CABP1_RAT
ID CABP1_RAT Reviewed; 298 AA.
AC O88751; Q711K8; Q91WZ7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Calcium-binding protein 1;
DE Short=CaBP1;
DE AltName: Full=Caldendrin;
GN Name=Cabp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=9694893; DOI=10.1074/jbc.273.33.21324;
RA Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M.,
RA Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.;
RT "Caldendrin, a novel neuronal calcium-binding protein confined to the
RT somato-dendritic compartment.";
RL J. Biol. Chem. 273:21324-21331(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11906216; DOI=10.1006/mcne.2001.1078;
RA Laube G., Seidenbecher C.I., Richter K., Dieterich D.C., Hoffmann B.,
RA Landwehr M., Smalla K.H., Winter C., Boeckers T.M., Wolf G.,
RA Gundelfinger E.D., Kreutz M.R.;
RT "The neuron-specific Ca2+-binding protein caldendrin: gene structure,
RT splice isoforms, and expression in the rat central nervous system.";
RL Mol. Cell. Neurosci. 19:459-475(2002).
RN [3]
RP SEQUENCE REVISION TO 290-291.
RA Seidenbecher C.I.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH ITPR1; ITPR2 AND ITPR3.
RX PubMed=12032348; DOI=10.1073/pnas.102006299;
RA Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F.,
RA Foskett J.K.;
RT "Identification of a family of calcium sensors as protein ligands of
RT inositol trisphosphate receptor Ca(2+) release channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH CACNA1A.
RX PubMed=11865310; DOI=10.1038/nn805;
RA Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
RA Catterall W.A.;
RT "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
RT binding protein 1.";
RL Nat. Neurosci. 5:210-217(2002).
RN [6]
RP INTERACTION WITH MAP1LC3B, AND SUBCELLULAR LOCATION.
RX PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054;
RA Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C.,
RA Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M.,
RA Gundelfinger E.D., Kreutz M.R.;
RT "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an
RT association with the microtubule cytoskeleton highlighting exclusive
RT binding partners for neuronal Ca(2+)-sensor proteins.";
RL J. Mol. Biol. 336:957-970(2004).
RN [7]
RP INTERACTION WITH NSMF.
RX PubMed=18303947; DOI=10.1371/journal.pbio.0060034;
RA Dieterich D.C., Karpova A., Mikhaylova M., Zdobnova I., Konig I.,
RA Landwehr M., Kreutz M., Smalla K.H., Richter K., Landgraf P., Reissner C.,
RA Boeckers T.M., Zuschratter W., Spilker C., Seidenbecher C.I., Garner C.C.,
RA Gundelfinger E.D., Kreutz M.R.;
RT "Caldendrin-Jacob: a protein liaison that couples NMDA receptor signalling
RT to the nucleus.";
RL PLoS Biol. 6:E34-E34(2008).
CC -!- FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-
CC triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular
CC calcium signaling (By similarity). Enhances inactivation and does not
CC support calcium-dependent facilitation of voltage-dependent P/Q-type
CC calcium channels (PubMed:11865310). Causes calcium-dependent
CC facilitation and inhibits inactivation of L-type calcium channels by
CC binding to the same sites as calmodulin in the C-terminal domain of
CC CACNA1C, but has an opposite effect on channel function. Suppresses the
CC calcium-dependent inactivation of CACNA1D. Inhibits TRPC5 channels.
CC Prevents NMDA receptor-induced cellular degeneration. Required for the
CC normal transfer of light signals through the retina (By similarity).
CC {ECO:0000250|UniProtKB:Q9JLK7, ECO:0000250|UniProtKB:Q9NZU7,
CC ECO:0000269|PubMed:11865310}.
CC -!- SUBUNIT: Interacts ITPR1, ITPR2 and ITPR3. The strength of this
CC interaction inversely correlates with calcium concentration. Interacts
CC with CACNA1A (via C-terminal CDB motif) in the pre- and postsynaptic
CC membranes. Interacts with CACNA1C. Interacts with CACNA1D (By
CC similarity). Interacts (via EF-hands 1 and 2) at microtubules with
CC MAP1LC3B. 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 MYO1C and TRPC5. Interacts with
CC SPACA9 (By similarity). {ECO:0000250|UniProtKB:Q9JLK7,
CC ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:11865310,
CC ECO:0000269|PubMed:15095872, ECO:0000269|PubMed:18303947}.
CC -!- INTERACTION:
CC O88751-1; Q9EPI6-1: Nsmf; NbExp=4; IntAct=EBI-15688755, EBI-15688762;
CC O88751-1; Q99NF2-1: Nsmf; Xeno; NbExp=2; IntAct=EBI-15688755, EBI-15688721;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15095872}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15095872}. Note=Occurs in
CC both the cytoplasmic and cytoskeletal compartment of cell somata and
CC dendrites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O88751-1; Sequence=Displayed;
CC Name=2; Synonyms=Caldendrin-S1;
CC IsoId=O88751-2; Sequence=VSP_026157;
CC Name=3; Synonyms=Caldendrin-S2;
CC IsoId=O88751-3; Sequence=VSP_026158;
CC -!- TISSUE SPECIFICITY: Somatodendritic compartment of neurons
CC (PubMed:11906216). Restricted expression in retina to a subpopulation
CC of amacrine, bipolar, and ganglion cells (PubMed:11906216). According
CC to PubMed:11906216, expression is heterogeneous within brain regions
CC and their major cell types and does not match with those of marker
CC proteins for characterized neuronal subpopulations (PubMed:11906216).
