ID   APBA2_MOUSE             Reviewed;         750 AA.
AC   P98084; Q6PAJ2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Amyloid-beta A4 precursor protein-binding family A member 2;
DE   AltName: Full=Adapter protein X11beta;
DE   AltName: Full=Neuron-specific X11L protein;
DE   AltName: Full=Neuronal Munc18-1-interacting protein 2;
DE            Short=Mint-2;
GN   Name=Apba2; Synonyms=X11l;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 70-750.
RC   TISSUE=Brain;
RX   PubMed=7719031; DOI=10.1007/bf00350899;
RA   Duclos F., Koenig M.;
RT   "Comparison of primary structure of a neuron-specific protein, X11, between
RT   human and mouse.";
RL   Mamm. Genome 6:57-58(1995).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
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   -!- FUNCTION: Putative function in synaptic vesicle exocytosis by binding
CC       to STXBP1, an essential component of the synaptic vesicle exocytotic
CC       machinery. May modulate processing of the amyloid-beta precursor
CC       protein (APP) and hence formation of APP-beta.
CC   -!- SUBUNIT: Part of a multimeric complex containing STXBP1 and syntaxin-1.
CC       Binds to the cytoplasmic domain of amyloid-beta protein, and to the
CC       nuclear factor NF-kappa-B/p65 via its PDZ domain. Interacts with the N-
CC       terminal domain of NECAB3 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P98084; P12023: App; NbExp=2; IntAct=EBI-81669, EBI-78814;
CC       P98084; P49768: PSEN1; Xeno; NbExp=2; IntAct=EBI-81669, EBI-297277;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in neurons, predominantly of
CC       the cerebellum, hippocampus, and spinal cord. Lesser extent in neurons
CC       of the cerebral cortex and anterior thalmic nuclei.
CC   -!- DOMAIN: Composed of an N-terminal domain that binds STXBP1, a middle
CC       phosphotyrosine-binding domain (PID/PTB) that mediates binding with the
CC       cytoplasmic domain of the amyloid-beta precursor protein, and two C-
CC       terminal PDZ domains thought to attach proteins to the plasma membrane.
CC   -!- CAUTION: Was originally thought to be the ortholog of human X11
CC       (APBA1). {ECO:0000305|PubMed:15489334}.
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DR   EMBL; BC060269; AAH60269.1; -; mRNA.
DR   EMBL; BC057620; AAH57620.1; -; mRNA.
DR   EMBL; L34676; AAA73936.1; -; mRNA.
DR   CCDS; CCDS21335.1; -.
DR   RefSeq; NP_001278095.1; NM_001291166.1.
DR   RefSeq; NP_001278096.1; NM_001291167.1.
DR   RefSeq; NP_031487.1; NM_007461.2.
DR   RefSeq; XP_006540636.1; XM_006540573.3.
DR   RefSeq; XP_006540637.1; XM_006540574.3.
DR   RefSeq; XP_017177434.1; XM_017321945.1.
DR   AlphaFoldDB; P98084; -.
DR   SMR; P98084; -.
DR   BioGRID; 198140; 1.
DR   IntAct; P98084; 5.
DR   MINT; P98084; -.
DR   STRING; 10090.ENSMUSP00000032732; -.
DR   iPTMnet; P98084; -.
DR   PhosphoSitePlus; P98084; -.
DR   jPOST; P98084; -.
DR   MaxQB; P98084; -.
DR   PaxDb; 10090-ENSMUSP00000032732; -.
DR   ProteomicsDB; 281792; -.
DR   Antibodypedia; 22443; 231 antibodies from 35 providers.
DR   DNASU; 11784; -.
DR   Ensembl; ENSMUST00000032732.15; ENSMUSP00000032732.9; ENSMUSG00000030519.15.
DR   GeneID; 11784; -.
DR   KEGG; mmu:11784; -.
DR   UCSC; uc009hgj.2; mouse.
DR   AGR; MGI:1261791; -.
