NECA3_MOUSE
ID NECA3_MOUSE Reviewed; 353 AA.
AC Q9D6J4; A1L0S0; A1L0S1; A2AKE8; A2AKE9; Q3TYZ9; Q9ESR0;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=N-terminal EF-hand calcium-binding protein 3;
DE AltName: Full=Amyloid-beta A4 protein-binding family A member 2-binding protein;
DE AltName: Full=X11L-binding protein 51;
DE Short=mXB51;
GN Name=Necab3; Synonyms=Apba2bp, Xb51;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Inner ear, and Retina;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-353 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10833507; DOI=10.1074/jbc.c000302200;
RA Lee D.-S., Tomita S., Kirino Y., Suzuki T.;
RT "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51,
RT a novel X11L-binding protein.";
RL J. Biol. Chem. 275:23134-23138(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-353 (ISOFORM 1).
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=14697346; DOI=10.1016/j.yexcr.2003.09.025;
RA Yoo J.C., Chang J.R., Kim S.H., Jang S.K., Wolgemuth D.J., Kim K., Rhee K.;
RT "NIP1/XB51/NECAB3 is a potential substrate of Nek2, suggesting specific
RT roles of Nek2 in Golgi.";
RL Exp. Cell Res. 292:393-402(2004).
CC -!- FUNCTION: Inhibits the interaction of APBA2 with amyloid-beta precursor
CC protein (APP), and hence allows formation of amyloid-beta (By
CC similarity). May enhance the activity of HIF1A and thus promote
CC glycolysis under normoxic conditions; the function requires its ABM
CC domain and may implicate the stabilization of the interaction between
CC HIF1AN and APBA3 (By similarity). {ECO:0000250|UniProtKB:Q96P71}.
CC -!- SUBUNIT: Interacts with the N-terminal domain of APBA2. Interacts with
CC NEK2 (By similarity). Interacts with APBA3; APBA3 seems to mediate the
CC interaction between NECAB3 and HIF1AN (By similarity).
CC {ECO:0000250|UniProtKB:Q96P71}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q96P71}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D6J4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6J4-2; Sequence=VSP_000740;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the brain.
CC {ECO:0000269|PubMed:14697346}.
CC -!- PTM: Phosphorylated by NEK2. {ECO:0000250|UniProtKB:Q96P71}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI26875.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI26876.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB16414.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK013520; BAB28895.1; -; mRNA.
DR EMBL; AK044296; BAC31859.1; -; mRNA.
DR EMBL; AK158225; BAE34411.1; -; mRNA.
DR EMBL; AL772292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06077.1; -; Genomic_DNA.
DR EMBL; CH466551; EDL06081.1; -; Genomic_DNA.
DR EMBL; AB039948; BAB16414.1; ALT_INIT; mRNA.
DR EMBL; BC126874; AAI26875.1; ALT_INIT; mRNA.
DR EMBL; BC126875; AAI26876.1; ALT_INIT; mRNA.
DR CCDS; CCDS50766.1; -. [Q9D6J4-1]
DR RefSeq; NP_067521.2; NM_021546.3. [Q9D6J4-1]
DR AlphaFoldDB; Q9D6J4; -.
DR STRING; 10090.ENSMUSP00000000895; -.
DR PhosphoSitePlus; Q9D6J4; -.
DR PaxDb; Q9D6J4; -.
DR PRIDE; Q9D6J4; -.
DR ProteomicsDB; 252875; -. [Q9D6J4-1]
DR ProteomicsDB; 252876; -. [Q9D6J4-2]
DR Antibodypedia; 25664; 142 antibodies from 26 providers.
DR DNASU; 56846; -.
DR Ensembl; ENSMUST00000000895; ENSMUSP00000000895; ENSMUSG00000027489. [Q9D6J4-1]
DR Ensembl; ENSMUST00000109716; ENSMUSP00000105338; ENSMUSG00000027489. [Q9D6J4-2]
DR GeneID; 56846; -.
DR KEGG; mmu:56846; -.
DR UCSC; uc008njh.1; mouse. [Q9D6J4-1]
DR UCSC; uc008nji.1; mouse. [Q9D6J4-2]
DR CTD; 63941; -.
DR MGI; MGI:1861721; Necab3.
DR VEuPathDB; HostDB:ENSMUSG00000027489; -.
DR eggNOG; ENOG502QWRY; Eukaryota.
DR GeneTree; ENSGT00950000183131; -.
DR HOGENOM; CLU_041553_3_0_1; -.
DR InParanoid; Q9D6J4; -.
DR OMA; EACFILY; -.
DR OrthoDB; 924307at2759; -.
DR PhylomeDB; Q9D6J4; -.
DR TreeFam; TF331029; -.
DR BioGRID-ORCS; 56846; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q9D6J4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D6J4; protein.
DR Bgee; ENSMUSG00000027489; Expressed in habenula and 95 other tissues.
DR ExpressionAtlas; Q9D6J4; baseline and differential.
DR Genevisible; Q9D6J4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; ISS:UniProtKB.
DR GO; GO:0042984; P:regulation of amyloid precursor protein biosynthetic process; ISO:MGI.
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; PF13202; EF-hand_5; 1.
DR SMART; SM00054; EFh; 1.
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; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Golgi apparatus; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..353
FT /note="N-terminal EF-hand calcium-binding protein 3"
FT /id="PRO_0000073864"
FT DOMAIN 27..62
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 253..342
FT /note="ABM"
FT REGION 172..181
FT /note="Required for interaction with APBA3"
FT /evidence="ECO:0000250|UniProtKB:Q96P71"
FT REGION 193..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 233..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000740"
FT CONFLICT 166
FT /note="R -> W (in Ref. 5; AAI26875)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="F -> C (in Ref. 1; BAB28895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39906 MW; 606C1D570FA36864 CRC64;
MACAGLLTVC LLGPPAPQQP RHSAPAAGHA LFQDVFRRAD KNDDGKLSFE EFQNYFADGV
LSSAELRELF SGIDDHLTDN LETEKLCDYF STHLGVYRPV LAALESLNRA VLTAMDTTKL
EYEQASKVDQ FVTRFLLRET VNQLQALQTS LEGASDTLEA QAHGQRLDEE TIKAQSRPCG
SRRAGRRALR SISWSPSWSP GSSDTGRSSE AEQQWRLQVN RLQELIDQLE CKAPRLEPTH
EEDLTKGFDS HILVAQRQVQ VAEDALQDFH RALCCYMNFT GAQSHCLHVS AQKMLDNAAF
TLYEFWQDEA SWRRHQQSPC SKAFQRTLID HLQAPDTLTT VFFPASWWIM NNN
