ID APBB2_MOUSE Reviewed; 760 AA.
AC Q9DBR4; Q6DFX8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Amyloid beta precursor protein binding family B member 2 {ECO:0000250|UniProtKB:Q92870};
DE AltName: Full=Amyloid-beta (A4) precursor protein-binding family B member 2 {ECO:0000312|MGI:MGI:108405};
DE AltName: Full=Protein Fe65-like 1 {ECO:0000250|UniProtKB:Q92870};
GN Name=Apbb2 {ECO:0000312|MGI:MGI:108405};
GN Synonyms=Fe65l {ECO:0000250|UniProtKB:Q92870},
GN Fe65l1 {ECO:0000303|PubMed:25757569};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-334; SER-409 AND
RP SER-412, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25757569; DOI=10.1096/fj.14-261453;
RA Suh J., Moncaster J.A., Wang L., Hafeez I., Herz J., Tanzi R.E.,
RA Goldstein L.E., Guenette S.Y.;
RT "FE65 and FE65L1 amyloid precursor protein-binding protein compound null
RT mice display adult-onset cataract and muscle weakness.";
RL FASEB J. 29:2628-2639(2015).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27734846; DOI=10.1038/srep25652;
RA Strecker P., Ludewig S., Rust M., Mundinger T.A., Goerlich A.,
RA Kraechan E.G., Mehrfeld C., Herz J., Korte M., Guenette S.Y., Kins S.;
RT "FE65 and FE65L1 share common synaptic functions and genetically interact
RT with the APP family in neuromuscular junction formation.";
RL Sci. Rep. 6:25652-25652(2016).
RN [6]
RP STRUCTURE BY NMR OF 582-704.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal phosphotyrosine interaction domain of
RT APBB2 from mouse.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [7] {ECO:0007744|PDB:1WGU, ECO:0007744|PDB:2ROZ, ECO:0007744|PDB:2YSZ, ECO:0007744|PDB:2YT0, ECO:0007744|PDB:2YT1}
RP STRUCTURE BY NMR OF 564-567 AND 582-704, AND INTERACTION WITH APP.
RX PubMed=18650440; DOI=10.1074/jbc.m803892200;
RA Li H., Koshiba S., Hayashi F., Tochio N., Tomizawa T., Kasai T., Yabuki T.,
RA Motoda Y., Harada T., Watanabe S., Inoue M., Hayashizaki Y., Tanaka A.,
RA Kigawa T., Yokoyama S.;
RT "Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1
RT complexed with the cytoplasmic tail of amyloid precursor protein reveals a
RT novel peptide binding mode.";
RL J. Biol. Chem. 283:27165-27178(2008).
CC -!- FUNCTION: Plays a role in the maintenance of lens transparency, and may
CC also play a role in muscle cell strength (PubMed:25757569,
CC PubMed:27734846). Involved in hippocampal neurite branching and
CC neuromuscular junction formation, as a result plays a role in spatial
CC memory functioning (PubMed:27734846). Activates transcription of APP
CC (By similarity). {ECO:0000250|UniProtKB:Q92870,
CC ECO:0000269|PubMed:25757569, ECO:0000269|PubMed:27734846}.
