CABP1_BOVIN
ID CABP1_BOVIN Reviewed; 226 AA.
AC Q9N1R0; Q9N1R1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Calcium-binding protein 1;
DE Short=CaBP1;
GN Name=CABP1;
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] (ISOFORMS L-CABP1 AND S-CABP1), PARTIAL PROTEIN
RP SEQUENCE, AND IDENTIFICATION BY 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).
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 Causes calcium-dependent facilitation and inhibits inactivation of L-
CC type calcium channels by binding to the same sites as calmodulin in the
CC C-terminal domain of CACNA1C, but has an opposite effect on channel
CC function. Suppresses the calcium-dependent inactivation of CACNA1D.
CC Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular
CC degeneration. Required for the normal transfer of light signals through
CC the retina. {ECO:0000250|UniProtKB:O88751,
CC ECO:0000250|UniProtKB:Q9JLK7, ECO:0000250|UniProtKB:Q9NZU7}.
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with ITPR1, ITPR2 and
CC ITPR3. This binding is calcium dependent and the interaction correlates
CC with calcium concentration. An additional calcium-independent
CC interaction with the N-terminus of ITPR1 results in a decreased InsP(3)
CC binding to the receptor (By similarity). Interacts with CACNA1A (via C-
CC terminal CDB motif) in the pre- and postsynaptic membranes (By
CC similarity). Interacts with CACNA1C (via C-terminal C and IQ motifs).
CC Interacts with CACNA1D (By similarity). 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) (By similarity).
CC Interacts (via EF-hands 1 and 2) at microtubules with MAP1LC3B (By
CC similarity). Interacts with MYO1C (By similarity). Interacts (via EF-
CC hands 1 and 2) with NSMF (via the central NLS-containing motif region),
CC the interaction occurs in a calcium dependent manner after synaptic
CC NMDA receptor stimulation and prevents nuclear import of NSMF.
CC Interacts with SPACA9 (By similarity). {ECO:0000250|UniProtKB:O88751,
CC ECO:0000250|UniProtKB:Q9JLK7, ECO:0000250|UniProtKB:Q9NZU7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=L-CaBP1;
CC IsoId=Q9N1R0-1; Sequence=Displayed;
CC Name=S-CaBP1;
CC IsoId=Q9N1R0-2; Sequence=VSP_000730;
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}.
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DR EMBL; AF169151; AAF25785.1; -; mRNA.
DR EMBL; AF169150; AAF25784.1; -; mRNA.
DR RefSeq; NP_776679.1; NM_174254.2. [Q9N1R0-1]
DR AlphaFoldDB; Q9N1R0; -.
DR SMR; Q9N1R0; -.
DR STRING; 9913.ENSBTAP00000026714; -.
DR PaxDb; Q9N1R0; -.
DR Ensembl; ENSBTAT00000044919; ENSBTAP00000042361; ENSBTAG00000020049. [Q9N1R0-2]
DR Ensembl; ENSBTAT00000083615; ENSBTAP00000072049; ENSBTAG00000020049. [Q9N1R0-1]
DR GeneID; 281653; -.
DR KEGG; bta:281653; -.
DR CTD; 9478; -.
DR VEuPathDB; HostDB:ENSBTAG00000020049; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000158555; -.
DR HOGENOM; CLU_061288_2_2_1; -.
DR InParanoid; Q9N1R0; -.
DR OMA; KKMCQEE; -.
DR OrthoDB; 1424914at2759; -.
DR TreeFam; TF334804; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000020049; Expressed in cerebellum and 89 other tissues.
DR ExpressionAtlas; Q9N1R0; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:AgBase.
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:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISS:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
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:0007601; P:visual perception; ISS: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; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat; Sensory transduction; Synapse; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..226
FT /note="Calcium-binding protein 1"
FT /id="PRO_0000073512"
FT DOMAIN 81..116
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 135..152
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 158..193
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 195..226
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
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 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 179
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..74
FT /note="Missing (in isoform S-CaBP1)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_000730"
FT INIT_MET Q9N1R0-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q9N1R0-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305"
FT LIPID Q9N1R0-2:4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25755 MW; BC1AF2D62FDF9F02 CRC64;
MGNCVKSPLR NLSRKMRQEE TSYTVVQTSE EGLAASGELP GPLLMLAQNC AVMHNLLGPA
CIFLRKGFAE NRQPDRSLRP EEIEELREAF REFDKDKDGY INCRDLGNCM RTMGYMPTEM
ELIELSQQIN MNLGGHVDFD DFVELMGPKL LAETADMIGV KELRDAFREF DTNGDGEIST
SELREAMRKL LGHQVGHRDI EEIIRDVDLN GDGRVDFEEF VRMMSR
