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 04-NOV-2026, entry version 153. 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. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001346840.1; NM_001359911.1. DR RefSeq; NP_001346841.1; NM_001359912.1. DR RefSeq; NP_776823.1; NM_174398.3. DR RefSeq; XP_005215670.1; XM_005215613.5. DR RefSeq; XP_015329999.1; XM_015474513.3. DR RefSeq; XP_024857174.1; XM_025001406.2. DR RefSeq; XP_024857175.1; XM_025001407.2. DR RefSeq; XP_024857176.1; XM_025001408.2. DR RefSeq; XP_024857177.1; XM_025001409.2. DR RefSeq; XP_059749108.1; XM_059893125.1. DR PDB; 1BJF; X-ray; 2.40 A; A/B=1-193. DR AlphaFoldDB; P61602; -. DR SMR; P61602; -. DR FunCoup; P61602; 802. DR IntAct; P61602; 2. DR STRING; 9913.ENSBTAP00000069878; -. DR iPTMnet; P61602; -. DR PaxDb; 9913-ENSBTAP00000069878; -. DR Ensembl; ENSBTAT00000068404.2; ENSBTAP00000069878.1; ENSBTAG00000026963.7. DR Ensembl; ENSBTAT00085004357; ENSBTAP00085024730; ENSBTAG00085023074. DR Ensembl; ENSBTAT00090036339; ENSBTAP00090018633; ENSBTAG00090018040. 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; ACMKQRQ; -. DR OrthoDB; 191686at2759; -. 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 cell types or tissues. DR ExpressionAtlas; P61602; baseline. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. 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:0009966; P:regulation of signal transduction; IBA:GO_Central. DR CDD; cd00051; EFh; 2. DR FunFam; 1.10.238.10:FF:000009; Visinin-like protein 1; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. 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; CALCIUM BINDING PROTEINS; 1. DR PANTHER; PTHR23055:SF87; NEUROCALCIN-DELTA; 1. DR Pfam; PF00036; EF-hand_1; 1. DR Pfam; PF13499; EF-hand_7; 1. DR PRINTS; PR00450; RECOVERIN. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 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 //