APBA3_MOUSE
ID APBA3_MOUSE Reviewed; 571 AA.
AC O88888; Q3TDI1; Q8BR09;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
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 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 [MRNA].
RX PubMed=9822620; DOI=10.1074/jbc.273.48.31633;
RA Borg J.-P., Straight S.W., Kaech S.M., de Taddeo-Borg M., Kroon D.E.,
RA Karnak D., Turner R.S., Kim S.K., Margolis B.;
RT "Identification of an evolutionarily conserved heterotrimeric protein
RT complex involved in protein targeting.";
RL J. Biol. Chem. 273:31633-31636(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, and Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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: 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; AF070975; AAC78837.1; -; mRNA.
DR EMBL; AK045965; BAC32549.1; -; mRNA.
DR EMBL; AK170182; BAE41620.1; -; mRNA.
DR EMBL; CH466553; EDL31434.1; -; Genomic_DNA.
DR EMBL; BC005423; AAH05423.1; -; mRNA.
DR EMBL; BC009666; AAH09666.1; -; mRNA.
DR CCDS; CCDS24050.1; -.
DR RefSeq; NP_061228.1; NM_018758.2.
DR RefSeq; XP_006513968.1; XM_006513905.1.
DR RefSeq; XP_006513969.1; XM_006513906.3.
DR AlphaFoldDB; O88888; -.
DR SMR; O88888; -.
DR BioGRID; 208237; 1.
DR IntAct; O88888; 1.
DR MINT; O88888; -.
DR STRING; 10090.ENSMUSP00000050995; -.
DR iPTMnet; O88888; -.
DR PhosphoSitePlus; O88888; -.
DR EPD; O88888; -.
DR PaxDb; O88888; -.
DR PeptideAtlas; O88888; -.
DR PRIDE; O88888; -.
DR ProteomicsDB; 296414; -.
DR Antibodypedia; 23338; 168 antibodies from 28 providers.
DR DNASU; 57267; -.
DR Ensembl; ENSMUST00000057798; ENSMUSP00000050995; ENSMUSG00000004931.
DR Ensembl; ENSMUST00000220297; ENSMUSP00000151985; ENSMUSG00000004931.
DR GeneID; 57267; -.
DR KEGG; mmu:57267; -.
DR UCSC; uc007ggz.2; mouse.
DR CTD; 9546; -.
DR MGI; MGI:1888527; Apba3.
DR VEuPathDB; HostDB:ENSMUSG00000004931; -.
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000160384; -.
DR HOGENOM; CLU_013563_2_0_1; -.
DR InParanoid; O88888; -.
DR OMA; YPAPQEV; -.
DR OrthoDB; 436779at2759; -.
DR PhylomeDB; O88888; -.
DR TreeFam; TF315245; -.
DR BioGRID-ORCS; 57267; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Apba3; mouse.
DR PRO; PR:O88888; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O88888; protein.
DR Bgee; ENSMUSG00000004931; Expressed in hindlimb stylopod muscle and 59 other tissues.
DR ExpressionAtlas; O88888; baseline and differential.
DR Genevisible; O88888; MM.
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:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; 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:0043086; P:negative regulation of catalytic activity; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
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..571
FT /note="Amyloid-beta A4 precursor protein-binding family A
FT member 3"
FT /id="PRO_0000064621"
FT DOMAIN 214..378
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 391..477
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 482..556
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..195
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 COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..195
FT /note="Polar 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 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70248"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96018"
FT CONFLICT 238
FT /note="T -> A (in Ref. 2; BAC32549)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="D -> G (in Ref. 2; BAC32549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 60718 MW; 1BBAC7BD1CCF3BCA CRC64;
MEFLPGPQHP PGPPTMDLEE PKGPEVPSEN HPSNTQSALG PGGPVTLSEM ELDTSSVQEL
VQQLEALPSD LGGPFPDGAP CPLHIATGQG LATQENPDAG GLLSAEAGGD DLLGLLRDEA
SSPAQSVPQD PAQTAPRLLQ PPEDPDGDPG WMEGASAEPA DSRSSSSSPE PWLETAPLVT
QQEPPVGTQS RETLASCPAV TEVPGPCGPE ELMDGVIFGA KYLGSTQLLS ERSPAPSTRM
GQAQEAMDRV KAPEGETQPM VEVDIFISTK RVKVLAADSQ DALMDHALQT ISYIADIGPV
LVLMARRRLA RRTTPQDRQR RLYKMLCHVF HSEDAQLIAQ AIGQAFSIAY SQFLQENRID
PSQVGTQPST AASHPHNGDL DHFCNSQNCR EVCIQKRPGE GLGVALVESG WGSLLPTAVI
ANLLHGGPAE RCGALSIGDR VTAINGTSLV GLSLAACQAA VREVRRLSSV TLSIIHCPPV
TTAVIRRPHV REQLGFCVED GIICSLLRGG AAERGGVRVG HRIIEVNGQS VVAMPHARII
QLLTETREIH IKTMPAATYR LLTGQEQPVY L
