CALB2_MOUSE
ID CALB2_MOUSE Reviewed; 271 AA.
AC Q08331; Q60964; Q9JM81;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calretinin;
DE Short=CR;
GN Name=Calb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Tanaka Y., Taki K., Eguchi N., Kaneko T.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-31.
RC STRAIN=129/Sv;
RX PubMed=9387877; DOI=10.1016/s0169-328x(97)00143-5;
RA Strauss K.I., Kuznicki J., Winsky L., Kawagoe J.I., Hammer M.,
RA Jacobowitz D.M.;
RT "The mouse calretinin gene promoter region: structural and functional
RT components.";
RL Brain Res. Mol. Brain Res. 49:175-187(1997).
RN [4]
RP PROTEIN SEQUENCE OF 27-50; 124-133; 179-189 AND 234-244, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-271.
RX PubMed=8255773; DOI=10.1093/nar/21.22.5171;
RA Ellis J., Rogers J.;
RT "Design and specificity of hammerhead ribozymes against calretinin mRNA.";
RL Nucleic Acids Res. 21:5171-5178(1993).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calretinin is a calcium-binding protein which is abundant in
CC auditory neurons.
CC -!- SIMILARITY: Belongs to the calbindin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037969; BAA90701.1; -; Genomic_DNA.
DR EMBL; BC017646; AAH17646.1; -; mRNA.
DR EMBL; U34818; AAA84429.1; -; Genomic_DNA.
DR EMBL; X73985; CAA52163.1; -; mRNA.
DR CCDS; CCDS22661.1; -.
DR PIR; S41476; S41476.
DR RefSeq; NP_031612.1; NM_007586.1.
DR AlphaFoldDB; Q08331; -.
DR SMR; Q08331; -.
DR BioGRID; 198450; 5.
DR IntAct; Q08331; 1.
DR STRING; 10090.ENSMUSP00000003754; -.
DR iPTMnet; Q08331; -.
DR PhosphoSitePlus; Q08331; -.
DR UCD-2DPAGE; Q08331; -.
DR jPOST; Q08331; -.
DR MaxQB; Q08331; -.
DR PaxDb; Q08331; -.
DR PeptideAtlas; Q08331; -.
DR PRIDE; Q08331; -.
DR ProteomicsDB; 281759; -.
DR ABCD; Q08331; 2 sequenced antibodies.
DR Antibodypedia; 1545; 685 antibodies from 48 providers.
DR DNASU; 12308; -.
DR Ensembl; ENSMUST00000003754; ENSMUSP00000003754; ENSMUSG00000003657.
DR GeneID; 12308; -.
DR KEGG; mmu:12308; -.
DR UCSC; uc009nko.1; mouse.
DR CTD; 794; -.
DR MGI; MGI:101914; Calb2.
DR VEuPathDB; HostDB:ENSMUSG00000003657; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000183108; -.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; Q08331; -.
DR OMA; WSHYDRD; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; Q08331; -.
DR TreeFam; TF325083; -.
DR BioGRID-ORCS; 12308; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Calb2; mouse.
DR PRO; PR:Q08331; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q08331; protein.
DR Bgee; ENSMUSG00000003657; Expressed in habenula and 109 other tissues.
DR ExpressionAtlas; Q08331; baseline and differential.
DR Genevisible; Q08331; MM.
DR GO; GO:0032437; C:cuticular plate; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005921; C:gap junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0032420; C:stereocilium; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IBA:GO_Central.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IBA:GO_Central.
DR CDD; cd16177; EFh_HEF_CR; 1.
DR InterPro; IPR029646; CALB2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR19972:SF4; PTHR19972:SF4; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 5.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 5.
DR PROSITE; PS50222; EF_HAND_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..271
FT /note="Calretinin"
FT /id="PRO_0000073480"
FT DOMAIN 16..51
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 63..98
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 107..142
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 151..186
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 195..230
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 235..270
FT /note="EF-hand 6"
FT /evidence="ECO:0000305"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 214
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P47728"
SQ SEQUENCE 271 AA; 31373 MW; C6376AD7130DAACD CRC64;
MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK
SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSSA EFMEAWRKYD
TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL
PVQENFLLKF QGMKLTSEEF NAIFTFYDKD GSGYIDENEL DALLKDLYEK NKKEMNIQQL
TTYRKSVMSL AEAGKLYRKD LEIVLCSEPP V
