CABP4_MOUSE
ID CABP4_MOUSE Reviewed; 271 AA.
AC Q8VHC5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Calcium-binding protein 4;
DE Short=CaBP4;
GN Name=Cabp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INTERACTION WITH CACNA1F, AND FUNCTION.
RC TISSUE=Retina;
RX PubMed=15452577; DOI=10.1038/nn1320;
RA Haeseleer F., Imanishi Y., Maeda T., Possin D.E., Maeda A., Lee A.,
RA Rieke F., Palczewski K.;
RT "Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in
RT photoreceptor synaptic function.";
RL Nat. Neurosci. 7:1079-1087(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16249514; DOI=10.1167/iovs.05-0478;
RA Maeda T., Lem J., Palczewski K., Haeseleer F.;
RT "A critical role of CaBP4 in the cone synapse.";
RL Invest. Ophthalmol. Vis. Sci. 46:4320-4327(2005).
RN [4]
RP FUNCTION, INTERACTION WITH CACNA1D, AND TISSUE SPECIFICITY.
RX PubMed=17050707; DOI=10.1523/jneurosci.3236-06.2006;
RA Yang P.S., Alseikhan B.A., Hiel H., Grant L., Mori M.X., Yang W.,
RA Fuchs P.A., Yue D.T.;
RT "Switching of Ca2+-dependent inactivation of Ca(v)1.3 channels by calcium
RT binding proteins of auditory hair cells.";
RL J. Neurosci. 26:10677-10689(2006).
RN [5]
RP FUNCTION, INTERACTION WITH CACNA1D, AND TISSUE SPECIFICITY.
RX PubMed=17947313; DOI=10.1113/jphysiol.2007.142307;
RA Cui G., Meyer A.C., Calin-Jageman I., Neef J., Haeseleer F., Moser T.,
RA Lee A.;
RT "Ca2+-binding proteins tune Ca2+-feedback to Cav1.3 channels in mouse
RT auditory hair cells.";
RL J. Physiol. (Lond.) 585:791-803(2007).
RN [6]
RP PHOSPHORYLATION AT SER-37, AND MUTAGENESIS OF SER-37; SER-46;
RP 50-SER-SER-51; GLU-149; THR-223; GLU-226 AND GLU-263.
RX PubMed=18003854; DOI=10.1523/jneurosci.4264-07.2007;
RA Lee A., Jimenez A., Cui G., Haeseleer F.;
RT "Phosphorylation of the Ca2+-binding protein CaBP4 by protein kinase C zeta
RT in photoreceptors.";
RL J. Neurosci. 27:12743-12754(2007).
RN [7]
RP INTERACTION WITH UNC119.
RX PubMed=18296658; DOI=10.1167/iovs.07-1166;
RA Haeseleer F.;
RT "Interaction and colocalization of CaBP4 and Unc119 (MRG4) in
RT photoreceptors.";
RL Invest. Ophthalmol. Vis. Sci. 49:2366-2375(2008).
CC -!- FUNCTION: Involved in normal synaptic function through regulation of
CC Ca(2+) influx and neurotransmitter release in photoreceptor synaptic
CC terminals and in auditory transmission. Modulator of CACNA1D and
CC CACNA1F, suppressing the calcium-dependent inactivation and shifting
CC the activation range to more hyperpolarized voltages.
CC {ECO:0000269|PubMed:15452577, ECO:0000269|PubMed:16249514,
CC ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313}.
CC -!- SUBUNIT: Interacts with CACNA1F and CACNA1D (via IQ domain) in a
CC calcium independent manner. Interacts (via N-terminus) with UNC119.
CC {ECO:0000269|PubMed:15452577, ECO:0000269|PubMed:17050707,
CC ECO:0000269|PubMed:17947313, ECO:0000269|PubMed:18296658}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P57796}.
CC Presynapse {ECO:0000269|PubMed:15452577}. Note=Found in rod spherules
CC and cone pedicles of the presynapses from both types of photoreceptors.
CC {ECO:0000269|PubMed:15452577}.
CC -!- TISSUE SPECIFICITY: Expressed in retina and in the inner hair cells
CC (IHC) of the cochlea. {ECO:0000269|PubMed:15452577,
CC ECO:0000269|PubMed:16249514, ECO:0000269|PubMed:17050707,
CC ECO:0000269|PubMed:17947313}.