DR   CTD; 321; -.
DR   MGI; MGI:1261791; Apba2.
DR   VEuPathDB; HostDB:ENSMUSG00000030519; -.
DR   eggNOG; KOG3605; Eukaryota.
DR   GeneTree; ENSGT00940000158943; -.
DR   HOGENOM; CLU_013563_3_0_1; -.
DR   InParanoid; P98084; -.
DR   OMA; HEENHIE; -.
DR   OrthoDB; 2881953at2759; -.
DR   PhylomeDB; P98084; -.
DR   TreeFam; TF315245; -.
DR   BioGRID-ORCS; 11784; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Apba2; mouse.
DR   PRO; PR:P98084; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P98084; Protein.
DR   Bgee; ENSMUSG00000030519; Expressed in embryonic brain and 149 other cell types or tissues.
DR   ExpressionAtlas; P98084; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR   CDD; cd00992; PDZ_signaling; 2.
DR   CDD; cd01208; PTB_X11; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   PANTHER; PTHR12345:SF12; AMYLOID-BETA A4 PRECURSOR PROTEIN-BINDING FAMILY A MEMBER 2; 1.
DR   PANTHER; PTHR12345; SYNTENIN RELATED; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00462; PTB; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS01179; PID; 1.
DR   Genevisible; P98084; MM.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..750
FT                   /note="Amyloid-beta A4 precursor protein-binding family A
FT                   member 2"
FT                   /id="PRO_0000064617"
FT   DOMAIN          367..556
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          569..654
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          660..736
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..271
FT                   /note="STXBP1-binding"
FT   COMPBIAS        78..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99767"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99767"
FT   CONFLICT        313
FT                   /note="K -> M (in Ref. 2; AAA73936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="N -> T (in Ref. 2; AAA73936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="V -> A (in Ref. 2; AAA73936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        677..679
FT                   /note="QNG -> RW (in Ref. 2; AAA73936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        688..690
FT                   /note="GIA -> VLQ (in Ref. 2; AAA73936)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   750 AA;  82758 MW;  FC231C966DB467DE CRC64;
     MAHRKRQSTA SSMLDHRARP GPIPHDQEPE SEDTELPLES YVPTGLELGT LRPESPTPEE
     QECHNHSPDG DSSSDYVNNT SEEEDYDEGL PEEEEGVTYY IRYCPEDDSY LEGMDCNGEE
     YIAHGAHPVD TDECQEAVED WTDSVGPHTH SHGAENSQEY PDGHLPIPED DPTVLEVHDQ
     EEDGHYCSSK ESYQDYYPPE TNGNTGGASP YRMRRGDGDL EEQEEDIDQI VAEIKMSLSM
     TSITSASEAS PEHMPELDPG DSTEACPPSD TGHGPGRQEA RPKSLNLPPE VKHPGDLQRG
     LKTKTRTPEE RPKWPQEQVC NGLEQPRKQQ RSDLNGPTDN NNIPETKKVA SFPSFVAVPG
     PCEAEDLIDG IIFAANYLGS TQLLSERNPS KNIRMMQAQE AVSRVKRMQK AAKIKKKANS
     EGDAQTLTEV DLFISTQRIK VLNADTQETM MDHALRTISY IADIGNIVVL MARRRMPRSA
     SQDCIETTPG AQEGKKQYKM ICHVFESEDA QLIAQSIGQA FSVAYQEFLR ANGINPEDLS
     QKEYSDIINT QEMYNDDLIH FSNSENCKEL QLEKHKGEIL GVVVVESGWG SILPTVILAN
     MMNGGPAARS GKLSIGDQIM SINGTSLVGL PLATCQGIIK GLKNQTQVKL NIVSCPPVTT
     VLIKRPDLKY QLGFSVQNGI ICSLMRGGIA ERGGVRVGHR IIEINGQSVV ATAHEKIVQA
     LSNSVGEIHM KTMPAAMFRL LTGQETPLYI
//