APBA2_RAT
ID APBA2_RAT Reviewed; 750 AA.
AC O35431;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
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=Mint2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9395480; DOI=10.1074/jbc.272.50.31459;
RA Okamoto M., Suedhof T.C.;
RT "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis.";
RL J. Biol. Chem. 272:31459-31464(1997).
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 O35431; P61765: Stxbp1; NbExp=3; IntAct=EBI-2028211, EBI-1029097;
CC O35431; Q8R4T5: Tamalin; NbExp=4; IntAct=EBI-2028211, EBI-7361884;
CC O35431; P05067: APP; Xeno; NbExp=5; IntAct=EBI-2028211, EBI-77613;
CC -!- TISSUE SPECIFICITY: Brain.
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.
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DR EMBL; AF029107; AAC05305.1; -; mRNA.
DR RefSeq; NP_113968.1; NM_031780.1.
DR PDB; 3SUZ; X-ray; 2.70 A; A=365-750.
DR PDB; 3SV1; X-ray; 3.30 A; A/B/C=365-552.
DR PDBsum; 3SUZ; -.
DR PDBsum; 3SV1; -.
DR AlphaFoldDB; O35431; -.
DR SMR; O35431; -.
DR BioGRID; 249775; 6.
DR IntAct; O35431; 4.
DR MINT; O35431; -.
DR STRING; 10116.ENSRNOP00000022049; -.
DR iPTMnet; O35431; -.
DR PhosphoSitePlus; O35431; -.
DR PaxDb; O35431; -.
DR PRIDE; O35431; -.
DR Ensembl; ENSRNOT00000022049; ENSRNOP00000022049; ENSRNOG00000016358.
DR GeneID; 83610; -.
DR KEGG; rno:83610; -.
DR UCSC; RGD:620845; rat.
DR CTD; 321; -.
DR RGD; 620845; Apba2.
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000158943; -.
DR HOGENOM; CLU_013563_3_0_1; -.
DR InParanoid; O35431; -.
DR OMA; HEENHIE; -.
DR OrthoDB; 436779at2759; -.
DR PhylomeDB; O35431; -.
DR TreeFam; TF315245; -.
DR PRO; PR:O35431; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016358; Expressed in frontal cortex and 10 other tissues.
DR Genevisible; O35431; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; NAS:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; TAS:RGD.
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 3D-structure; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..750
FT /note="Amyloid-beta A4 precursor protein-binding family A
FT member 2"
FT /id="PRO_0000064619"
FT DOMAIN 369..556
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 569..655
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 660..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 143..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..271
FT /note="STXBP1-binding"
FT REGION 241..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 295..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..347
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 HELIX 365..369
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 371..385
FT /evidence="ECO:0007829|PDB:3SUZ"
FT HELIX 391..417
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 436..443
FT /evidence="ECO:0007829|PDB:3SUZ"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3SUZ"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 465..474
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 498..506
FT /evidence="ECO:0007829|PDB:3SUZ"
FT HELIX 510..531
FT /evidence="ECO:0007829|PDB:3SUZ"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:3SUZ"
FT HELIX 541..560
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:3SUZ"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:3SUZ"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:3SUZ"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:3SUZ"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:3SUZ"
SQ SEQUENCE 750 AA; 82850 MW; C96842E9657169B6 CRC64;
MAHRKRQSTA SSMLDHRARP GPIPHDQEPE NEDTELPLES YVPTGLELGT LRPDSPTPEE
QECHNHSPDG DSSSDYVNNT SEEEDYDEGL PEEEEGVTYY IRYCPEDDSY LEGMDCNGEE
YLAHGAHPVD TDECQEAVED WTDSVGPHTH SHGAENSQEY PDSHLPIPED DPTVLEVHDQ
EEDGHYCPSK ESYQDYYPPE TNGNTGGASP YRMRRGDGDL EEQEEDIDQI VAEIKMSLSM
TSITSASEAS PEHMPELDPG DSTEACSPSD TGRGPSRQEA RPKSLNLPPE VKHSGDPQRG
LKTKTRTPEE RPKWPQEQVC NGLEQPRKQQ RSDLNGPTDN NNIPETKKVA SFPSFVAVPG
PCEPEDLIDG 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
