CALB2_RAT
ID CALB2_RAT Reviewed; 271 AA.
AC P47728;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Calretinin;
DE Short=CR;
GN Name=Calb2;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7918640; DOI=10.1016/0167-4781(94)90069-8;
RA Strauss K.I., Jacobowitz D.M.;
RT "Calretinin is expressed in the Leydig cells of rat testis.";
RL Biochim. Biophys. Acta 1219:435-440(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 83-103; 134-141; 152-161; 171-178 AND 246-255, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1988053; DOI=10.1021/bi00217a010;
RA Gabrielides C., McCormack A.L., Hunt D.F., Christakos S.;
RT "Brain calbindin-D28k and an Mr 29,000 calcium binding protein in
RT cerebellum are different but related proteins: evidence obtained from
RT sequence analysis by tandem mass spectrometry.";
RL Biochemistry 30:656-662(1991).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; X66974; CAA47385.1; -; mRNA.
DR EMBL; BC087603; AAH87603.1; -; mRNA.
DR PIR; S25006; S25006.
DR RefSeq; NP_446440.1; NM_053988.1.
DR AlphaFoldDB; P47728; -.
DR SMR; P47728; -.
DR IntAct; P47728; 1.
DR STRING; 10116.ENSRNOP00000022943; -.
DR iPTMnet; P47728; -.
DR PhosphoSitePlus; P47728; -.
DR SwissPalm; P47728; -.
DR World-2DPAGE; 0004:P47728; -.
DR PaxDb; P47728; -.
DR PRIDE; P47728; -.
DR ABCD; P47728; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000022943; ENSRNOP00000022943; ENSRNOG00000016977.
DR GeneID; 117059; -.
DR KEGG; rno:117059; -.
DR UCSC; RGD:620981; rat.
DR CTD; 794; -.
DR RGD; 620981; Calb2.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000183108; -.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; P47728; -.
DR OMA; WSHYDRD; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; P47728; -.
DR TreeFam; TF325083; -.
DR PRO; PR:P47728; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000016977; Expressed in ovary and 10 other tissues.
DR Genevisible; P47728; RN.
DR GO; GO:0032437; C:cuticular plate; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005921; C:gap junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0097060; C:synaptic membrane; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; ISO:RGD.
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_0000073481"
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:0007744|PubMed:22673903"
SQ SEQUENCE 271 AA; 31405 MW; D2676AD7130DAACD 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 M
