NCALD_BOVIN
ID NCALD_BOVIN Reviewed; 193 AA.
AC P61602; A1L533; P29554; Q0IIL3; Q9H0W2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Neurocalcin-delta;
GN Name=NCALD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 107-112 AND 121-126.
RC TISSUE=Brain;
RX PubMed=1599450; DOI=10.1016/s0006-291x(05)80968-4;
RA Okazaki K., Watanabe M., Ando Y., Hagiwara M., Terasawa M., Hidaka H.;
RT "Full sequence of neurocalcin, a novel calcium-binding protein abundant in
RT central nervous system.";
RL Biochem. Biophys. Res. Commun. 185:147-153(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8387172; DOI=10.1016/0168-0102(93)90074-z;
RA Hidaka H., Okazaki K.;
RT "Neurocalcin family: a novel calcium-binding protein abundant in bovine
RT central nervous system.";
RL Neurosci. Res. 16:73-77(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CALCIUM-BINDING, AND MYRISTOYLATION AT GLY-2.
RX PubMed=7852401; DOI=10.1016/s0021-9258(18)82908-8;
RA Ladant D.;
RT "Calcium and membrane binding properties of bovine neurocalcin delta
RT expressed in Escherichia coli.";
RL J. Biol. Chem. 270:3179-3185(1995).
RN [6]
RP CRYSTALLIZATION.
RX PubMed=8811741;
RX DOI=10.1002/(sici)1097-0134(199606)25:2<261::aid-prot11>3.0.co;2-h;
RA Kumar V.D., Hidaka H., Okazaki K., Vijay-Kumar S.;
RT "Crystallization and preliminary X-ray crystallographic studies of
RT recombinant bovine neurocalcin delta.";
RL Proteins 25:261-264(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9886296; DOI=10.1038/4956;
RA Vijay-Kumar S., Kumar V.D.;
RT "Crystal structure of recombinant bovine neurocalcin.";
RL Nat. Struct. Biol. 6:80-88(1999).
CC -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC rhodopsin phosphorylation. Binds three calcium ions.
CC -!- SUBUNIT: Interacts with GUCY2D. {ECO:0000250|UniProtKB:Q5PQN0}.
CC -!- INTERACTION:
CC P61602; P14100: PDE1A; NbExp=2; IntAct=EBI-908133, EBI-907809;
CC -!- TISSUE SPECIFICITY: Retina, cerebrum, cerebellum, brain stem, spinal
CC cord, testis, ovary and small intestine.
CC -!- MISCELLANEOUS: Five isoprotein forms of neurocalcin are designated
CC alpha, beta, gamma1, gamma2 and delta.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D10884; BAA01706.1; -; mRNA.
DR EMBL; BT029820; ABM06083.1; -; mRNA.
DR EMBL; BC122588; AAI22589.1; -; mRNA.
DR PIR; JH0616; JH0616.
DR RefSeq; NP_776823.1; NM_174398.2.
DR RefSeq; XP_005215666.1; XM_005215609.3.
DR RefSeq; XP_005215667.1; XM_005215610.3.
DR RefSeq; XP_005215670.1; XM_005215613.3.
DR RefSeq; XP_010810465.1; XM_010812163.2.
DR RefSeq; XP_015329999.1; XM_015474513.1.
DR PDB; 1BJF; X-ray; 2.40 A; A/B=1-193.
DR PDBsum; 1BJF; -.
DR AlphaFoldDB; P61602; -.
DR SMR; P61602; -.
DR IntAct; P61602; 2.
DR STRING; 9913.ENSBTAP00000038404; -.
DR iPTMnet; P61602; -.
DR PaxDb; P61602; -.
DR PRIDE; P61602; -.
DR Ensembl; ENSBTAT00000038591; ENSBTAP00000038404; ENSBTAG00000026963.
DR Ensembl; ENSBTAT00000068404; ENSBTAP00000069878; ENSBTAG00000026963.
DR GeneID; 281940; -.
DR KEGG; bta:281940; -.
DR CTD; 83988; -.
DR VEuPathDB; HostDB:ENSBTAG00000026963; -.
DR VGNC; VGNC:31897; NCALD.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158862; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P61602; -.
DR OMA; MGCVCMK; -.
DR OrthoDB; 1369072at2759; -.
DR TreeFam; TF300009; -.
DR Reactome; R-BTA-451308; Activation of Ca-permeable Kainate Receptor.
DR EvolutionaryTrace; P61602; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000026963; Expressed in occipital lobe and 103 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Lipoprotein;
KW Metal-binding; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..193
FT /note="Neurocalcin-delta"
FT /id="PRO_0000073781"
FT DOMAIN 40..58
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 144..179
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:7852401"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:1BJF"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1BJF"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1BJF"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1BJF"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:1BJF"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:1BJF"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:1BJF"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1BJF"
SQ SEQUENCE 193 AA; 22245 MW; 20DD8B6FF47C4CBF CRC64;
MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD
ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE
MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV
RLLQCDPSSA GQF
