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Calbindin (Calbindin D28) (D-28K) (Spot 35 protein) (Vitamin D-dependent calcium-binding protein, avian-type)

 CALB1_RAT               Reviewed;         261 AA.
P07171;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 155.
RecName: Full=Calbindin;
AltName: Full=Calbindin D28;
AltName: Full=D-28K;
AltName: Full=Spot 35 protein;
AltName: Full=Vitamin D-dependent calcium-binding protein, avian-type;
Name=Calb1;
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].
TISSUE=Brain;
PubMed=3755822; DOI=10.1093/nar/14.16.6768;
Yamakuni T., Kuwano R., Odani S., Miki N., Yamaguchi Y., Takahashi Y.;
"Nucleotide sequence of cDNA to mRNA for a cerebellar Ca-binding
protein, spot 35 protein.";
Nucleic Acids Res. 14:6768-6768(1986).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=2843757; DOI=10.1210/mend-2-5-465;
Hunziker W., Schrickel S.;
"Rat brain calbindin D28: six domain structure and extensive amino
acid homology with chicken calbindin D28.";
Mol. Endocrinol. 2:465-473(1988).
[3]
NUCLEOTIDE SEQUENCE.
TISSUE=Brain;
PubMed=3049577;
Gross M.D., Kumar R., Hunziker W.;
"Expression in Escherichia coli of full-length and mutant rat brain
calbindin D28. Comparison with the purified native protein.";
J. Biol. Chem. 263:14426-14432(1988).
[4]
NUCLEOTIDE SEQUENCE.
TISSUE=Cerebellum;
PubMed=3031218; DOI=10.1111/j.1471-4159.1987.tb05706.x;
Yamakuni T., Kuwano R., Odani S., Miki N., Yamaguchi K., Takahashi Y.;
"Molecular cloning of cDNA to mRNA for a cerebellar spot 35 protein.";
J. Neurochem. 48:1590-1596(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=2792772; DOI=10.1016/0378-1119(89)90253-9;
Lomri N.E., Perret C., Gouhier N., Thomasset M.;
"Cloning and analysis of calbindin-D28K cDNA and its expression in the
central nervous system.";
Gene 80:87-98(1989).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 73-93; 143-152; 222-235 AND 237-246, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Diao W.;
Submitted (APR-2007) to UniProtKB.
[8]
PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=1988053; DOI=10.1021/bi00217a010;
Gabrielides C., McCormack A.L., Hunt D.F., Christakos S.;
"Brain calbindin-D28k and an Mr 29,000 calcium binding protein in
cerebellum are different but related proteins: evidence obtained from
sequence analysis by tandem mass spectrometry.";
Biochemistry 30:656-662(1991).
[9]
STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS.
PubMed=16799559; DOI=10.1038/nsmb1112;
Kojetin D.J., Venters R.A., Kordys D.R., Thompson R.J., Kumar R.,
Cavanagh J.;
"Structure, binding interface and hydrophobic transitions of Ca2+-
loaded calbindin-D(28K).";
Nat. Struct. Mol. Biol. 13:641-647(2006).
-!- FUNCTION: Buffers cytosolic calcium. May stimulate a membrane
Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
-!- SUBUNIT: Interacts with RANBP9. {ECO:0000250}.
-!- DOMAIN: This protein has four functional calcium-binding sites;
potential sites II and VI have lost affinity for calcium.
-!- SIMILARITY: Belongs to the calbindin family. {ECO:0000305}.
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EMBL; M31178; AAA40851.1; -; mRNA.
EMBL; X04280; CAA27828.1; -; mRNA.
EMBL; M27839; AAA40852.1; -; Genomic_DNA.
EMBL; BC081764; AAH81764.1; -; mRNA.
PIR; A30808; KLRTB.
RefSeq; NP_114190.1; NM_031984.2.
UniGene; Rn.3908; -.
PDB; 2F33; NMR; -; A=1-261.
PDB; 2G9B; NMR; -; A=1-261.
PDBsum; 2F33; -.
PDBsum; 2G9B; -.
ProteinModelPortal; P07171; -.
SMR; P07171; -.
STRING; 10116.ENSRNOP00000010845; -.
iPTMnet; P07171; -.
PhosphoSitePlus; P07171; -.
PaxDb; P07171; -.
PRIDE; P07171; -.
Ensembl; ENSRNOT00000010845; ENSRNOP00000010845; ENSRNOG00000007456.
GeneID; 83839; -.
KEGG; rno:83839; -.
