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Calcium-binding protein 1 (CaBP1) (Caldendrin)

 CABP1_RAT               Reviewed;         298 AA.
O88751; Q711K8; Q91WZ7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
25-OCT-2017, entry version 142.
RecName: Full=Calcium-binding protein 1;
Short=CaBP1;
AltName: Full=Caldendrin;
Name=Cabp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
STRAIN=Sprague-Dawley;
PubMed=9694893; DOI=10.1074/jbc.273.33.21324;
Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M.,
Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.;
"Caldendrin, a novel neuronal calcium-binding protein confined to the
somato-dendritic compartment.";
J. Biol. Chem. 273:21324-21331(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11906216; DOI=10.1006/mcne.2001.1078;
Laube G., Seidenbecher C.I., Richter K., Dieterich D.C., Hoffmann B.,
Landwehr M., Smalla K.H., Winter C., Boeckers T.M., Wolf G.,
Gundelfinger E.D., Kreutz M.R.;
"The neuron-specific Ca2+-binding protein caldendrin: gene structure,
splice isoforms, and expression in the rat central nervous system.";
Mol. Cell. Neurosci. 19:459-475(2002).
[3]
SEQUENCE REVISION TO 290-291.
Seidenbecher C.I.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
INTERACTION WITH ITPR1; ITPR2 AND ITPR3.
PubMed=12032348; DOI=10.1073/pnas.102006299;
Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K.,
Haeseleer F., Foskett J.K.;
"Identification of a family of calcium sensors as protein ligands of
inositol trisphosphate receptor Ca(2+) release channels.";
Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
[5]
FUNCTION, AND INTERACTION WITH CACNA1A.
PubMed=11865310; DOI=10.1038/nn805;
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
Catterall W.A.;
"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
binding protein 1.";
Nat. Neurosci. 5:210-217(2002).
[6]
INTERACTION WITH MAP1LC3B, AND SUBCELLULAR LOCATION.
PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054;
Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M.,
Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A.,
Bockers T.M., Gundelfinger E.D., Kreutz M.R.;
"Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an
association with the microtubule cytoskeleton highlighting exclusive
binding partners for neuronal Ca(2+)-sensor proteins.";
J. Mol. Biol. 336:957-970(2004).
[7]
INTERACTION WITH NSMF.
PubMed=18303947; DOI=10.1371/journal.pbio.0060034;
Dieterich D.C., Karpova A., Mikhaylova M., Zdobnova I., Konig I.,
Landwehr M., Kreutz M., Smalla K.H., Richter K., Landgraf P.,
Reissner C., Boeckers T.M., Zuschratter W., Spilker C.,
Seidenbecher C.I., Garner C.C., Gundelfinger E.D., Kreutz M.R.;
"Caldendrin-Jacob: a protein liaison that couples NMDA receptor
signalling to the nucleus.";
PLoS Biol. 6:E34-E34(2008).
-!- FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-
triphosphate receptors (ITPRs). Inhibits agonist-induced
intracellular calcium signaling. Enhances inactivation and does
not support calcium-dependent facilitation of voltage-dependent
P/Q-type calcium channels. Causes calcium-dependent facilitation
and inhibits inactivation of L-type calcium channels by binding to
the same sites as calmodulin in the C-terminal domain of CACNA1C,
but resulting in an opposit effects on channel function.
Suppresses the calcium-dependent inactivation of CACNA1D (By
similarity). Inhibits TRPC5 channels (By similarity). Prevents
NMDA receptor-induced cellular degeneration. {ECO:0000250,
ECO:0000269|PubMed:11865310}.
-!- SUBUNIT: Interacts ITPR1, ITPR2 and ITPR3. The strength of this
interaction inversely correlates with calcium concentration.
Interacts with CACNA1A (via C-terminal CDB motif) in the pre- and
postsynaptic membranes. Interacts with CACNA1C. Interacts with
CACNA1D (By similarity). Interacts (via EF-hands 1 and 2) at
microtubules with MAP1LC3B. Interacts (via EF-hands 1 and 2) with
NSMF (via the central NLS-containing motif region), the
interaction occurs in a calcium dependent manner after synaptic
NMDA receptor stimulation and prevents nuclear import of NSMF.
Interacts with MYO1C and TRPC5. Interacts with SPACA9 (By
similarity). {ECO:0000250|UniProtKB:Q9JLK7,
ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:11865310,
ECO:0000269|PubMed:15095872, ECO:0000269|PubMed:18303947}.
-!- INTERACTION:
Q99NF2-1:Nsmf (xeno); NbExp=2; IntAct=EBI-15688755, EBI-15688721;
Q9EPI6-1:Nsmf; NbExp=4; IntAct=EBI-15688755, EBI-15688762;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15095872}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15095872}. Note=Occurs
in both the cytoplasmic and cytoskeletal compartment of cell
somata and dendrites.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O88751-1; Sequence=Displayed;
Note=Major isoform expressed in the brain.;
Name=2; Synonyms=Caldendrin-S1;
IsoId=O88751-2; Sequence=VSP_026157;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. Contains a S-palmitoyl cysteine at position 4.
Minor isoform expressed in the brain, in the granule cell layer
of the cerebellum, at low level. Not developmentally regulated.
{ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:11906216};
Name=3; Synonyms=Caldendrin-S2;
IsoId=O88751-3; Sequence=VSP_026158;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. Contains a S-palmitoyl cysteine at position 4.
Minor isoform expressed in the brain, in the granule cell layer
of the cerebellum, at low level. Not developmentally regulated.
{ECO:0000250|UniProtKB:Q9NZU7, ECO:0000269|PubMed:11906216};
-!- TISSUE SPECIFICITY: Somatodendritic compartment of neurons.
Restricted expression in retina to a subpopulation of amacrine,
bipolar, and ganglion cells. According to PubMed:11906216,
expression is heterogeneous within brain regions and their major
cell types and does not match with those of marker proteins for
characterized neuronal subpopulations.
{ECO:0000269|PubMed:11906216}.
-!- DEVELOPMENTAL STAGE: Its expression is regulated differentially in
retinal cell types during development.
-!- DOMAIN: EF-1 binds magnesium constitutively under physiological
conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2
binds neither calcium nor magnesium. {ECO:0000250}.
-!- PTM: Phosphorylated. The phosphorylation regulates the activity
(By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y17048; CAD20347.1; -; mRNA.
EMBL; AJ315761; CAC43037.1; -; mRNA.
EMBL; AJ315657; CAC42417.1; -; mRNA.
RefSeq; NP_001028847.1; NM_001033675.1. [O88751-2]
RefSeq; NP_001028848.1; NM_001033676.1.
RefSeq; NP_598213.1; NM_133529.2. [O88751-3]
UniGene; Rn.23560; -.
ProteinModelPortal; O88751; -.
SMR; O88751; -.
CORUM; O88751; -.
IntAct; O88751; 3.
STRING; 10116.ENSRNOP00000001551; -.
PaxDb; O88751; -.
PRIDE; O88751; -.
Ensembl; ENSRNOT00000001552; ENSRNOP00000001552; ENSRNOG00000001173. [O88751-3]
Ensembl; ENSRNOT00000039281; ENSRNOP00000033685; ENSRNOG00000001173. [O88751-2]
GeneID; 171051; -.
KEGG; rno:171051; -.
UCSC; RGD:620385; rat. [O88751-1]
CTD; 9478; -.
RGD; 620385; Cabp1.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOGENOM; HOG000233018; -.
HOVERGEN; HBG012180; -.
InParanoid; O88751; -.
OMA; NVLGPAC; -.
OrthoDB; EOG091G0PB4; -.
PhylomeDB; O88751; -.
PRO; PR:O88751; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001173; -.
ExpressionAtlas; O88751; baseline and differential.
Genevisible; O88751; RN.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:RGD.
GO; GO:0005856; C:cytoskeleton; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:RGD.
GO; GO:0008139; F:nuclear localization sequence binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; IPI:RGD.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0010651; P:negative regulation of cell communication by electrical coupling; IDA:RGD.
GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:UniProtKB.
GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:RGD.
GO; GO:1905539; P:regulation of postsynapse to nucleus signaling pathway; IMP:SynGO.
GO; GO:0048167; P:regulation of synaptic plasticity; NAS:RGD.
GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IDA:RGD.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 2.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Metal-binding; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 298 Calcium-binding protein 1.
/FTId=PRO_0000073515.
DOMAIN 153 188 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 189 224 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 230 265 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 267 298 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 166 177 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 243 254 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 280 291 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
METAL 166 166 Magnesium. {ECO:0000250}.
METAL 168 168 Magnesium. {ECO:0000250}.
METAL 170 170 Magnesium. {ECO:0000250}.
METAL 172 172 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 243 243 Calcium 1. {ECO:0000250}.
METAL 245 245 Calcium 1. {ECO:0000250}.
METAL 247 247 Calcium 1. {ECO:0000250}.
METAL 249 249 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 254 254 Calcium 1. {ECO:0000250}.
METAL 280 280 Calcium 2. {ECO:0000250}.
METAL 281 281 Calcium 2; via amide nitrogen.
{ECO:0000250}.
METAL 282 282 Calcium 2. {ECO:0000250}.
METAL 284 284 Calcium 2. {ECO:0000250}.
METAL 285 285 Calcium 2; via amide nitrogen.
{ECO:0000250}.
METAL 286 286 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 288 288 Calcium 2. {ECO:0000250}.
METAL 291 291 Calcium 2. {ECO:0000250}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NZU7}.
VAR_SEQ 1 146 MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRR
LPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQA
HCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAP
AGTPEADPFLHQLRPMLSSAFGQ -> MGNCVKSPLRNLSR
K (in isoform 2).
{ECO:0000303|PubMed:11906216}.
/FTId=VSP_026157.
VAR_SEQ 1 146 MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRR
LPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQA
HCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAP
AGTPEADPFLHQLRPMLSSAFGQ -> MGNCVKSPLRNLSR
KMRQEEKTSYMAVQTSEDGLADGGELPGPLMMLAQNCAVMH
NLLGPACIFLRKGFAENRQP (in isoform 3).
{ECO:0000303|PubMed:11906216}.
/FTId=VSP_026158.
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


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