ID   APBA2_PONAB             Reviewed;         749 AA.
AC   Q5RD33;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Amyloid-beta A4 precursor protein-binding family A member 2;
GN   Name=APBA2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
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   -!- 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       {ECO:0000250}.
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DR   EMBL; CR858085; CAH90324.1; -; mRNA.
DR   RefSeq; NP_001125150.1; NM_001131678.1.
DR   AlphaFoldDB; Q5RD33; -.
DR   SMR; Q5RD33; -.
DR   STRING; 9601.ENSPPYP00000007120; -.
DR   PRIDE; Q5RD33; -.
DR   GeneID; 100172037; -.
DR   KEGG; pon:100172037; -.
DR   CTD; 321; -.
DR   eggNOG; KOG3605; Eukaryota.
DR   InParanoid; Q5RD33; -.
DR   OrthoDB; 436779at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..749
FT                   /note="Amyloid-beta A4 precursor protein-binding family A
FT                   member 2"
FT                   /id="PRO_0000064618"
FT   DOMAIN          366..555
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          568..653
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          659..735
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          130..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..270
FT                   /note="STXBP1-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        78..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..343
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         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99767"
SQ   SEQUENCE   749 AA;  82470 MW;  BE9EFA166E760EE9 CRC64;
     MAHQKLESVG SGMLDHRVRP GPVPHSQEPE SEDMELPLEG YVPEGLELAA LRPESPAPEE
     QECHNHSPDG DSSSDYVNNT SEEEDYDEGL PEEEEGITYY IRYCPEDDSY LEGMDCNGEE
     YLAHGAHPVD TDECQEAVEE WTDSAGPRPH SHEAEGSQDY PDGQLPIPED EPSVLEAHDQ
     EEDGHYCASK EGYQDYYPEE ANGNTSASPY RLRRGDRDLE DQEEDIDQIV AEIKMSLSMT
     SITSASEASP EHGPEPGPGD SAEACPPIKA SCSPSRHEAR PKSLNLPPEA KHPGDPQRGF
     KPKTRTPEER PKWPHEQVCN GLEQPRKQQR SDLNGPVDNN NIPETKKVAS FPSFVAVPGP
     CEPEDLIDGI IFAANYLGST QLLSERNPSK NIRMMQAQEA VSRVKRMQKA AKIKKKANSE
     GDAQTLTEVD LFISAQRIKV LNADTQETMM DHALRTISYI ADIGNIVVLM ARRRMPRSAS
     QDCIETTPGA QEGKKQYKMI CHVFESEDAQ LIAQSIGQAF SVAYQEFLRA NGINPEDLSQ
     KEYSDIINTQ EMYNDDLIHF SNSENCKELQ LEKHKGEILG VVVVESGWGS ILPTVILANM
     MNGGPAARSG KLSIGDQIMS INGTSLVGLP LATCQGIIKG LKNQTQVKLN IVSCPPVTTV
     LIKRPDLKYQ LGFSVQNGII CSLMRGGIAE RGGVRVGHRI IEINGQSVVA TAHEKIVQAL
     SNSVGEIHMK TMPAAMFRLL TGQETPLYI