APBA3_RAT
ID APBA3_RAT Reviewed; 569 AA.
AC O70248; B1WBQ3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Amyloid-beta A4 precursor protein-binding family A member 3;
DE AltName: Full=Adapter protein X11gamma;
DE AltName: Full=Neuron-specific X11L2 protein;
DE AltName: Full=Neuronal Munc18-1-interacting protein 3;
DE Short=Mint-3;
GN Name=Apba3; Synonyms=Mint3;
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].
RX PubMed=9860131; DOI=10.1016/s0171-9335(98)80103-9;
RA Okamoto M., Suedhof T.C.;
RT "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2.";
RL Eur. J. Cell Biol. 77:161-165(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/Mcwi; TISSUE=Embryonic spleen;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May modulate processing of the amyloid-beta precursor protein
CC (APP) and hence formation of APP-beta. May enhance the activity of
CC HIF1A in macrophages by inhibiting the activity of HIF1AN (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the cytoplasmic domain of amyloid protein (APP).
CC Interacts with HIF1AN (via N-terminus) (By similarity). Interacts with
CC NECAB3; seems to mediate the interaction between NECAB3 and HIF1AN (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O96018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Composed of an N-terminal domain, a middle phosphotyrosine-
CC binding domain (PID/PTB) that mediates binding with the cytoplasmic
CC domain of the amyloid-beta precursor protein, and two C-terminal PDZ
CC domains thought to attach proteins to the plasma membrane.
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DR EMBL; AF029109; AAC17978.1; -; mRNA.
DR EMBL; CH474029; EDL89170.1; -; Genomic_DNA.
DR EMBL; BC161842; AAI61842.1; -; mRNA.
DR RefSeq; NP_113969.1; NM_031781.1.
DR RefSeq; XP_006241082.1; XM_006241020.2.
DR AlphaFoldDB; O70248; -.
DR SMR; O70248; -.
DR BioGRID; 249776; 1.
DR IntAct; O70248; 4.
DR MINT; O70248; -.
DR STRING; 10116.ENSRNOP00000027784; -.
DR iPTMnet; O70248; -.
DR PhosphoSitePlus; O70248; -.
DR PaxDb; O70248; -.
DR PRIDE; O70248; -.
DR Ensembl; ENSRNOT00000027784; ENSRNOP00000027784; ENSRNOG00000020466.
DR GeneID; 83611; -.
DR KEGG; rno:83611; -.
DR UCSC; RGD:620846; rat.
DR CTD; 9546; -.
DR RGD; 620846; Apba3.
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000160384; -.
DR HOGENOM; CLU_013563_2_0_1; -.
DR InParanoid; O70248; -.
DR OMA; YPAPQEV; -.
DR OrthoDB; 436779at2759; -.
DR TreeFam; TF315245; -.
DR PRO; PR:O70248; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000020466; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; O70248; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO: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:0043086; P:negative regulation of catalytic activity; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR030531; Apba3.
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:SF9; PTHR12345:SF9; 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 Acetylation; Cytoplasm; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..569
FT /note="Amyloid-beta A4 precursor protein-binding family A
FT member 3"
FT /id="PRO_0000064622"
FT DOMAIN 212..376
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 389..475
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 480..554
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O96018"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96018"
FT CONFLICT 37
FT /note="W -> G (in Ref. 1; AAC17978)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="T -> S (in Ref. 1; AAC17978)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="R -> G (in Ref. 1; AAC17978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 60882 MW; A3DA45F4B2BBB338 CRC64;
MEFLPEPQHP PGPPTMDLEE PKGPEVPSED HPSNTQWALG PRGPDTLSEM ELDTSSVRAL
VQQLEALPSD LGGQFPDGAP CPLHIATGQG LATQENLDAG GLLSAEAGGD NLLGLLRCEA
SLPAQSVPPD PAQAAPRLLQ PPEDPGGDPG WMEGTEPADN RSSSSSPELW LETAPLVTHR
DPPVGTQSQE TLASCPAVSE VPGPCGQEEL MDGVLFGAKY LGSTQLLSER NPPPSTRMGQ
AQEAMDRVKA PEGETQPMTE VDIFISTKRV KVLAADSQDA LMDHALQTIS YIADIGPVLV
LMARRRLAKR TTSQDRQRQL YKMLCHVFHS EDAQLIAQAI GQAFSIAYSQ FLQENRIDPS
QVGMQPSASA SHPHNGDLDH FCNSQNCREV CIQKRPGEGL GVALVESGWG SLLPTAVIAN
LLHGGPAERC GALSIGDRVT AINGTSLVGL SLAACQAAVR EVRRHSSVTL SIIHCPPVTT
AVIHRPHVRE QLGFCVENGI ICSLLRGSAA ERGGVRVGHR IIEVNGQSVV AMPHARIIQL
LTETREIHIK TMPAATYRLL TGQEQPVYL
