CABP2_MOUSE
ID CABP2_MOUSE Reviewed; 216 AA.
AC Q9JLK4; Q3KNX9; Q9JLK5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Calcium-binding protein 2;
DE Short=CaBP2;
GN Name=Cabp2;
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] (ISOFORMS L-CABP2 AND S-CABP2).
RC TISSUE=Retina;
RX PubMed=10625670; DOI=10.1074/jbc.275.2.1247;
RA Haeseleer F., Sokal I., Verlinde C.L.M.J., Erdjument-Bromage H., Tempst P.,
RA Pronin A.N., Benovic J.L., Fariss R.N., Palczewski K.;
RT "Five members of a novel Ca(2+)-binding protein (CABP) subfamily with
RT similarity to calmodulin.";
RL J. Biol. Chem. 275:1247-1260(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-CABP2).
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 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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=27822497; DOI=10.1523/eneuro.0099-16.2016;
RA Sinha R., Lee A., Rieke F., Haeseleer F.;
RT "Lack of CaBp1/caldendrin or cabp2 leads to altered ganglion cell
RT responses.";
RL ENeuro 3:0-0(2016).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=26809054; DOI=10.1371/journal.pone.0147495;
RA Yang T., Scholl E.S., Pan N., Fritzsch B., Haeseleer F., Lee A.;
RT "Expression and localization of cabp ca2+ binding proteins in the mouse
RT cochlea.";
RL PLoS ONE 11:E0147495-E0147495(2016).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=28183797; DOI=10.1073/pnas.1617533114;
RA Picher M.M., Gehrt A., Meese S., Ivanovic A., Predoehl F., Jung S.,
RA Schrauwen I., Dragonetti A.G., Colombo R., Van Camp G., Strenzke N.,
RA Moser T.;
RT "Ca(2+)-binding protein 2 inhibits Ca(2+)-channel inactivation in mouse
RT inner hair cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1717-E1726(2017).
CC -!- FUNCTION: Required for sound encoding at inner hair cells (IHCs)
CC synapses, likely via inhibition of the inactivation of voltage-gated
CC calcium channel of type 1.3 (Cav1.3) in the IHCs (PubMed:28183797).
CC Required for the normal transfer of light signals through the retina
CC (PubMed:27822497). {ECO:0000269|PubMed:27822497,
CC ECO:0000269|PubMed:28183797}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=L-CaBP2;
CC IsoId=Q9JLK4-1; Sequence=Displayed;
CC Name=S-CaBP2;
CC IsoId=Q9JLK4-2; Sequence=VSP_000735;
CC -!- TISSUE SPECIFICITY: Expressed in the inner hair cells (IHCs), outer
CC hair cells,(OHCs) and vestibular hair cells within the ear and in the
CC retina (at protein level) (PubMed:28183797, PubMed:17947313). Expressed
CC in the retinal cone type 6 ON-bipolar cells and type 1 OFF-bipolar
CC cells (at protein level) (PubMed:27822497). Expressed in the organ of
CC Corti and spiral ganglion neurons in the cochlea (at protein level)
CC (PubMed:26809054). {ECO:0000269|PubMed:17947313,
CC ECO:0000269|PubMed:26809054, ECO:0000269|PubMed:27822497,
CC ECO:0000269|PubMed:28183797}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit synaptic hearing impairment and
CC impaired auditory brainstem responses. Enhanced inactivation of Ca(2+)
CC influx in inner hair cells (IHCs), whereas its amplitude and voltage
CC dependence of activation is normal. Reduced normal spontaneous and
CC sound-evoked firing of spiral ganglion neurons (SGNs) seen
CC (PubMed:28183797). Mice exhibit normal retinal morphology but altered
CC light responses of retinal ganglion cells (PubMed:27822497).
CC {ECO:0000269|PubMed:27822497, ECO:0000269|PubMed:28183797}.
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DR EMBL; AF169157; AAF25791.1; -; mRNA.
DR EMBL; AF169156; AAF25790.1; -; mRNA.
DR EMBL; BC107029; AAI07030.1; -; mRNA.
DR RefSeq; NP_001153724.1; NM_001160252.1.
DR RefSeq; NP_001153725.1; NM_001160253.1.
DR RefSeq; NP_038906.2; NM_013878.2.
DR AlphaFoldDB; Q9JLK4; -.
DR SMR; Q9JLK4; -.
DR STRING; 10090.ENSMUSP00000125255; -.
DR PaxDb; Q9JLK4; -.
DR PRIDE; Q9JLK4; -.
DR ProteomicsDB; 273873; -. [Q9JLK4-1]
DR ProteomicsDB; 273874; -. [Q9JLK4-2]
DR DNASU; 29866; -.
DR GeneID; 29866; -.
DR KEGG; mmu:29866; -.
DR CTD; 51475; -.
DR MGI; MGI:1352749; Cabp2.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; Q9JLK4; -.
DR OrthoDB; 1424914at2759; -.
DR PhylomeDB; Q9JLK4; -.
DR BioGRID-ORCS; 29866; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9JLK4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JLK4; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR015754; Ca-bd_2.
DR InterPro; IPR043582; CaBP1/2/4/5.
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:SF2; PTHR45917:SF2; 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 Alternative splicing; Calcium; Cell membrane; Cytoplasm; Golgi apparatus;
KW Hearing; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..216
FT /note="Calcium-binding protein 2"
FT /id="PRO_0000073518"
FT DOMAIN 74..109
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 125..142
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 148..183
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 185..216
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 16..68
FT /note="Missing (in isoform S-CaBP2)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_000735"
SQ SEQUENCE 216 AA; 24223 MW; 416A49E44A7290DD CRC64;
MGNCAKTPWH RGSKERWQWP GSPLGGSRPS PGPRTEEQEG TQGYSVLGSL VGPACIFLRP
SIAATQLDRE LRPEEIEELQ IAFQEFDRDR DGYIGYRELG ACMRTLGYMP TEMELIEISQ
QISGGKVDFE DFVELMGPKL LAETADMIGV RELRDAFREF DTNGDGCISV GELRAALKAL
LGERLSQREV DEILQDIDLN GDGLVDFEEF VRMMSR