CC -!- SUBUNIT: Interacts (via C-terminus) with APP (via C-terminus)
CC (PubMed:18650440). Interacts with APLP2 (via cytoplasmic domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q92870,
CC ECO:0000269|PubMed:18650440}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q92870}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q92870}. Early endosome
CC {ECO:0000250|UniProtKB:Q92870}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DBR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBR4-2; Sequence=VSP_011661;
CC Name=3;
CC IsoId=Q9DBR4-3; Sequence=VSP_011661, VSP_011662;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, retinal lens and muscle
CC cells (at protein level). {ECO:0000269|PubMed:25757569}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice develop cataracts from 16 months of
CC age with defects such as ulcer-like anomalies in the cornea, and
CC opacity in the lens cortex or wider lens. Decreased muscle strength,
CC however clasping ability is unaffected (PubMed:25757569). Impaired
CC spatial memory retrieval and learning (PubMed:27734846). Reduced
CC branching of hippocampal neurites and increased fragmentation of
CC neuromuscular junctions (PubMed:27734846). APBB1 and APBB2 double
CC knockout mice show progressive retinal lens disruption from 1 month of
CC age, morphologically lenses show massive vacuolization, lens capsule
CC rupture and disruption of the lens fiber cells organization. Decreased
CC muscle strength, however clasping ability is unaffected
CC (PubMed:25757569, PubMed:27734846). Defects in peripheral motor
CC function including balance and coordination, reduced environmental
CC anxiety, reduced hippocampal basal synaptic transmission and synaptic
CC plasticity (PubMed:27734846). {ECO:0000269|PubMed:25757569,
CC ECO:0000269|PubMed:27734846}.
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DR EMBL; AK004792; BAB23568.2; -; mRNA.
DR EMBL; BC076587; AAH76587.1; -; mRNA.
DR CCDS; CCDS51510.1; -. [Q9DBR4-1]
DR CCDS; CCDS57344.1; -. [Q9DBR4-3]
DR RefSeq; NP_001188343.1; NM_001201414.1.
DR RefSeq; NP_001188344.1; NM_001201415.1. [Q9DBR4-3]
DR RefSeq; NP_033816.1; NM_009686.2. [Q9DBR4-1]
DR PDB; 1WGU; NMR; -; A=582-704.
DR PDB; 2ROZ; NMR; -; B=582-704.
DR PDB; 2YSZ; NMR; -; A=582-704.
DR PDB; 2YT0; NMR; -; A=564-567, A=582-704.
DR PDB; 2YT1; NMR; -; A=582-704.
DR PDBsum; 1WGU; -.
DR PDBsum; 2ROZ; -.
DR PDBsum; 2YSZ; -.
DR PDBsum; 2YT0; -.
DR PDBsum; 2YT1; -.
DR AlphaFoldDB; Q9DBR4; -.
DR BMRB; Q9DBR4; -.
DR SMR; Q9DBR4; -.
DR BioGRID; 198142; 8.
DR ELM; Q9DBR4; -.
DR IntAct; Q9DBR4; 1.
DR MINT; Q9DBR4; -.
DR STRING; 10090.ENSMUSP00000123752; -.
DR iPTMnet; Q9DBR4; -.
DR PhosphoSitePlus; Q9DBR4; -.
DR SwissPalm; Q9DBR4; -.
DR jPOST; Q9DBR4; -.
DR MaxQB; Q9DBR4; -.
DR PaxDb; 10090-ENSMUSP00000125211; -.
DR ProteomicsDB; 296363; -. [Q9DBR4-1]
DR ProteomicsDB; 296364; -. [Q9DBR4-2]
DR ProteomicsDB; 296365; -. [Q9DBR4-3]
DR Pumba; Q9DBR4; -.
DR Antibodypedia; 5811; 205 antibodies from 30 providers.
DR DNASU; 11787; -.
DR Ensembl; ENSMUST00000159786.8; ENSMUSP00000125211.3; ENSMUSG00000029207.17. [Q9DBR4-3]
DR Ensembl; ENSMUST00000162349.8; ENSMUSP00000123752.3; ENSMUSG00000029207.17. [Q9DBR4-1]
DR GeneID; 11787; -.
DR KEGG; mmu:11787; -.
DR UCSC; uc008xpb.2; mouse. [Q9DBR4-3]
DR UCSC; uc033ijy.1; mouse. [Q9DBR4-1]
DR AGR; MGI:108405; -.
DR CTD; 323; -.
DR MGI; MGI:108405; Apbb2.
DR VEuPathDB; HostDB:ENSMUSG00000029207; -.
DR eggNOG; ENOG502QT08; Eukaryota.
DR GeneTree; ENSGT00390000000002; -.
DR InParanoid; Q9DBR4; -.
