of Ca(v)1.3 channels by calcium binding proteins of auditory hair cells."
    Yang P.S., Alseikhan B.A., Hiel H., Grant L., Mori M.X., Yang W., Fuchs P.A., Yue D.T.
    J. Neurosci. 26:10677-10689(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1D, TISSUE SPECIFICITY.
  5. "Ca2+-binding proteins tune Ca2+-feedback to Cav1.3 channels in mouse auditory hair cells."
    Cui G., Meyer A.C., Calin-Jageman I., Neef J., Haeseleer F., Moser T., Lee A.
    J. Physiol. (Lond.) 585:791-803(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1D, TISSUE SPECIFICITY.
  6. "Phosphorylation of the Ca2+-binding protein CaBP4 by protein kinase C zeta in photoreceptors."
    Lee A., Jimenez A., Cui G., Haeseleer F.
    J. Neurosci. 27:12743-12754(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-37, MUTAGENESIS OF SER-37; SER-46; 50-SER-SER-51; GLU-149; THR-223; GLU-226 AND GLU-263.
  7. "Interaction and colocalization of CaBP4 and Unc119 (MRG4) in photoreceptors."
    Haeseleer F.
    Invest. Ophthalmol. Vis. Sci. 49:2366-2375(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC119.

Entry informationi

Entry nameiCABP4_MOUSE
AccessioniPrimary (citable) accession number: Q8VHC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.