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NECA1_MOUSE
ID   NECA1_MOUSE             Reviewed;         352 AA.
AC   Q8BG18; Q80W91;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=N-terminal EF-hand calcium-binding protein 1;
DE            Short=EF-hand calcium-binding protein 1;
GN   Name=Necab1; Synonyms=Efcbp1;
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 [MRNA].
RC   STRAIN=Kunming;
RA   Wu H., Yu L., Li D.;
RT   "Cloning and characterization of human and mouse NECAB1.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Liver, and Spinal cord;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=12044471; DOI=10.1016/s0306-4522(02)00063-5;
RA   Sugita S., Ho A., Suedhof T.C.;
RT   "NECABs: a family of neuronal Ca(2+)-binding proteins with an unusual
RT   domain structure and a restricted expression pattern.";
RL   Neuroscience 112:51-63(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-197, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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   -!- SUBUNIT: Interacts with STX1. May interact with CPNE6.
CC       {ECO:0000250|UniProtKB:Q8N987}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12044471}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain (at protein level). Expressed in
CC       the cerebral cortex only in layer 4, thalamic nuclei (the mediodorsal
CC       nucleus), hippocampus (a small band of pyramidal neurons at the
CC       boundary between CA1 and CA3), interneurons interspersed throughout the
CC       hippocampus proper, interneurons in the hilus, bodies of the neurons
CC       but also their dendritic projections (at protein level).
CC       {ECO:0000269|PubMed:12044471}.
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DR   EMBL; AY278200; AAP32077.1; -; mRNA.
DR   EMBL; AK039240; BAC30290.1; -; mRNA.
DR   EMBL; AK050307; BAC34179.1; -; mRNA.
DR   EMBL; AK081951; BAC38379.1; -; mRNA.
DR   EMBL; AL732571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL831792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC067055; AAH67055.1; -; mRNA.
DR   CCDS; CCDS17982.1; -.
DR   RefSeq; NP_848732.3; NM_178617.4.
DR   AlphaFoldDB; Q8BG18; -.
DR   BioGRID; 213379; 1.
DR   STRING; 10090.ENSMUSP00000038165; -.
DR   iPTMnet; Q8BG18; -.
DR   PhosphoSitePlus; Q8BG18; -.
DR   MaxQB; Q8BG18; -.
DR   PaxDb; Q8BG18; -.
DR   PRIDE; Q8BG18; -.
DR   ProteomicsDB; 252800; -.
DR   Antibodypedia; 6629; 209 antibodies from 21 providers.
DR   DNASU; 69352; -.
DR   Ensembl; ENSMUST00000041606; ENSMUSP00000038165; ENSMUSG00000040536.
DR   Ensembl; ENSMUST00000108273; ENSMUSP00000103908; ENSMUSG00000040536.
DR   GeneID; 69352; -.
DR   KEGG; mmu:69352; -.
DR   UCSC; uc008sbi.2; mouse.
DR   CTD; 64168; -.
DR   MGI; MGI:1916602; Necab1.
DR   VEuPathDB; HostDB:ENSMUSG00000040536; -.
DR   eggNOG; ENOG502QWRY; Eukaryota.
DR   GeneTree; ENSGT00950000183131; -.
DR   HOGENOM; CLU_041553_0_0_1; -.
DR   InParanoid; Q8BG18; -.
DR   OMA; EVLLIQW; -.
DR   OrthoDB; 924307at2759; -.
DR   PhylomeDB; Q8BG18; -.
DR   TreeFam; TF331029; -.
DR   BioGRID-ORCS; 69352; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Necab1; mouse.
DR   PRO; PR:Q8BG18; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8BG18; protein.
DR   Bgee; ENSMUSG00000040536; Expressed in medial dorsal nucleus of thalamus and 72 other tissues.
DR   Genevisible; Q8BG18; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0042984; P:regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR039862; NECAB1/2/3.
DR   PANTHER; PTHR12178; PTHR12178; 1.
DR   Pfam; PF03992; ABM; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51725; ABM; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..352
FT                   /note="N-terminal EF-hand calcium-binding protein 1"
FT                   /id="PRO_0000282610"
FT   DOMAIN          26..61
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          252..340
FT                   /note="ABM"
FT   REGION          155..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          135..163
FT                   /evidence="ECO:0000255"
FT   COILED          209..275
FT                   /evidence="ECO:0000255"
FT   BINDING         39
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         41
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESB5"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        244
FT                   /note="E -> G (in Ref. 1; AAP32077)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  40934 MW;  D2B069AA7BA97036 CRC64;
     MEDSRETSPS SNNSSEELSS TLQLSKGMSI FLDILRRADK NDDGKLSFEE FKAYFADGVL
     SGEELHELFH TIDTHNTNNL DTEELCEYFS QHLGEYENVL AALEDLNLSI LKAMGKTKKD
     YQEASNLEQF VTRFLLKETL NQLQSLQNSL ECAMETTEEQ TRQERQGPSK PEVLSIQWPG
     KRSSRRVQRH NSFSPNSPQF NVSSPALLEE DNQWMTQINR LQKLIDRLEK KDLKLEPLEE
     EIIEENTKPH IMLVQRQMSV TEEDLEEFQL ALKHYVESAS AQSGCLRISI QKLSNESRYM
     IYEFWENSSV WNRHLQTNYS KTFQRSNVDF LETPELTSTM LVPASWWILN NN
 
 
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