CABP1_MOUSE
ID CABP1_MOUSE Reviewed; 227 AA.
AC Q9JLK7; Q9JLK6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calcium-binding protein 1;
DE Short=CaBP1;
GN Name=Cabp1;
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-CABP1 AND S-CABP1).
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 INTERACTION WITH TRPC5.
RX PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
RA Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.;
RT "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
RT oocytes.";
RL Pflugers Arch. 450:345-354(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH CACNA1D.
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 [4]
RP FUNCTION, AND INTERACTION WITH CACNA1D.
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 [5]
RP INTERACTION WITH MYO1C.
RX PubMed=17994197; DOI=10.1007/s10974-007-9124-7;
RA Tang N., Lin T., Yang J., Foskett J.K., Ostap E.M.;
RT "CIB1 and CaBP1 bind to the myo1c regulatory domain.";
RL J. Muscle Res. Cell Motil. 28:285-291(2007).
RN [6]
RP INTERACTION WITH SPACA9.
RX PubMed=24256100; DOI=10.1186/1471-2121-14-50;
RA Bhattacharya R., Devi M.S., Dhople V.M., Jesudasan R.A.;
RT "A mouse protein that localizes to acrosome and sperm tail is regulated by
RT Y-chromosome.";
RL BMC Cell Biol. 14:50-50(2013).
RN [7]
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 [8]
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).
CC -!- FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-
CC triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular
CC calcium signaling. Enhances inactivation and does not support calcium-
CC dependent facilitation of voltage-dependent P/Q-type calcium channels
CC (By similarity). Causes calcium-dependent facilitation and inhibits
CC inactivation of L-type calcium channels by binding to the same sites as
CC calmodulin in the C-terminal domain of CACNA1C, but has an opposite
CC effect on channel function. Suppresses the calcium-dependent
CC inactivation of CACNA1D (PubMed:17050707, PubMed:17947313). Inhibits
CC TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration
CC (By similarity). Required for the normal transfer of light signals
CC through the retina (PubMed:27822497). {ECO:0000250|UniProtKB:Q9NZU7,
CC ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313,
CC ECO:0000269|PubMed:27822497}.
CC -!- SUBUNIT: Homodimer; when bound to calcium or magnesium. Interacts (via
CC C-terminus) with ITPR1, ITPR2 and ITPR3. This binding is calcium
CC dependent and the interaction correlates with calcium concentration. An
CC additional calcium-independent interaction with the N-terminus of ITPR1
CC results in a decreased InsP(3) binding to the receptor (By similarity).
CC Interacts with CACNA1A (via C-terminal CDB motif) in the pre- and
CC postsynaptic membranes (By similarity). Interacts with CACNA1D and
CC CACNA1C (via C-terminal C and IQ motifs). The binding to the C motif is
CC calcium independent whereas the binding to IQ requires the presence of
CC calcium and is mutually exclusive with calmodulin binding (By
CC similarity). Interacts with TRPC5 (via C-terminus). Interacts (via EF-
CC hands 1 and 2) at microtubules with MAP1LC3B (By similarity). Interacts
CC with MYO1C. Interacts (via EF-hands 1 and 2) with NSMF (via the central
CC NLS-containing motif region), the interaction occurs in a calcium
CC dependent manner after synaptic NMDA receptor stimulation and prevents
CC nuclear import of NSMF. Interacts with SPACA9 homolog.
CC {ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:15895247,
CC ECO:0000269|PubMed:17050707, ECO:0000269|PubMed:17947313,
CC ECO:0000269|PubMed:17994197, ECO:0000269|PubMed:24256100}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=L-CaBP1;
CC IsoId=Q9JLK7-1; Sequence=Displayed;
CC Name=S-CaBP1;
CC IsoId=Q9JLK7-2; Sequence=VSP_000733;
CC -!- TISSUE SPECIFICITY: Expressed in the inner retina, specifically in
CC amacrine cells and in cone OFF-bipolar cells (at protein level)
CC (PubMed:27822497). {ECO:0000269|PubMed:27822497}.
CC -!- DOMAIN: EF-1 binds magnesium constitutively under physiological
CC conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds
CC neither calcium nor magnesium. {ECO:0000250}.
