CABP5_BOVIN
ID CABP5_BOVIN Reviewed; 173 AA.
AC Q9N1Q8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Calcium-binding protein 5;
DE Short=CaBP5;
GN Name=CABP5;
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], PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
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 STXBP1 AND MYO6, 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 (By similarity). Involved in the transmission of
CC light signals (By similarity). May positively regulate neurotransmitter
CC vesicle endocytosis and exocytosis in a salt-dependent manner (By
CC similarity). May play a role in the extension and network organization
CC of neurites (By similarity). {ECO:0000250|UniProtKB:D3ZW89,
CC ECO:0000250|UniProtKB:Q9JLK3}.
CC -!- SUBUNIT: Interacts with CACNA1C (via C-terminal CDB motif) in a
CC calcium-dependent manner (By similarity). Interacts with STXBP1
CC (PubMed:22039235). Interacts with MYO6 (PubMed:22039235).
CC {ECO:0000250|UniProtKB:Q9JLK3, ECO:0000269|PubMed:22039235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NP86}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:22039235}.
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DR EMBL; AF169160; AAF25794.1; -; mRNA.
DR RefSeq; NP_777153.1; NM_174728.2.
DR AlphaFoldDB; Q9N1Q8; -.
DR SMR; Q9N1Q8; -.
DR STRING; 9913.ENSBTAP00000021449; -.
DR PaxDb; Q9N1Q8; -.
DR PRIDE; Q9N1Q8; -.
DR Ensembl; ENSBTAT00000021449; ENSBTAP00000021449; ENSBTAG00000016114.
DR GeneID; 282715; -.
DR KEGG; bta:282715; -.
DR CTD; 56344; -.
DR VEuPathDB; HostDB:ENSBTAG00000016114; -.
DR VGNC; VGNC:26667; CABP5.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000160506; -.
DR HOGENOM; CLU_061288_2_2_1; -.
DR InParanoid; Q9N1Q8; -.
DR OMA; QQVRMNL; -.
DR OrthoDB; 1470794at2759; -.
DR TreeFam; TF334804; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000016114; Expressed in retina and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; Direct protein sequencing; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..173
FT /note="Calcium-binding protein 5"
FT /id="PRO_0000073523"
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; 19628 MW; C76D75BF4D3214A8 CRC64;
MQFPMGPACI FLRKGIAEKQ RERPLGPDEI EELREAFLEF DKDRDGFISC KDLGNLMRTM
GYMPTEMELI ELGQQIRMNL GGRVDFDDFV ELMTPKLLAE TAGMIGVQEM RDAFKEFDAN
GDGEITLGEL QQAMQRLLGD KLTSQEISEV VQEADINGDG TVDFEEFVKM MSR
