LOCUS       NP_061228                571 aa            linear   ROD 05-MAY-2025
DEFINITION  amyloid-beta A4 precursor protein-binding family A member 3 isoform
            a [Mus musculus].
ACCESSION   NP_061228
VERSION     NP_061228.1
DBSOURCE    REFSEQ: accession NM_018758.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Uematsu,T., Tsuchiya,K., Kobayashi,N., Seiki,M., Inoue,J.I.,
            Kaneko,S. and Sakamoto,T.
  TITLE     Mint3 depletion-mediated glycolytic and oxidative alterations
            promote pyroptosis and prevent the spread of Listeria monocytogenes
            infection in macrophages
  JOURNAL   Cell Death Dis 12 (4), 404 (2021)
   PUBMED   33854054
  REMARK    GeneRIF: Mint3 depletion-mediated glycolytic and oxidative
            alterations promote pyroptosis and prevent the spread of Listeria
            monocytogenes infection in macrophages.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Lin,A.Y., Henry,S., Reissner,C., Neupert,C., Kenny,C., Missler,M.,
            Beffert,U. and Ho,A.
  TITLE     A rare autism-associated MINT2/APBA2 mutation disrupts neurexin
            trafficking and synaptic function
  JOURNAL   Sci Rep 9 (1), 6024 (2019)
   PUBMED   30988517
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Hara,T., Murakami,Y., Seiki,M. and Sakamoto,T.
  TITLE     Mint3 in bone marrow-derived cells promotes lung metastasis in
            breast cancer model mice
  JOURNAL   Biochem Biophys Res Commun 490 (3), 688-692 (2017)
   PUBMED   28634075
  REMARK    GeneRIF: Mint3 depletion attenuated metastasis to the lungs in
            breast cancer model mice.
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Hara,T., Nakaoka,H.J., Hayashi,T., Mimura,K., Hoshino,D., Inoue,M.,
            Nagamura,F., Murakami,Y., Seiki,M. and Sakamoto,T.
  TITLE     Control of metastatic niche formation by targeting APBA3/Mint3 in
            inflammatory monocytes
  JOURNAL   Proc Natl Acad Sci U S A 114 (22), E4416-E4424 (2017)
   PUBMED   28507122
  REMARK    GeneRIF: APBA3-deficient mice show reduced metastasis, with no
            apparent effect on primary tumor growth. APBA3 deficiency in
            inflammatory monocytes hampers glycolysis-dependent chemotaxis of
            cells toward metastatic sites.
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Huai,W., Song,H., Yu,Z., Wang,W., Han,L., Sakamoto,T., Seiki,M.,
            Zhang,L., Zhang,Q. and Zhao,W.
  TITLE     Mint3 potentiates TLR3/4- and RIG-I-induced IFN-beta expression and
            antiviral immune responses
  JOURNAL   Proc Natl Acad Sci U S A 113 (42), 11925-11930 (2016)
   PUBMED   27698125
  REMARK    GeneRIF: we have identified Mint3 as a physiological positive
            regulator of TLR3/4 and RIG-I-induced IFN-beta production and have
            outlined a feedback mechanism for the control of antiviral immune
            responses.
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Gulyas-Kovacs,A., de Wit,H., Milosevic,I., Kochubey,O., Toonen,R.,
            Klingauf,J., Verhage,M. and Sorensen,J.B.
  TITLE     Munc18-1: sequential interactions with the fusion machinery
            stimulate vesicle docking and priming
  JOURNAL   J Neurosci 27 (32), 8676-8686 (2007)
   PUBMED   17687045
  REMARK    GeneRIF: Binding of Munc18-1 to closed, target-SNARE syntaxin 1
            stimulates vesicle docking and regulates the consecutive priming
            step during exocytosis of secretory or synaptic vesicles.
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Ho,A., Morishita,W., Atasoy,D., Liu,X., Tabuchi,K., Hammer,R.E.,
            Malenka,R.C. and Sudhof,T.C.
  TITLE     Genetic analysis of Mint/X11 proteins: essential presynaptic
            functions of a neuronal adaptor protein family
  JOURNAL   J Neurosci 26 (50), 13089-13101 (2006)
   PUBMED   17167098
  REMARK    GeneRIF: Mints are important regulators of presynaptic
            neurotransmitter release that are essential for mouse survival.
