CALB1_CHICK
ID CALB1_CHICK Reviewed; 262 AA.
AC P04354;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Calbindin;
DE AltName: Full=Calbindin D28;
DE AltName: Full=D-28K;
DE AltName: Full=Vitamin D-dependent calcium-binding protein, avian-type;
GN Name=CALB1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3841205; DOI=10.1093/nar/13.24.8867;
RA Wilson P.W., Harding M., Lawson D.E.M.;
RT "Putative amino acid sequence of chick calcium-binding protein deduced from
RT a complementary DNA sequence.";
RL Nucleic Acids Res. 13:8867-8881(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3463988; DOI=10.1073/pnas.83.20.7578;
RA Hunziker W.;
RT "The 28-kDa vitamin D-dependent calcium-binding protein has a six-domain
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7578-7582(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2967915; DOI=10.1210/mend-2-4-355;
RA Minghetti P.P., Cancela L., Fujisawa Y., Theofan G., Norman A.W.;
RT "Molecular structure of the chicken vitamin D-induced calbindin-D28K gene
RT reveals eleven exons, six Ca2+-binding domains, and numerous promoter
RT regulatory elements.";
RL Mol. Endocrinol. 2:355-367(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3411606; DOI=10.1016/0022-2836(88)90475-5;
RA Wilson P.W., Rogers J.H., Harding M., Pohl V., Pattyn G., Lawson D.E.M.;
RT "Structure of chick chromosomal genes for calbindin and calretinin.";
RL J. Mol. Biol. 200:615-625(1988).
RN [5]
RP PROTEIN SEQUENCE OF 2-262, AND ACETYLATION AT THR-2.
RX PubMed=3474624; DOI=10.1073/pnas.84.14.4772;
RA Fullmer C.S., Wasserman R.H.;
RT "Chicken intestinal 28-kilodalton calbindin-D: complete amino acid sequence
RT and structural considerations.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4772-4776(1987).
RN [6]
RP TISSUE SPECIFICITY.
RC STRAIN=White leghorn;
RX PubMed=9736748; DOI=10.1073/pnas.95.19.11400;
RA Heller S., Sheane C.A., Javed Z., Hudspeth A.J.;
RT "Molecular markers for cell types of the inner ear and candidate genes for
RT hearing disorders.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11400-11405(1998).
CC -!- FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-
CC ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
CC -!- TISSUE SPECIFICITY: Highly abundant in supporting cells. Also present
CC in hair cells. {ECO:0000269|PubMed:9736748}.
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; X03343; CAA27049.1; -; mRNA.
DR EMBL; M14230; AAA48659.1; -; mRNA.
DR EMBL; M31143; AAA83832.1; -; Genomic_DNA.
DR EMBL; M31139; AAA83832.1; JOINED; Genomic_DNA.
DR EMBL; M31140; AAA83832.1; JOINED; Genomic_DNA.
DR EMBL; M31141; AAA83832.1; JOINED; Genomic_DNA.
DR EMBL; M31142; AAA83832.1; JOINED; Genomic_DNA.
DR EMBL; X06629; CAA29843.1; -; Genomic_DNA.
DR EMBL; X06630; CAA29843.1; JOINED; Genomic_DNA.
DR EMBL; X06631; CAA29843.1; JOINED; Genomic_DNA.
DR EMBL; X06632; CAA29843.1; JOINED; Genomic_DNA.
DR EMBL; X06633; CAA29843.1; JOINED; Genomic_DNA.
DR PIR; A40926; KLCHI.
DR RefSeq; NP_990844.1; NM_205513.1.
DR AlphaFoldDB; P04354; -.
DR SMR; P04354; -.
DR BioGRID; 676764; 1.
DR IntAct; P04354; 1.
DR STRING; 9031.ENSGALP00000026395; -.
DR iPTMnet; P04354; -.
DR PaxDb; P04354; -.
DR Ensembl; ENSGALT00000074265; ENSGALP00000056213; ENSGALG00000032282.
DR GeneID; 396519; -.
DR KEGG; gga:396519; -.
DR CTD; 793; -.
DR VEuPathDB; HostDB:geneid_396519; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000183108; -.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; P04354; -.
DR OMA; EEFMQTW; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; P04354; -.
DR TreeFam; TF325083; -.
DR PRO; PR:P04354; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000032282; Expressed in kidney and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0012506; C:vesicle membrane; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR GO; GO:0006816; P:calcium ion transport; TAS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS: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; IBA:GO_Central.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; NAS:UniProtKB.
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; PF13405; EF-hand_6; 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:0000269|PubMed:3474624"
FT CHAIN 2..262
FT /note="Calbindin"
FT /id="PRO_0000073476"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 54..89
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 99..134
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 143..178
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 187..222
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 211
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-acetylthreonine"
FT /evidence="ECO:0000305|PubMed:3474624"
SQ SEQUENCE 262 AA; 30167 MW; 52081141364F08A5 CRC64;
MTAETHLQGV EISAAQFFEI WHHYDSDGNG YMDGKELQNF IQELQQARKK AGLDLTPEMK
AFVDQYGKAT DGKIGIVELA QVLPTEENFL LFFRCQQLKS SEDFMQTWRK YDSDHSGFID
SEELKSFLKD LLQKANKQIE DSKLTEYTEI MLRMFDANND GKLELTELAR LLPVQENFLI
KFQGVKMCAK EFNKAFEMYD QDGNGYIDEN ELDALLKDLC EKNKKELDIN NLATYKKSIM
ALSDGGKLYR AELALILCAE EN