CC -!- PTM: Phosphorylated. Phosphorylation levels change with the light
CC conditions and regulate the activity, but has no effect on calcium
CC binding. {ECO:0000269|PubMed:18003854}.
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DR EMBL; AY039218; AAK83463.1; -; mRNA.
DR EMBL; BC049263; AAH49263.1; -; mRNA.
DR CCDS; CCDS29416.1; -.
DR RefSeq; NP_653115.1; NM_144532.2.
DR PDB; 2M28; NMR; -; A=101-271.
DR PDB; 2M29; NMR; -; A=101-271.
DR PDBsum; 2M28; -.
DR PDBsum; 2M29; -.
DR AlphaFoldDB; Q8VHC5; -.
DR BMRB; Q8VHC5; -.
DR SMR; Q8VHC5; -.
DR DIP; DIP-60739N; -.
DR IntAct; Q8VHC5; 2.
DR STRING; 10090.ENSMUSP00000025761; -.
DR iPTMnet; Q8VHC5; -.
DR PhosphoSitePlus; Q8VHC5; -.
DR PaxDb; Q8VHC5; -.
DR PRIDE; Q8VHC5; -.
DR ProteomicsDB; 273817; -.
DR Antibodypedia; 30420; 234 antibodies from 26 providers.
DR DNASU; 73660; -.
DR Ensembl; ENSMUST00000025761; ENSMUSP00000025761; ENSMUSG00000024842.
DR GeneID; 73660; -.
DR KEGG; mmu:73660; -.
DR UCSC; uc008fyw.1; mouse.
DR CTD; 57010; -.
DR MGI; MGI:1920910; Cabp4.
DR VEuPathDB; HostDB:ENSMUSG00000024842; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000161468; -.
DR HOGENOM; CLU_061288_8_1_1; -.
DR InParanoid; Q8VHC5; -.
DR OMA; KNPSRTR; -.
DR OrthoDB; 1340191at2759; -.
DR PhylomeDB; Q8VHC5; -.
DR TreeFam; TF334804; -.
DR BioGRID-ORCS; 73660; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Cabp4; mouse.
DR PRO; PR:Q8VHC5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8VHC5; protein.
DR Bgee; ENSMUSG00000024842; Expressed in layer of retina and 51 other tissues.
DR Genevisible; Q8VHC5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:MGI.
DR GO; GO:0007602; P:phototransduction; IMP:MGI.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0060040; P:retinal bipolar neuron differentiation; IMP:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
DR CDD; cd00051; EFh; 1.
DR DisProt; DP01592; -.
DR InterPro; IPR043582; CaBP1/2/4/5.
DR InterPro; IPR033014; CABP4.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45917; PTHR45917; 1.
DR PANTHER; PTHR45917:SF4; PTHR45917:SF4; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cytoplasm; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..271
FT /note="Calcium-binding protein 4"
FT /id="PRO_0000073522"
FT DOMAIN 125..160
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 179..196
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 202..237
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 239..271
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 37
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 37
FT /note="S->A: Decreased phosphorylation."
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 46
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 50..51
FT /note="SS->AA: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 149
FT /note="E->Q: Loss of calcium binding; when associated with
FT Q-226 and Q-263."
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 223
FT /note="T->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 226
FT /note="E->Q: Loss of calcium binding; when associated with
FT Q-149 and Q-263."
FT /evidence="ECO:0000269|PubMed:18003854"
FT MUTAGEN 263
FT /note="E->Q: Loss of calcium binding; when associated with
FT Q-149 and Q-226."
FT /evidence="ECO:0000269|PubMed:18003854"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:2M29"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2M29"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:2M29"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2M29"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:2M29"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2M29"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:2M29"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:2M28"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:2M28"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2M28"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:2M28"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2M28"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:2M28"
SQ SEQUENCE 271 AA; 30268 MW; 3B6C7883C3DB8C1C CRC64;
MATEHNVQLV PGSQKIPKGV VSPRSAAEGP ALTRRRSKKE SWHPGSQKAS SGDQSSSQGS
EASGSSKHPP RTKVGQEEPS SAPARPASHR HSHRHRSDPQ QDAAQRTYGP LLNRMFGKDR
ELGPEELEEL QAAFEEFDTD QDGYIGYREL GDCMRTLGYM PTEMELLEVS QHVKMRMGGF
VDFEEFVELI SPKLREETAH MLGVRELRIA FREFDKDRDG RITVAELRQA APALLGEPLE
GTELDEMLRE MDLNGDGTID FDEFVMMLST G
