APBA2_MOUSE
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 03-AUG-2022, entry version 154.
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 IntAct; P98084; 5.
DR MINT; P98084; -.
DR STRING; 10090.ENSMUSP00000032732; -.
DR iPTMnet; P98084; -.
DR PhosphoSitePlus; P98084; -.
DR jPOST; P98084; -.
DR MaxQB; P98084; -.
DR PaxDb; P98084; -.
DR PRIDE; P98084; -.
DR ProteomicsDB; 281792; -.
DR Antibodypedia; 22443; 209 antibodies from 35 providers.
DR DNASU; 11784; -.
DR Ensembl; ENSMUST00000032732; ENSMUSP00000032732; ENSMUSG00000030519.
DR GeneID; 11784; -.
DR KEGG; mmu:11784; -.
DR UCSC; uc009hgj.2; mouse.
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; 436779at2759; -.
DR PhylomeDB; P98084; -.
DR TreeFam; TF315245; -.
DR BioGRID-ORCS; 11784; 2 hits in 73 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 146 other tissues.
DR ExpressionAtlas; P98084; baseline and differential.
DR Genevisible; P98084; MM.
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; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR030529; Apba2.
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; PTHR12345:SF12; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00462; PTB; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS01179; PID; 1.
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