CC -!- PTM: Phosphorylated. The phosphorylation regulates the activity (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit a normal retinal morphology but
CC altered light responses of retinal ganglion cells (PubMed:27822497).
CC {ECO:0000269|PubMed:27822497}.
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DR EMBL; AF169152; AAF25786.1; -; mRNA.
DR EMBL; AF169153; AAF25787.1; -; mRNA.
DR CCDS; CCDS19582.1; -. [Q9JLK7-1]
DR CCDS; CCDS80378.1; -. [Q9JLK7-2]
DR RefSeq; NP_001297644.1; NM_001310715.1. [Q9JLK7-2]
DR RefSeq; NP_038907.1; NM_013879.2. [Q9JLK7-1]
DR AlphaFoldDB; Q9JLK7; -.
DR SMR; Q9JLK7; -.
DR BioGRID; 205933; 1.
DR CORUM; Q9JLK7; -.
DR STRING; 10090.ENSMUSP00000031519; -.
DR PhosphoSitePlus; Q9JLK7; -.
DR MaxQB; Q9JLK7; -.
DR PaxDb; Q9JLK7; -.
DR PRIDE; Q9JLK7; -.
DR ProteomicsDB; 273815; -. [Q9JLK7-1]
DR ProteomicsDB; 273816; -. [Q9JLK7-2]
DR Antibodypedia; 31502; 125 antibodies from 30 providers.
DR DNASU; 29867; -.
DR Ensembl; ENSMUST00000031519; ENSMUSP00000031519; ENSMUSG00000029544. [Q9JLK7-1]
DR Ensembl; ENSMUST00000112112; ENSMUSP00000107740; ENSMUSG00000029544. [Q9JLK7-2]
DR GeneID; 29867; -.
DR KEGG; mmu:29867; -.
DR UCSC; uc008zdg.1; mouse. [Q9JLK7-1]
DR UCSC; uc008zdh.1; mouse. [Q9JLK7-2]
DR CTD; 9478; -.
DR MGI; MGI:1352750; Cabp1.
DR VEuPathDB; HostDB:ENSMUSG00000029544; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000158555; -.
DR HOGENOM; CLU_061288_2_2_1; -.
DR InParanoid; Q9JLK7; -.
DR OMA; KKMCQEE; -.
DR PhylomeDB; Q9JLK7; -.
DR TreeFam; TF334804; -.
DR BioGRID-ORCS; 29867; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cabp1; mouse.
DR PRO; PR:Q9JLK7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JLK7; protein.
DR Bgee; ENSMUSG00000029544; Expressed in retinal neural layer and 93 other tissues.
DR ExpressionAtlas; Q9JLK7; baseline and differential.
DR Genevisible; Q9JLK7; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0099573; C:glutamatergic postsynaptic density; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0044280; C:subplasmalemmal coating; ISO:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0010651; P:negative regulation of cell communication by electrical coupling; ISO:MGI.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:1905539; P:regulation of postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR CDD; cd00051; EFh; 1.
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 Pfam; PF13499; EF-hand_7; 2.
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; Lipoprotein; Metal-binding; Myristate;
KW Palmitate; Phosphoprotein; Reference proteome; Repeat;
KW Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..227
FT /note="Calcium-binding protein 1"
FT /id="PRO_0000073514"
FT DOMAIN 82..117
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 136..153
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 159..194
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 196..227
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU7"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU7"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU7"
FT VAR_SEQ 16..75
FT /note="Missing (in isoform S-CaBP1)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_000733"
FT INIT_MET Q9JLK7-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q9JLK7-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305"
FT LIPID Q9JLK7-2:4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25943 MW; C0AA48F481664617 CRC64;
MGNCVKSPLR NLSRKMRQEE KTSYMAVQTS EDGLADGGEL HGPLMMLAQN CAVMHNLLGP
ACIFLRKGFA ENRQPDRSLR PEEIEELREA FREFDKDKDG YINCRDLGNC MRTMGYMPTE
MELIELSQQI NMNLGGHVDF DDFVELMGPK LLAETADMIG VKELRDAFRE FDTNGDGEIS
TSELREAMRK LLGHQVGHRD IEEIIRDVDL NGDGRVDFEE FVRMMSR
