CALB1_MOUSE
ID CALB1_MOUSE Reviewed; 261 AA.
AC P12658; Q545N6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Calbindin;
DE AltName: Full=Calbindin D28;
DE AltName: Full=D-28K;
DE AltName: Full=PCD-29;
DE AltName: Full=Spot 35 protein;
DE AltName: Full=Vitamin D-dependent calcium-binding protein, avian-type;
GN Name=Calb1;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=3199205; DOI=10.1523/jneurosci.08-12-04780.1988;
RA Nordquist D.T., Kozak C.A., Orr H.T.;
RT "cDNA cloning and characterization of three genes uniquely expressed in
RT cerebellum by Purkinje neurons.";
RL J. Neurosci. 8:4780-4789(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7980557; DOI=10.1006/bbrc.1994.2543;
RA Takeda T., Arakawa M., Kuwano R.;
RT "Organization and expression of the mouse spot35/calbindin-D28k gene:
RT identification of the vitamin D-responsive promoter region.";
RL Biochem. Biophys. Res. Commun. 204:889-897(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 35-47; 170-180; 222-235 AND 237-246, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 102-261.
RX PubMed=2465881; DOI=10.1089/dna.1988.7.585;
RA Wood T.L., Kobayashi Y., Frantz G., Varghese S., Christakos S., Tobin A.J.;
RT "Molecular cloning of mammalian 28,000 Mr vitamin D-dependent calcium
RT binding protein (calbindin-D28K): expression of calbindin-D28K RNAs in
RT rodent brain and kidney.";
RL DNA 7:585-593(1988).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17977745; DOI=10.1016/j.mcn.2007.09.006;
RA Saul S.M., Brzezinski J.A. IV, Altschuler R.A., Shore S.E., Rudolph D.D.,
RA Kabara L.L., Halsey K.E., Hufnagel R.B., Zhou J., Dolan D.F., Glaser T.;
RT "Math5 expression and function in the central auditory system.";
RL Mol. Cell. Neurosci. 37:153-169(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Liver;
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: 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 -!- TISSUE SPECIFICITY: Expressed in the modiolar nerve root and in bushy
CC neurons in the ventral cochlear nucleus (at protein level).
CC {ECO:0000269|PubMed:17977745}.
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; M21531; AAA39898.1; -; mRNA.
DR EMBL; D26352; BAA05386.1; -; Genomic_DNA.
DR EMBL; AK002635; BAB22249.1; -; mRNA.
DR EMBL; AK005081; BAB23805.1; -; mRNA.
DR EMBL; AK005243; BAB23900.1; -; mRNA.
DR EMBL; AK028050; BAC25721.1; -; mRNA.
DR EMBL; AK048517; BAC33354.1; -; mRNA.
DR EMBL; AK077499; BAC36831.1; -; mRNA.
DR EMBL; BC016421; AAH16421.1; -; mRNA.
DR EMBL; M23663; AAA53198.1; -; mRNA.
DR CCDS; CCDS17984.1; -.
DR PIR; A34955; A34955.
DR RefSeq; NP_033918.1; NM_009788.4.
DR AlphaFoldDB; P12658; -.
DR SMR; P12658; -.
DR BioGRID; 198449; 6.
DR STRING; 10090.ENSMUSP00000029876; -.
DR iPTMnet; P12658; -.
DR PhosphoSitePlus; P12658; -.
DR jPOST; P12658; -.
DR MaxQB; P12658; -.
DR PaxDb; P12658; -.
DR PeptideAtlas; P12658; -.
DR PRIDE; P12658; -.
DR ProteomicsDB; 273829; -.
DR ABCD; P12658; 2 sequenced antibodies.
DR Antibodypedia; 3678; 482 antibodies from 45 providers.
DR DNASU; 12307; -.
DR Ensembl; ENSMUST00000029876; ENSMUSP00000029876; ENSMUSG00000028222.
DR GeneID; 12307; -.
DR KEGG; mmu:12307; -.
DR UCSC; uc008sbl.1; mouse.
DR CTD; 793; -.
DR MGI; MGI:88248; Calb1.
DR VEuPathDB; HostDB:ENSMUSG00000028222; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000183108; -.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; P12658; -.
DR OMA; EEFMQTW; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; P12658; -.
DR TreeFam; TF325083; -.
DR BioGRID-ORCS; 12307; 0 hits in 73 CRISPR screens.
DR PRO; PR:P12658; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P12658; protein.
DR Bgee; ENSMUSG00000028222; Expressed in molar tooth and 160 other tissues.
DR Genevisible; P12658; MM.
DR GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0032437; C:cuticular plate; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IMP:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0032420; C:stereocilium; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:SynGO.
DR GO; GO:0099567; F:calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0072205; P:metanephric collecting duct development; IEP:UniProtKB.
DR GO; GO:0072286; P:metanephric connecting tubule development; IEP:UniProtKB.
DR GO; GO:0072221; P:metanephric distal convoluted tubule development; IEP:UniProtKB.
DR GO; GO:0035502; P:metanephric part of ureteric bud development; IEP:UniProtKB.
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; IMP:SynGO.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; IEP:UniProtKB.
DR GO; GO:0007614; P:short-term memory; ISO:MGI.
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 Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Reference proteome; Repeat; Vitamin D.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04467"
FT CHAIN 2..261
FT /note="Calbindin"
FT /id="PRO_0000073473"
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:0000250|UniProtKB:P04467"
SQ SEQUENCE 261 AA; 29994 MW; BCC600FD1A86AF3D CRC64;
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELLQARKKA GLELSPEMKS
FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET
EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK
FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQELDINN ITTYKKNIMA
LSDGGKLYRT DLALILSAGD N