DR OMA; NVPHADD; -.
DR OrthoDB; 5404780at2759; -.
DR PhylomeDB; Q9DBR4; -.
DR TreeFam; TF314331; -.
DR BioGRID-ORCS; 11787; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Apbb2; mouse.
DR EvolutionaryTrace; Q9DBR4; -.
DR PRO; PR:Q9DBR4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DBR4; Protein.
DR Bgee; ENSMUSG00000029207; Expressed in undifferentiated genital tubercle and 264 other cell types or tissues.
DR ExpressionAtlas; Q9DBR4; baseline and differential.
DR Genevisible; Q9DBR4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR GO; GO:0036438; P:maintenance of lens transparency; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:1901988; P:negative regulation of cell cycle phase transition; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0006939; P:smooth muscle contraction; IMP:UniProtKB.
DR CDD; cd01272; PTB1_Fe65; 1.
DR CDD; cd01271; PTB2_Fe65; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR039576; APBB1/2/3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR14058; AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING FAMILY B; 1.
DR PANTHER; PTHR14058:SF11; AMYLOID BETA PRECURSOR PROTEIN BINDING FAMILY B MEMBER 2; 1.
DR Pfam; PF00640; PID; 2.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01179; PID; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..760
FT /note="Amyloid beta precursor protein binding family B
FT member 2"
FT /id="PRO_0000076053"
FT DOMAIN 290..322
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 413..580
FT /note="PID 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 586..738
FT /note="PID 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 177..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92870"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 348..368
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011661"
FT VAR_SEQ 509..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011662"
FT STRAND 592..601
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:2ROZ"
FT HELIX 609..620
FT /evidence="ECO:0007829|PDB:1WGU"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 629..635
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:1WGU"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 671..676
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 678..680
FT /evidence="ECO:0007829|PDB:1WGU"
FT STRAND 682..688
FT /evidence="ECO:0007829|PDB:1WGU"
FT HELIX 694..704
FT /evidence="ECO:0007829|PDB:1WGU"
SQ SEQUENCE 760 AA; 83201 MW; 9E66E34489F4D736 CRC64;
MSEVLPADSG VGTLAVFMAS SGSTDIANRN SPATPPNTLN LRSSHNELLN AEIKHSDAKN
STPPKCRKKY ALTNIQAAMG LSDPAVQPLL GNGSANIKLV KNGENQLRKA AEQGQQDPNK
NLSPAAVINL TSEKLEVKDP HPQESSGCEI LPSQPRRTKS FLNYYADLET SARELGQNLG
PCQGVGEEKA QPGPGQAPVV IGNGDLLPQK PNKPQSSPED GQVATVSSSP ETKKDHPKTG
AKTDCALHRI QNLAPSDEES SWTTLSQDSA SPSSPDETDI WSDHSFQTDP DLPPGWKRVN
DIAGTYYWHI PTGTTQWERP VSIPADLHGS RKGSLSSVTP SPTPENEKQP WSDFAVLNGG
KINSDIWKDL HAATVNPDPS LKEFEGATLR YASLKLRNAP HGDDDDSCSI NSDPEAKCFA
VRSLGWVEMA EEDLAPGKSS VAVNNCIRQL SYCKNDIRDT VGIWGEGKDM YLSLENDMLS
LVDPMDRSVL HSQPIVNIRV WGVGRDNGRE RDFAYVARDK DTRILKCHVF RCDTPAKAIA
TSLHEICSKI MAERKNAKAL ACSSLQERTN MSLDVPLQVD FPTPKTELVQ KFRVQYLGML
PVDRPVGMDT LNSAIENLMT SSSKEDWPSV NMNVADATVT VISEKNEEEV LVECRVRFLS
FMGVGKDVHT FAFIMDTGNQ RFECHVFWCE PNAANVSEAV QAACMLRYQK CLVARPPSQK
VRPPPPPADS VTRRVTTNVK RGVLSLIDTL KQKRPVTETP
//
