ID   ABI2_MOUSE              Reviewed;         446 AA.
AC   P62484; Q6PHU3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Abl interactor 2 {ECO:0000303|PubMed:15572692};
DE   AltName: Full=Abelson interactor 2 {ECO:0000250|UniProtKB:Q9NYB9};
DE            Short=Abi-2 {ECO:0000250|UniProtKB:Q9NYB9};
DE   AltName: Full=Abl-binding protein 3;
DE            Short=AblBP3;
DE   AltName: Full=Arg-binding protein 1 {ECO:0000250|UniProtKB:Q9NYB9};
DE            Short=ArgBP1 {ECO:0000250|UniProtKB:Q9NYB9};
GN   Name=Abi2 {ECO:0000303|PubMed:15572692, ECO:0000312|MGI:MGI:106913};
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].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10995551; DOI=10.1006/mcne.2000.0865;
RA   Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S.,
RA   Pendergast A.M.;
RT   "Localization and phosphorylation of Abl-interactor proteins, Abi-1 and
RT   Abi-2, in the developing nervous system.";
RL   Mol. Cell. Neurosci. 16:244-257(2000).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11516653; DOI=10.1016/s0960-9822(01)00239-1;
RA   Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V.,
RA   Pendergast A.M.;
RT   "The Abl interactor proteins localize to sites of actin polymerization at
RT   the tips of lamellipodia and filopodia.";
RL   Curr. Biol. 11:891-895(2001).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=15572692; DOI=10.1128/mcb.24.24.10905-10922.2004;
RA   Grove M., Demyanenko G., Echarri A., Zipfel P.A., Quiroz M.E.,
RA   Rodriguiz R.M., Playford M., Martensen S.A., Robinson M.R., Wetsel W.C.,
RA   Maness P.F., Pendergast A.M.;
RT   "ABI2-deficient mice exhibit defective cell migration, aberrant dendritic
RT   spine morphogenesis, and deficits in learning and memory.";
RL   Mol. Cell. Biol. 24:10905-10922(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; THR-294 AND SER-301, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
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   [6]
RP   FUNCTION OF WAVE1 COMPLEX.
RX   PubMed=27605705; DOI=10.1091/mbc.e16-05-0326;
RA   Xu C., Fu X., Zhu S., Liu J.J.;
RT   "Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-induced
RT   TrkB endocytosis and dendrite outgrowth.";
RL   Mol. Biol. Cell 27:3342-3356(2016).
CC   -!- FUNCTION: Regulator of actin cytoskeleton dynamics underlying cell
CC       motility and adhesion. Functions as a component of the WAVE complex,
CC       which activates actin nucleating machinery Arp2/3 to drive lamellipodia
CC       formation (By similarity). Acts as a regulator and substrate of
CC       nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked
CC       to cell growth and differentiation. Positively regulates ABL1-mediated
CC       phosphorylation of ENAH, which is required for proper polymerization of
CC       nucleated actin filaments at the leading edge (By similarity).
CC       Contributes to the regulation of actin assembly at the tips of neuron
CC       projections. In particular, controls dendritic spine morphogenesis and
CC       may promote dendritic spine specification toward large mushroom-type
CC       spines known as repositories of memory in the brain (PubMed:15572692).
CC       In hippocampal neurons, may mediate actin-dependent BDNF-NTRK2 early
CC       endocytic trafficking that triggers dendrite outgrowth
CC       (PubMed:27605705). Participates in ocular lens morphogenesis, likely by
CC       regulating lamellipodia-driven adherens junction formation at the
CC       epithelial cell-secondary lens fiber interface (PubMed:15572692). Also
CC       required for nascent adherens junction assembly in epithelial cells (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NYB9,
CC       ECO:0000269|PubMed:15572692, ECO:0000269|PubMed:27605705}.
CC   -!- SUBUNIT: Component of the WAVE complex composed of ABI2, CYFIP1 or
CC       CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC       containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC       WASF1/WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes
CC       the complex to dissociate, releasing activated WASF1 (By similarity).
CC       Interacts (via SH3 domain) with ABL1 and ABL2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NYB9}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC       {ECO:0000269|PubMed:11516653}. Cell projection, filopodium
CC       {ECO:0000250|UniProtKB:Q9NYB9}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9NYB9}. Cell junction, adherens junction
CC       {ECO:0000269|PubMed:15572692}. Cell projection, dendritic spine
CC       {ECO:0000269|PubMed:15572692}. Note=Localized to the protruding
CC       lamellipodia and filopodia tips (By similarity). Present at nascent
CC       adherens junctions where it clusters adjacent to the tips of F-actin
CC       protrusions (By similarity). {ECO:0000250|UniProtKB:Q9NYB9}.
CC   -!- TISSUE SPECIFICITY: Expresses in embryonic and adult brain. In adult
CC       brain prominently expressed in the neocortex, hippocampus and dentate
CC       gyrus. {ECO:0000269|PubMed:10995551}.
CC   -!- DEVELOPMENTAL STAGE: Detected at 10 dpc in developing brain, and
CC       expression is more prominent in the neuroepithelium compared to the
CC       surrounding tissue. At 12 dpc expression is enhanced throughout the CNS
CC       and is detected along the full length of the spinal chord. At 16 dpc
CC       expression remains enhanced in the CNS, and is particularly prominent
CC       in the olfactory bulb (PubMed:10995551). Also highly expressed in
CC       dorsal root ganglia (PubMed:10995551). At 18.5 dpc is prominently
CC       expressed in the marginal zone of the cortex, an area rich in neuronal
CC       and glial cell projections (at protein level) (PubMed:15572692).