CC Isoform 2: Minor isoform expressed in the brain, in the granule cell
CC layer of the cerebellum, at low level. Not developmentally regulated
CC (PubMed:11906216). Isoform 3: Minor isoform expressed in the brain, in
CC the granule cell layer (PubMed:11906216). of the cerebellum, at low
CC level. Not developmentally regulated. {ECO:0000269|PubMed:11906216}.
CC -!- DEVELOPMENTAL STAGE: Its expression is regulated differentially in
CC retinal cell types during development.
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 -!- MISCELLANEOUS: [Isoform 1]: Major isoform expressed in the brain.
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DR EMBL; Y17048; CAD20347.1; -; mRNA.
DR EMBL; AJ315761; CAC43037.1; -; mRNA.
DR EMBL; AJ315657; CAC42417.1; -; mRNA.
DR RefSeq; NP_001028847.1; NM_001033675.1. [O88751-2]
DR RefSeq; NP_001028848.1; NM_001033676.1.
DR RefSeq; NP_598213.1; NM_133529.2. [O88751-3]
DR AlphaFoldDB; O88751; -.
DR BMRB; O88751; -.
DR SMR; O88751; -.
DR CORUM; O88751; -.
DR IntAct; O88751; 3.
DR STRING; 10116.ENSRNOP00000001551; -.
DR PaxDb; O88751; -.
DR PRIDE; O88751; -.
DR Ensembl; ENSRNOT00000001552; ENSRNOP00000001552; ENSRNOG00000001173. [O88751-3]
DR Ensembl; ENSRNOT00000039281; ENSRNOP00000033685; ENSRNOG00000001173. [O88751-2]
DR GeneID; 171051; -.
DR KEGG; rno:171051; -.
DR UCSC; RGD:620385; rat. [O88751-1]
DR CTD; 9478; -.
DR RGD; 620385; Cabp1.
DR VEuPathDB; HostDB:ENSRNOG00000001173; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000158555; -.
DR HOGENOM; CLU_061288_8_0_1; -.
DR InParanoid; O88751; -.
DR OMA; KKMCQEE; -.
DR OrthoDB; 1424914at2759; -.
DR PhylomeDB; O88751; -.
DR PRO; PR:O88751; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001173; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; O88751; baseline and differential.
DR Genevisible; O88751; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0099573; C:glutamatergic postsynaptic density; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0044280; C:subplasmalemmal coating; IDA:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:0010651; P:negative regulation of cell communication by electrical coupling; IDA:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:1905539; P:regulation of postsynapse to nucleus signaling pathway; IMP:SynGO.
DR GO; GO:0048167; P:regulation of synaptic plasticity; NAS:RGD.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IDA:RGD.
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; Cytoplasm; Cytoskeleton;
KW Developmental protein; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Sensory transduction; Vision.
FT CHAIN 1..298
FT /note="Calcium-binding protein 1"
FT /id="PRO_0000073515"
FT DOMAIN 153..188
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 207..224
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 230..265
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 267..298
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU7"
FT VAR_SEQ 1..146
FT /note="MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPAT
FT CGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRG
FT SLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQ -> MGNCVKSPLRNLSRK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11906216"
FT /id="VSP_026157"
FT VAR_SEQ 1..146
FT /note="MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPAT
FT CGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRG
FT SLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQ -> MGNCVKSPLRNLSRKMRQEE
FT KTSYMAVQTSEDGLADGGELPGPLMMLAQNCAVMHNLLGPACIFLRKGFAENRQP (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11906216"
FT /id="VSP_026158"
FT INIT_MET O88751-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID O88751-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305"
FT LIPID O88751-2:4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT INIT_MET O88751-3:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID O88751-3:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305"
FT LIPID O88751-3:4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33017 MW; 8A9B74CD6B9F6875 CRC64;
MSSHIAKSES KTSLLKAAAA SGGSRAPRHS SARDPGLRGR RLPGPCPDSP ATCGDPSSRR
PLCRPVPRDE GARGSRRGLP QAHCRPRETL PPARGRDGEE RGLAPALSLR GSLRSRGRGD
PAPAGTPEAD PFLHQLRPML SSAFGQDRSL RPEEIEELRE AFREFDKDKD GYINCRDLGN
CMRTMGYMPT EMELIELSQQ INMNLGGHVD FDDFVELMGP KLLAETADMI GVKELRDAFR
EFDTNGDGEI STSELREAMR KLLGHQVGHR DIEEIIRDVD LNGDGRVDFE EFVRMMSR
