ID   ABI1_RAT                Reviewed;         476 AA.
AC   Q9QZM5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=Abl interactor 1;
DE   AltName: Full=Abelson interactor 1;
DE            Short=Abi-1;
DE   AltName: Full=Eps8 SH3 domain-binding protein;
DE            Short=Eps8-binding protein;
DE   AltName: Full=e3B1;
GN   Name=Abi1 {ECO:0000312|RGD:621008};
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   STRAIN=Sprague-Dawley;
RA   Nicolas G., Galand C., Lecomte M.C.;
RT   "cDNA sequence of the rat eps8 binding protein (e3B1).";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
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   FUNCTION IN NEUROGENESIS, INTERACTION WITH EPS8; MYC; MAX; SHANK2; SHANK3
RP   AND WASF1, PHOSPHORYLATION AT TYR-53, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-53.
RX   PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
RA   Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
RA   Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
RT   "Abelson interacting protein 1 (Abi-1) is essential for dendrite
RT   morphogenesis and synapse formation.";
RL   EMBO J. 26:1397-1409(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-434, AND
RP   IDENTIFICATION BY 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 act in negative regulation of cell growth and
CC       transformation by interacting with nonreceptor tyrosine kinases ABL1
CC       and/or ABL2. May play a role in regulation of EGF-induced Erk pathway
CC       activation. Involved in cytoskeletal reorganization and EGFR signaling.
CC       Together with EPS8 participates in transduction of signals from Ras to
CC       Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac
CC       specific guanine nucleotide exchange factor (GEF) activity and ABI1
CC       seems to act as an adapter in the complex. Regulates ABL1/c-Abl-
CC       mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and
CC       there seems to regulate WASF1 protein level. In brain, seems to
CC       regulate the dendritic outgrowth and branching as well as to determine
CC       the shape and number of synaptic contacts of developing neurons.
CC       {ECO:0000269|PubMed:17304222}.
CC   -!- SUBUNIT: Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8, SOS1,
CC       SOS2, GRB2, SPTA1, NCKAP1/NAP1, the first SH3 domain of NCK1 and
CC       through its N-terminus with WASF1. Part of a complex consisting of
CC       ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and
CC       SOS1. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC       NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2.
CC       Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the
CC       interaction is direct. Interacts with the heterodimer MYC:MAX; the
CC       interaction may enhance MYC:MAX transcriptional activity. Interacts
CC       with FNBP1L (via the SH3 domain), WASF2, and CDC42, but only in the
CC       presence of FNBP1L (By similarity). {ECO:0000250|UniProtKB:Q8IZP0,
CC       ECO:0000269|PubMed:17304222}.
CC   -!- INTERACTION:
CC       Q9QZM5; P52164: Max; NbExp=2; IntAct=EBI-920097, EBI-1184963;
CC       Q9QZM5; Q9JLU4: Shank3; NbExp=7; IntAct=EBI-920097, EBI-6271152;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000269|PubMed:17304222}. Cell projection, lamellipodium
CC       {ECO:0000269|PubMed:17304222}. Cell projection, filopodium
CC       {ECO:0000269|PubMed:17304222}. Cell projection, growth cone
CC       {ECO:0000269|PubMed:10995551}. Postsynaptic density
CC       {ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:17304222}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:17304222}. Note=Localized to
CC       protruding lamellipodia and filopodia tips. May shuttle from the
CC       postsynaptic densities to the nucleus. {ECO:0000269|PubMed:10995551,
CC       ECO:0000269|PubMed:17304222}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in brain, high levels detected in
CC       cortex, hippocampus and cerebellum (at protein level).
CC       {ECO:0000269|PubMed:17304222}.
CC   -!- DEVELOPMENTAL STAGE: Low protein levels at birth that increase
CC       progressively at least until 14 days after birth.
CC       {ECO:0000269|PubMed:17304222}.
CC   -!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
CC       sufficient for interaction with STX1A. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine residues after serum stimulation or
CC       induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1,
CC       required for nuclear but not for synaptic localization.
CC       {ECO:0000269|PubMed:17304222}.
CC   -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR   EMBL; AF176784; AAD55263.1; -; mRNA.
DR   RefSeq; XP_006254416.1; XM_006254354.3.
DR   AlphaFoldDB; Q9QZM5; -.
DR   SMR; Q9QZM5; -.
DR   BioGRID; 249447; 1.
DR   DIP; DIP-36968N; -.
DR   IntAct; Q9QZM5; 10.
DR   MINT; Q9QZM5; -.
DR   STRING; 10116.ENSRNOP00000054381; -.
DR   iPTMnet; Q9QZM5; -.
DR   PhosphoSitePlus; Q9QZM5; -.
DR   jPOST; Q9QZM5; -.
DR   PaxDb; 10116-ENSRNOP00000054381; -.
DR   GeneID; 79249; -.
DR   UCSC; RGD:621008; rat.
DR   AGR; RGD:621008; -.
DR   CTD; 10006; -.
DR   RGD; 621008; Abi1.
DR   VEuPathDB; HostDB:ENSRNOG00000031325; -.
DR   eggNOG; KOG2546; Eukaryota.
DR   InParanoid; Q9QZM5; -.
DR   OrthoDB; 3028771at2759; -.
DR   PhylomeDB; Q9QZM5; -.
DR   Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR   Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR   PRO; PR:Q9QZM5; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000031325; Expressed in Ammon's horn and 19 other cell types or tissues.
DR   ExpressionAtlas; Q9QZM5; baseline and differential.
DR   GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0032433; C:filopodium tip; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0031209; C:SCAR complex; ISO:RGD.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:RGD.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR   GO; GO:0035591; F:signaling adaptor activity; ISO:RGD.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR   GO; GO:0072673; P:lamellipodium morphogenesis; ISO:RGD.
DR   GO; GO:0035855; P:megakaryocyte development; ISO:RGD.
DR   GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR   GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR   CDD; cd11971; SH3_Abi1; 1.
DR   Gene3D; 6.10.140.1620; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR028457; ABI.
DR   InterPro; IPR035725; Abi1_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:SF2; ABL INTERACTOR 1; 1.
DR   PANTHER; PTHR10460; ABL INTERACTOR FAMILY MEMBER; 1.
DR   Pfam; PF07815; Abi_HHR; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00499; P67PHOX.
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; Q9QZM5; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Nucleus; Phosphoprotein; Reference proteome; SH3 domain; Synapse.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   CHAIN           2..476
FT                   /note="Abl interactor 1"
FT                   /id="PRO_0000191789"
FT   DOMAIN          45..107
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          414..473
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          150..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..387
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         53
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:17304222"
FT   MOD_RES         169
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         173
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         208
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         210
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CBW3"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         287
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MOD_RES         423
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CBW3"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         475
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT   MUTAGEN         53
FT                   /note="Y->A: Not phosphorylated and perinuclear upon NMDA
FT                   treatment."
FT                   /evidence="ECO:0000269|PubMed:17304222"
SQ   SEQUENCE   476 AA;  51705 MW;  A2B8CC377090BEA6 CRC64;
     MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
     VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
     THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP
     VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG
     SGSRENSGSS SIGIPIAVPT PSPPTAGPAA PGAAPGSQYG TMTRQISRHN STTSSTSSGG
     YRRTPSVTAQ FSAQPHVNGG PLYSQNSISI APPPPPMPQL TPQIPLTGFV ARVQENIADS
     PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYS DPYADGDPAW APKNYIEKVV
     AIYDYTKDKD DELSFKEGAI IYVIKKNDDG WFEGVCNRVT GLFPGNYVES IMHYTD
//