CC       Detected at 16.5 dpc in ocular lens, specifically localized where the
CC       tips of migrating secondary fibers forms adherens junctions with
CC       anterior epithelial cells (at protein level) (PubMed:15572692).
CC       {ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:15572692}.
CC   -!- DOMAIN: The SH3 domain is critical for binding to ABL1 and ABL2.
CC       {ECO:0000250|UniProtKB:Q9NYB9}.
CC   -!- PTM: Phosphorylated by ABL1. {ECO:0000250|UniProtKB:Q9NYB9}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice are born at the expected Mendelian
CC       rate. Mutant mice have grossly distorted lenses due to defective
CC       orientation and migration of secondary lens fibers associated with
CC       impaired anterior and posterior sutures formation. Mice exhibit
CC       neuroanatomical abnormalities characterized by defective dendritic
CC       spine morphology and misoriented cortical and hippocampal neurons,
CC       causing profound deficits in learning and memory.
CC       {ECO:0000269|PubMed:15572692}.
CC   -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR   EMBL; BC056345; AAH56345.1; -; mRNA.
DR   CCDS; CCDS14991.1; -.
DR   RefSeq; NP_001185499.1; NM_001198570.1.
DR   RefSeq; NP_001185500.1; NM_001198571.1.
DR   RefSeq; NP_937760.1; NM_198127.2.
DR   AlphaFoldDB; P62484; -.
DR   BMRB; P62484; -.
DR   SMR; P62484; -.
DR   BioGRID; 236719; 22.
DR   DIP; DIP-48418N; -.
DR   IntAct; P62484; 5.
DR   STRING; 10090.ENSMUSP00000140274; -.
DR   GlyGen; P62484; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P62484; -.
DR   PhosphoSitePlus; P62484; -.
DR   EPD; P62484; -.
DR   MaxQB; P62484; -.
DR   PaxDb; 10090-ENSMUSP00000058754; -.
DR   PeptideAtlas; P62484; -.
DR   ProteomicsDB; 286062; -.
DR   Pumba; P62484; -.
DR   Antibodypedia; 34165; 263 antibodies from 31 providers.
DR   DNASU; 329165; -.
DR   Ensembl; ENSMUST00000052332.15; ENSMUSP00000058754.9; ENSMUSG00000026782.16.
DR   GeneID; 329165; -.
DR   KEGG; mmu:329165; -.
DR   UCSC; uc007beq.2; mouse.
DR   AGR; MGI:106913; -.
DR   CTD; 10152; -.
DR   MGI; MGI:106913; Abi2.
DR   VEuPathDB; HostDB:ENSMUSG00000026782; -.
DR   eggNOG; KOG2546; Eukaryota.
DR   GeneTree; ENSGT00940000156089; -.
DR   InParanoid; P62484; -.
DR   OrthoDB; 3028771at2759; -.
DR   PhylomeDB; P62484; -.
DR   TreeFam; TF314303; -.
DR   Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR   Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR   BioGRID-ORCS; 329165; 5 hits in 60 CRISPR screens.
DR   ChiTaRS; Abi2; mouse.
DR   PRO; PR:P62484; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P62484; Protein.
DR   Bgee; ENSMUSG00000026782; Expressed in lateral septal nucleus and 228 other cell types or tissues.
DR   ExpressionAtlas; P62484; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0032433; C:filopodium tip; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR   GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR   GO; GO:0031209; C:SCAR complex; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR   GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0070309; P:lens fiber cell morphogenesis; IMP:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR   GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR   GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR   GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR   GO; GO:0045186; P:zonula adherens assembly; ISS:UniProtKB.
DR   CDD; cd11972; SH3_Abi2; 1.
DR   Gene3D; 6.10.140.1620; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR028457; ABI.
DR   InterPro; IPR035726; Abi2_SH3.
DR   InterPro; IPR012849; Abl-interactor_HHR_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR10460:SF26; ABL INTERACTOR 2; 1.
DR   PANTHER; PTHR10460; ABL INTERACTOR FAMILY MEMBER; 1.
DR   Pfam; PF07815; Abi_HHR; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
DR   Genevisible; P62484; MM.
PE   1: Evidence at protein level;
KW   Cell junction; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Neurogenesis; Phosphoprotein; Reference proteome; SH3 domain; Synapse.
FT   CHAIN           1..446
FT                   /note="Abl interactor 2"
FT                   /id="PRO_0000191791"
FT   DOMAIN          45..107
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          384..443
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          158..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..353
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYB9"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYB9"
FT   MOD_RES         294
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   446 AA;  49387 MW;  8EC1FB543D93BEAA CRC64;
     MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS PDKQRALEET KAYTTQSLAS
     VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
     THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKVSTQNM KMGGLPRTTP PTQKPPSPPM
     SGKGTLGRHS PYRTLEPVRP PVVPNDYVPS PTRNMAPSQQ SPVRTASVNQ RNRTYSSSGS
     SGGSHPSSRS SSRENSGSGS VGVPIAVPTP SPPSVFPGHP VQFYSMNRPA SRHTPPTIGG
     SLPYRRPPSI TSQTSLQNQM NGGPFYNQNP VSDTPPPPPP VEEPVFDESP PPPPPPEDYE
     EEEAAVVEYS DPYAEEDPPW APRAYLEKVV AIYDYTKDKE DELSFQEGAI IYVIKKNDDG
     WYEGVMNGVT GLFPGNYVES IMHYSE
//