CABP4_BOVIN
ID CABP4_BOVIN Reviewed; 279 AA.
AC Q8HZJ4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Calcium-binding protein 4;
DE Short=CaBP4;
GN Name=CABP4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: May play a role in normal synaptic function, probably through
CC regulation of Ca(2+) influx and neurotransmitter release in
CC photoreceptor synaptic terminals and in auditory transmission.
CC Modulator of CACNA1F, shifting the activation range to more
CC hyperpolarized voltages (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CACNA1F and CACNA1D (via IQ domain) in a
CC calcium independent manner. Interacts (via N-terminus) with UNC119.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P57796}.
CC Presynapse {ECO:0000250|UniProtKB:Q8VHC5}. Note=Found in rod spherules
CC and cone pedicles of the presynapses from both types of photoreceptors.
CC {ECO:0000250|UniProtKB:Q8VHC5}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina.
CC {ECO:0000269|PubMed:15452577}.
CC -!- PTM: Phosphorylated. Phosphorylation levels change with the light
CC conditions and regulate the activity (By similarity). {ECO:0000250}.
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DR EMBL; AY048883; AAL05941.1; -; mRNA.
DR RefSeq; NP_776681.1; NM_174256.3.
DR AlphaFoldDB; Q8HZJ4; -.
DR SMR; Q8HZJ4; -.
DR STRING; 9913.ENSBTAP00000006283; -.
DR PaxDb; Q8HZJ4; -.
DR Ensembl; ENSBTAT00000006283; ENSBTAP00000006283; ENSBTAG00000004785.
DR GeneID; 281656; -.
DR KEGG; bta:281656; -.
DR CTD; 57010; -.
DR VEuPathDB; HostDB:ENSBTAG00000004785; -.
DR VGNC; VGNC:26666; CABP4.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000161468; -.
DR HOGENOM; CLU_061288_8_1_1; -.
DR InParanoid; Q8HZJ4; -.
DR OMA; KNPSRTR; -.
DR OrthoDB; 1340191at2759; -.
DR TreeFam; TF334804; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000004785; Expressed in retina and 10 other tissues.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0060040; P:retinal bipolar neuron differentiation; IEA:Ensembl.
DR GO; GO:0046549; P:retinal cone cell development; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
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; 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 2: Evidence at transcript level;
KW Calcium; Cell projection; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse.
FT CHAIN 1..279
FT /note="Calcium-binding protein 4"
FT /id="PRO_0000073520"
FT DOMAIN 133..168
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 187..204
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 210..245
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 247..279
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHC5"
SQ SEQUENCE 279 AA; 31164 MW; D5DF200B0486AA97 CRC64;
MAEEQGRGRH GPDPAPRPQK PPVEVLASSS GAEGPPLMRK RSSKREKGLR GSRKGPSSSG
EQTPMQGPEA PGSSKNPSRT REGQEGPIPS ASGLAPRRQS HRHRPGPQHD AAQRMYGPLL
NRIFGKDREL GPEELDELQA AFEEFDTDHD GYIGYRDLGE CMRTLGYMPT EMELIEVSQH
VKMRMGGRVD FEEFVEMMGP KLREETAHML GLRELRIAFR EFDRDRDGRI TVAELREAAP
ALLGEPLVGP ELEEMLQEVD LNGDGTVDFN EFVMMLSRH
