NCALD_MOUSE
ID NCALD_MOUSE Reviewed; 193 AA.
AC Q91X97; Q3TJS9; Q8BZN9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Neurocalcin-delta;
GN Name=Ncald; Synonyms=D15Ertd412e;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Head, and Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Salivary gland;
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 [3]
RP PROTEIN SEQUENCE OF 51-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Lung;
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: May be involved in the calcium-dependent regulation of
CC rhodopsin phosphorylation. Binds three calcium ions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GUCY2D. {ECO:0000250|UniProtKB:Q5PQN0}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AK034031; BAC28553.1; -; mRNA.
DR EMBL; AK048440; BAC33338.1; -; mRNA.
DR EMBL; AK167313; BAE39416.1; -; mRNA.
DR EMBL; BC011162; AAH11162.1; -; mRNA.
DR EMBL; BC026979; AAH26979.1; -; mRNA.
DR CCDS; CCDS27435.1; -.
DR RefSeq; NP_001164337.1; NM_001170866.1.
DR RefSeq; NP_001164338.1; NM_001170867.1.
DR RefSeq; NP_001164339.1; NM_001170868.1.
DR RefSeq; NP_598855.2; NM_134094.4.
DR RefSeq; XP_006520170.1; XM_006520107.3.
DR RefSeq; XP_006520171.1; XM_006520108.1.
DR RefSeq; XP_006520172.1; XM_006520109.2.
DR RefSeq; XP_006520174.1; XM_006520111.3.
DR RefSeq; XP_006520175.1; XM_006520112.3.
DR RefSeq; XP_006520176.1; XM_006520113.3.
DR RefSeq; XP_011243664.1; XM_011245362.2.
DR RefSeq; XP_011243665.1; XM_011245363.2.
DR RefSeq; XP_011243666.1; XM_011245364.2.
DR RefSeq; XP_011243667.1; XM_011245365.2.
DR RefSeq; XP_011243668.1; XM_011245366.2.
DR RefSeq; XP_017172180.1; XM_017316691.1.
DR RefSeq; XP_017172181.1; XM_017316692.1.
DR RefSeq; XP_017172182.1; XM_017316693.1.
DR RefSeq; XP_017172183.1; XM_017316694.1.
DR RefSeq; XP_017172184.1; XM_017316695.1.
DR RefSeq; XP_017172185.1; XM_017316696.1.
DR RefSeq; XP_017172186.1; XM_017316697.1.
DR AlphaFoldDB; Q91X97; -.
DR SMR; Q91X97; -.
DR BioGRID; 206679; 5.
DR IntAct; Q91X97; 1.
DR STRING; 10090.ENSMUSP00000087611; -.
DR iPTMnet; Q91X97; -.
DR PhosphoSitePlus; Q91X97; -.
DR MaxQB; Q91X97; -.
DR PaxDb; Q91X97; -.
DR PeptideAtlas; Q91X97; -.
DR PRIDE; Q91X97; -.
DR ProteomicsDB; 287618; -.
DR Antibodypedia; 42836; 178 antibodies from 27 providers.
DR DNASU; 52589; -.
DR Ensembl; ENSMUST00000090150; ENSMUSP00000087611; ENSMUSG00000051359.
DR Ensembl; ENSMUST00000116445; ENSMUSP00000112146; ENSMUSG00000051359.
DR Ensembl; ENSMUST00000119730; ENSMUSP00000113858; ENSMUSG00000051359.
DR Ensembl; ENSMUST00000120746; ENSMUSP00000112898; ENSMUSG00000051359.
DR Ensembl; ENSMUST00000168992; ENSMUSP00000130126; ENSMUSG00000051359.
DR GeneID; 52589; -.
DR KEGG; mmu:52589; -.
DR UCSC; uc007vng.2; mouse.
DR CTD; 83988; -.
DR MGI; MGI:1196326; Ncald.
DR VEuPathDB; HostDB:ENSMUSG00000051359; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158862; -.
DR InParanoid; Q91X97; -.
DR OMA; MGCVCMK; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; Q91X97; -.
DR TreeFam; TF300009; -.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR BioGRID-ORCS; 52589; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ncald; mouse.
DR PRO; PR:Q91X97; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91X97; protein.
DR Bgee; ENSMUSG00000051359; Expressed in lateral septal nucleus and 252 other tissues.
DR ExpressionAtlas; Q91X97; baseline and differential.
DR Genevisible; Q91X97; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:MGI.
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 Calcium; Direct protein sequencing; Lipoprotein; Metal-binding; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..193
FT /note="Neurocalcin-delta"
FT /id="PRO_0000073783"
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:0000250"
FT CONFLICT 151
FT /note="K -> N (in Ref. 2; AAH11162)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="D -> N (in Ref. 1; BAC28553)"
FT /evidence="ECO:0000305"
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
