CALB2_CHICK
ID CALB2_CHICK Reviewed; 269 AA.
AC P07090;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Calretinin;
DE Short=CR;
GN Name=CALB2;
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=8344307; DOI=10.1111/j.1432-1033.1993.tb18047.x;
RA Cheung W.T., Richards D.E., Rogers J.H.;
RT "Calcium binding by chick calretinin and rat calbindin D28k synthesised in
RT bacteria.";
RL Eur. J. Biochem. 215:401-410(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-194.
RX PubMed=3654755; DOI=10.1083/jcb.105.3.1343;
RA Rogers J.H.;
RT "Calretinin: a gene for a novel calcium-binding protein expressed
RT principally in neurons.";
RL J. Cell Biol. 105:1343-1353(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-207.
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).
CC -!- FUNCTION: Calretinin is a calcium-binding protein which is abundant in
CC auditory neurons.
CC -!- SIMILARITY: Belongs to the calbindin family. {ECO:0000305}.
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DR EMBL; X62866; CAA44666.1; -; mRNA.
DR EMBL; Y00625; CAA68664.1; -; mRNA.
DR PIR; S34773; A27067.
DR RefSeq; NP_990647.1; NM_205316.1.
DR AlphaFoldDB; P07090; -.
DR SMR; P07090; -.
DR BioGRID; 676515; 1.
DR IntAct; P07090; 1.
DR STRING; 9031.ENSGALP00000041715; -.
DR PaxDb; P07090; -.
DR GeneID; 396255; -.
DR KEGG; gga:396255; -.
DR CTD; 794; -.
DR VEuPathDB; HostDB:geneid_396255; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; P07090; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; P07090; -.
DR PRO; PR:P07090; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; 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:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..269
FT /note="Calretinin"
FT /id="PRO_0000073478"
FT DOMAIN 14..49
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 61..96
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 105..140
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 149..184
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 193..228
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 230..265
FT /note="EF-hand 6"
FT /evidence="ECO:0000305"
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 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 129
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="4"
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 173
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="5"
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 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 269 AA; 31077 MW; C6A723A04C4EE315 CRC64;
MAGQRAPHLH LAELSASQFL DVWRHFDADG NGYIEGKELE NFFQELESAR KGTGVDSKRD
SLGDKMKEFM HKYDKNADGK IEMAELAQIL PTEENFLLCF RQHVGSSSEF MEAWRRYDTD
RSGYIEANEL KGFLSDLLKK ANRPYDEAKL QEYTQTILRM FDMNGDGKLG LSEMSRLLPV
QENFLLKFQG MKLSSEEFNA IFAFYDKDGS GFIDEHELDA LLKDLYEKNK KEMSIQQLTN
YRRSIMNLSD GGKLYRKELE VVLCSEPPL