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Wang,P., Wang,X. and Pei,D.
  TITLE     Mint-3 regulates the retrieval of the internalized membrane-type
            matrix metalloproteinase, MT5-MMP, to the plasma membrane by
            binding to its carboxyl end motif EWV
  JOURNAL   J Biol Chem 279 (19), 20461-20470 (2004)
   PUBMED   14990567
  REMARK    GeneRIF: Mint-3 regulates the retrieval of the internalized
            membrane-type matrix metalloproteinase, MT5-MMP, to the plasma
            membrane by binding to its carboxyl end motif EWV
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Borg,J.P., Straight,S.W., Kaech,S.M., de Taddeo-Borg,M.,
            Kroon,D.E., Karnak,D., Turner,R.S., Kim,S.K. and Margolis,B.
  TITLE     Identification of an evolutionarily conserved heterotrimeric
            protein complex involved in protein targeting
  JOURNAL   J Biol Chem 273 (48), 31633-31636 (1998)
   PUBMED   9822620
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC155932.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009666.1, AK170182.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 39.72 cM"
     Protein         1..571
                     /product="amyloid-beta A4 precursor protein-binding family
                     A member 3 isoform a"
                     /note="Mint 3; adapter protein X11gamma; neuron-specific
                     X11L2 protein; neuronal munc18-1-interacting protein 3;
                     amyloid beta (A4) precursor protein-binding, family A,
                     member 3"
                     /calculated_mol_wt=60587
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88888.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O96018; propagated from
                     UniProtKB/Swiss-Prot (O88888.1)"
     Region          67..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88888.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70248; propagated from
                     UniProtKB/Swiss-Prot (O88888.1)"
     Region          209..361
                     /region_name="PTB_X11"
                     /note="X11-like Phosphotyrosine-binding (PTB) domain;
                     cd01208"
                     /db_xref="CDD:269919"
     Site            order(221,299,331)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269919"
     Site            order(239,288,291..296,339,350,353)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269919"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O96018; propagated from
                     UniProtKB/Swiss-Prot (O88888.1)"
     Region          390..475
                     /region_name="PDZ1_APBA1_3-like"
                     /note="PDZ domain 1 of amyloid-beta A4 precursor
                     protein-binding family A member 1 (APBA1), APBA2, APBA3,
                     and related domains; cd06720"
                     /db_xref="CDD:467203"
     Site            order(401..407,421,424,454,458,461..462)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467203"
     Region          479..555
                     /region_name="PDZ2_APBA1_3-like"
                     /note="PDZ domain 2 of amyloid-beta A4 precursor
                     protein-binding family A member 1 (APBA1), APBA2, APBA3,
                     and related domains; cd06793"
                     /db_xref="CDD:467255"
     Site            order(493..499,504,507,536,540,543..544)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467255"
     CDS             1..571
                     /gene="Apba3"
                     /gene_synonym="lin-10; Mint-3; mint3; X11gamma"
                     /coded_by="NM_018758.3:222..1937"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS24050.1"
                     /db_xref="GeneID:57267"
                     /db_xref="MGI:MGI:1888527"
ORIGIN      
        1 meflpgpqhp pgpptmdlee pkgpevpsen hpsntqsalg pggpvtlsem eldtssvqel
       61 vqqlealpsd lggpfpdgap cplhiatgqg latqenpdag gllsaeaggd dllgllrdea
      121 sspaqsvpqd paqtaprllq ppedpdgdpg wmegasaepa dsrssssspe pwletaplvt
      181 qqeppvgtqs retlascpav tevpgpcgpe elmdgvifga kylgstqlls erspapstrm
      241 gqaqeamdrv kapegetqpm vevdifistk rvkvlaadsq dalmdhalqt isyiadigpv
      301 lvlmarrrla rrttpqdrqr rlykmlchvf hsedaqliaq aigqafsiay sqflqenrid
      361 psqvgtqpst aashphngdl dhfcnsqncr evciqkrpge glgvalvesg wgsllptavi
      421 anllhggpae rcgalsigdr vtaingtslv glslaacqaa vrevrrlssv tlsiihcppv
      481 ttavirrphv reqlgfcved giicsllrgg aaerggvrvg hriievngqs vvampharii
      541 qlltetreih iktmpaatyr lltgqeqpvy l
//