UCSC; RGD:69340; rat.
CTD; 793; -.
RGD; 69340; Calb1.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00390000013118; -.
HOGENOM; HOG000231866; -.
HOVERGEN; HBG000855; -.
InParanoid; P07171; -.
KO; K14757; -.
OMA; MQTWRKY; -.
OrthoDB; EOG091G0GNH; -.
PhylomeDB; P07171; -.
TreeFam; TF325083; -.
EvolutionaryTrace; P07171; -.
PRO; PR:P07171; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000007456; -.
Genevisible; P07171; RN.
GO; GO:0030424; C:axon; IDA:BHF-UCL.
GO; GO:0044297; C:cell body; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0043005; C:neuron projection; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0045202; C:synapse; ISO:RGD.
GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; IC:SynGO.
GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
GO; GO:0007611; P:learning or memory; IEP:RGD.
GO; GO:0007626; P:locomotory behavior; ISO:RGD.
GO; GO:0007616; P:long-term memory; ISO:RGD.
GO; GO:0072205; P:metanephric collecting duct development; ISO:RGD.
GO; GO:0072286; P:metanephric connecting tubule development; ISO:RGD.
GO; GO:0072221; P:metanephric distal convoluted tubule development; ISO:RGD.
GO; GO:0035502; P:metanephric part of ureteric bud development; ISO:RGD.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:RGD.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISO:RGD.
GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IMP:SynGO.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:RGD.
GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
GO; GO:0010842; P:retina layer formation; ISO:RGD.
GO; GO:0007614; P:short-term memory; ISO:RGD.
GO; GO:0042359; P:vitamin D metabolic process; TAS:RGD.
InterPro; IPR029634; Calbindin.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
PANTHER; PTHR19972:SF3; PTHR19972:SF3; 1.
Pfam; PF13405; EF-hand_6; 1.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 2.
PROSITE; PS00018; EF_HAND_1; 4.
PROSITE; PS50222; EF_HAND_2; 5.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome;
Direct protein sequencing; Metal-binding; Reference proteome; Repeat;
Vitamin D.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1988053}.
CHAIN 2 261 Calbindin.
/FTId=PRO_0000073475.
DOMAIN 11 46 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 53 88 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 98 133 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 142 177 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 186 221 EF-hand 5. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 24 35 1.
CA_BIND 111 122 2.
CA_BIND 155 166 3.
CA_BIND 199 210 4.
REGION 2 7 Interaction with RANBP9. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:1988053}.
CONFLICT 139 139 D -> H (in Ref. 5; AAA40852).
{ECO:0000305}.
HELIX 2 5 {ECO:0000244|PDB:2F33}.
TURN 6 8 {ECO:0000244|PDB:2F33}.
HELIX 13 23 {ECO:0000244|PDB:2F33}.
STRAND 28 31 {ECO:0000244|PDB:2F33}.
HELIX 34 50 {ECO:0000244|PDB:2F33}.
HELIX 56 65 {ECO:0000244|PDB:2F33}.
HELIX 68 70 {ECO:0000244|PDB:2F33}.
HELIX 75 81 {ECO:0000244|PDB:2F33}.
HELIX 88 92 {ECO:0000244|PDB:2F33}.
HELIX 93 95 {ECO:0000244|PDB:2F33}.
HELIX 100 107 {ECO:0000244|PDB:2F33}.
TURN 112 114 {ECO:0000244|PDB:2F33}.
STRAND 116 118 {ECO:0000244|PDB:2F33}.
HELIX 120 134 {ECO:0000244|PDB:2F33}.
HELIX 140 153 {ECO:0000244|PDB:2F33}.
STRAND 156 160 {ECO:0000244|PDB:2F33}.
HELIX 164 170 {ECO:0000244|PDB:2F33}.
TURN 173 175 {ECO:0000244|PDB:2F33}.
HELIX 178 183 {ECO:0000244|PDB:2F33}.
HELIX 188 198 {ECO:0000244|PDB:2F33}.
STRAND 201 204 {ECO:0000244|PDB:2F33}.
HELIX 208 221 {ECO:0000244|PDB:2F33}.
TURN 223 225 {ECO:0000244|PDB:2F33}.
TURN 228 230 {ECO:0000244|PDB:2F33}.
HELIX 231 239 {ECO:0000244|PDB:2F33}.
HELIX 249 251 {ECO:0000244|PDB:2F33}.
HELIX 253 256 {ECO:0000244|PDB:2F33}.
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


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