CALB1_RAT
ID CALB1_RAT Reviewed; 261 AA.
AC P07171;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Calbindin;
DE AltName: Full=Calbindin D28;
DE AltName: Full=D-28K;
DE AltName: Full=Spot 35 protein;
DE AltName: Full=Vitamin D-dependent calcium-binding protein, avian-type;
GN Name=Calb1;
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 TISSUE=Brain;
RX PubMed=3755822; DOI=10.1093/nar/14.16.6768;
RA Yamakuni T., Kuwano R., Odani S., Miki N., Yamaguchi Y., Takahashi Y.;
RT "Nucleotide sequence of cDNA to mRNA for a cerebellar Ca-binding protein,
RT spot 35 protein.";
RL Nucleic Acids Res. 14:6768-6768(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2843757; DOI=10.1210/mend-2-5-465;
RA Hunziker W., Schrickel S.;
RT "Rat brain calbindin D28: six domain structure and extensive amino acid
RT homology with chicken calbindin D28.";
RL Mol. Endocrinol. 2:465-473(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain;
RX PubMed=3049577; DOI=10.1016/s0021-9258(18)68237-7;
RA Gross M.D., Kumar R., Hunziker W.;
RT "Expression in Escherichia coli of full-length and mutant rat brain
RT calbindin D28. Comparison with the purified native protein.";
RL J. Biol. Chem. 263:14426-14432(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum;
RX PubMed=3031218; DOI=10.1111/j.1471-4159.1987.tb05706.x;
RA Yamakuni T., Kuwano R., Odani S., Miki N., Yamaguchi K., Takahashi Y.;
RT "Molecular cloning of cDNA to mRNA for a cerebellar spot 35 protein.";
RL J. Neurochem. 48:1590-1596(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=2792772; DOI=10.1016/0378-1119(89)90253-9;
RA Lomri N.E., Perret C., Gouhier N., Thomasset M.;
RT "Cloning and analysis of calbindin-D28K cDNA and its expression in the
RT central nervous system.";
RL Gene 80:87-98(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP PROTEIN SEQUENCE OF 73-93; 143-152; 222-235 AND 237-246, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [9]
RP STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS.
RX PubMed=16799559; DOI=10.1038/nsmb1112;
RA Kojetin D.J., Venters R.A., Kordys D.R., Thompson R.J., Kumar R.,
RA Cavanagh J.;
RT "Structure, binding interface and hydrophobic transitions of Ca2+-loaded
RT calbindin-D(28K).";
RL Nat. Struct. Mol. Biol. 13:641-647(2006).
CC -!- FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-
CC ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
CC -!- SUBUNIT: Interacts with RANBP9. {ECO:0000250|UniProtKB:P05937}.
CC -!- DOMAIN: This protein has four functional calcium-binding sites;
CC potential sites II and VI have lost affinity for calcium.
CC {ECO:0000250|UniProtKB:P05937}.
CC -!- SIMILARITY: Belongs to the calbindin family. {ECO:0000305}.
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DR EMBL; M31178; AAA40851.1; -; mRNA.
DR EMBL; X04280; CAA27828.1; -; mRNA.
DR EMBL; M27839; AAA40852.1; -; Genomic_DNA.
DR EMBL; BC081764; AAH81764.1; -; mRNA.
DR PIR; A30808; KLRTB.
DR RefSeq; NP_114190.1; NM_031984.2.
DR PDB; 2F33; NMR; -; A=1-261.
DR PDB; 2G9B; NMR; -; A=1-261.
DR PDBsum; 2F33; -.
DR PDBsum; 2G9B; -.
DR AlphaFoldDB; P07171; -.
DR SMR; P07171; -.
DR BioGRID; 249865; 1.
DR IntAct; P07171; 1.
DR MINT; P07171; -.
DR STRING; 10116.ENSRNOP00000010845; -.
DR iPTMnet; P07171; -.
DR PhosphoSitePlus; P07171; -.
DR PaxDb; P07171; -.
DR PRIDE; P07171; -.
DR ABCD; P07171; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000010845; ENSRNOP00000010845; ENSRNOG00000007456.
DR GeneID; 83839; -.
DR KEGG; rno:83839; -.
DR UCSC; RGD:69340; rat.
DR CTD; 793; -.
DR RGD; 69340; Calb1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000183108; -.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; P07171; -.
DR OMA; EEFMQTW; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; P07171; -.
DR TreeFam; TF325083; -.
DR EvolutionaryTrace; P07171; -.
DR PRO; PR:P07171; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007456; Expressed in kidney and 16 other tissues.
DR Genevisible; P07171; RN.
DR GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0032437; C:cuticular plate; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0099567; F:calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0007611; P:learning or memory; IEP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
DR GO; GO:0072205; P:metanephric collecting duct development; ISO:RGD.
DR GO; GO:0072286; P:metanephric connecting tubule development; ISO:RGD.
DR GO; GO:0072221; P:metanephric distal convoluted tubule development; ISO:RGD.
DR GO; GO:0035502; P:metanephric part of ureteric bud development; 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; ISO:RGD.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0010842; P:retina layer formation; ISO:RGD.
DR GO; GO:0007614; P:short-term memory; ISO:RGD.
DR GO; GO:0042359; P:vitamin D metabolic process; TAS:RGD.
DR InterPro; IPR029634; Calbindin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR19972:SF14; PTHR19972:SF14; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat; Vitamin D.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1988053"
FT CHAIN 2..261
FT /note="Calbindin"
FT /id="PRO_0000073475"
FT DOMAIN 11..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 53..88
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 142..177
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 186..221
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 2..7
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250|UniProtKB:P05937"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
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 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1988053"
FT CONFLICT 139
FT /note="D -> H (in Ref. 5; AAA40852)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:2F33"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2F33"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 34..50
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2F33"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2F33"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:2F33"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:2F33"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2F33"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:2F33"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2F33"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2F33"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:2F33"
SQ SEQUENCE 261 AA; 29994 MW; B9C58D75C4D252C1 CRC64;
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELLQARKKA GLELSPEMKT
FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET
EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK
FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQELDINN ISTYKKNIMA
LSDGGKLYRT DLALILSAGD N
