CABP5_MOUSE
ID CABP5_MOUSE Reviewed; 173 AA.
AC Q9JLK3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Calcium-binding protein 5;
DE Short=CaBP5;
GN Name=Cabp5;
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].
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].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH CACNA1C, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18586882; DOI=10.1167/iovs.08-2236;
RA Rieke F., Lee A., Haeseleer F.;
RT "Characterization of Ca2+-binding protein 5 knockout mouse retina.";
RL Invest. Ophthalmol. Vis. Sci. 49:5126-5135(2008).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22039235; DOI=10.1167/iovs.11-8246;
RA Sokal I., Haeseleer F.;
RT "Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.";
RL Invest. Ophthalmol. Vis. Sci. 52:9131-9141(2011).
CC -!- FUNCTION: Inhibits calcium-dependent inactivation of L-type calcium
CC channel and shifts voltage dependence of activation to more depolarized
CC membrane potentials (PubMed:18586882). Involved in the transmission of
CC light signals (PubMed:18586882). May positively regulate
CC neurotransmitter vesicle endocytosis and exocytosis in a salt-dependent
CC manner (PubMed:22039235). May play a role in the extension and network
CC organization of neurites (PubMed:22039235).
CC {ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:22039235}.
CC -!- SUBUNIT: Interacts with CACNA1C (via C-terminal CDB motif) in a
CC calcium-dependent manner (PubMed:18586882). Interacts with STXBP1 (By
CC similarity). Interacts with MYO6 (By similarity).
CC {ECO:0000250|UniProtKB:Q9N1Q8, ECO:0000269|PubMed:18586882}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NP86}.
CC -!- TISSUE SPECIFICITY: Expressed in inner and outer plexiform layers of
CC the retina, and retinal bipolar cells (at protein level)
CC (PubMed:17947313, PubMed:18586882, PubMed:22039235). Expressed in the
CC inner hair cells (IHC) of the cochlea (PubMed:17947313,
CC PubMed:18586882). {ECO:0000269|PubMed:17947313,
CC ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:22039235}.
CC -!- DISRUPTION PHENOTYPE: No morphologic changes, but 50% reduction of the
CC sensitivity of retinal ganglion cell light responses.
CC {ECO:0000269|PubMed:18586882}.
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DR EMBL; AF169161; AAF25795.1; -; mRNA.
DR EMBL; BC018253; AAH18253.1; -; mRNA.
DR CCDS; CCDS20831.1; -.
DR RefSeq; NP_038905.1; NM_013877.3.
DR AlphaFoldDB; Q9JLK3; -.
DR SMR; Q9JLK3; -.
DR STRING; 10090.ENSMUSP00000005791; -.
DR iPTMnet; Q9JLK3; -.
DR PhosphoSitePlus; Q9JLK3; -.
DR PaxDb; Q9JLK3; -.
DR PRIDE; Q9JLK3; -.
DR ProteomicsDB; 273818; -.
DR Antibodypedia; 49583; 192 antibodies from 23 providers.
DR DNASU; 29865; -.
DR Ensembl; ENSMUST00000005791; ENSMUSP00000005791; ENSMUSG00000005649.
DR GeneID; 29865; -.
DR KEGG; mmu:29865; -.
DR UCSC; uc009ffv.1; mouse.
DR CTD; 56344; -.
DR MGI; MGI:1352746; Cabp5.
DR VEuPathDB; HostDB:ENSMUSG00000005649; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000160506; -.
DR HOGENOM; CLU_061288_2_2_1; -.
DR InParanoid; Q9JLK3; -.
DR OMA; QQVRMNL; -.
DR OrthoDB; 1470794at2759; -.
DR PhylomeDB; Q9JLK3; -.
DR TreeFam; TF334804; -.
DR BioGRID-ORCS; 29865; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Pdia6; mouse.
DR PRO; PR:Q9JLK3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JLK3; protein.
DR Bgee; ENSMUSG00000005649; Expressed in retinal neural layer and 18 other tissues.
DR ExpressionAtlas; Q9JLK3; baseline and differential.
DR Genevisible; Q9JLK3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
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 Calcium; Cytoplasm; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..173
FT /note="Calcium-binding protein 5"
FT /id="PRO_0000073525"
FT DOMAIN 28..63
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 82..99
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 105..140
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 142..173
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 173 AA; 19730 MW; 96D14CC81C8BFEE1 CRC64;
MQFPMGPACI FLRKGIAEKQ RERPLGQDEL DELREAFLEF DKDQDGFISY KDLGNLMRTM
GYMPTEMELT ELGQQIRMNL GGRVDFEDFV ELMTPKLLAE TAGMIGVQEM RDAFKEFDAN
GDGEITLAEL QQAMQRLLGE KLTPREIAEV VQEADINGDG TVDFEEFVKM MSR
