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Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase substrate protein p53)

 BAIP2_RAT               Reviewed;         535 AA.
Q6GMN2; Q923H3;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
Short=BAI-associated protein 2;
Short=BAI1-associated protein 2;
AltName: Full=Insulin receptor substrate protein of 53 kDa;
Short=IRSp53;
Short=Insulin receptor substrate p53;
AltName: Full=Insulin receptor tyrosine kinase substrate protein p53;
Name=Baiap2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=11514062; DOI=10.1016/S0304-3940(01)02064-X;
Thomas E.A., Foye P.E., Alvarez C.E., Usui H., Sutcliffe J.G.;
"Insulin receptor substrate protein p53 localization in rats suggests
mechanism for specific polyglutamine neurodegeneration.";
Neurosci. Lett. 309:145-148(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 12-18 AND 41-50, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[4]
PHOSPHORYLATION, MUTAGENESIS OF TYR-17; TYR-115 AND TYR-178,
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=11741283; DOI=10.1006/bbrc.2001.6102;
Okamura-Oho Y., Miyashita T., Yamada M.;
"Distinctive tissue distribution and phosphorylation of IRSp53
isoforms.";
Biochem. Biophys. Res. Commun. 289:957-960(2001).
[5]
INTERACTION WITH TIAM1.
PubMed=15899863; DOI=10.1128/MCB.25.11.4602-4614.2005;
Connolly B.A., Rice J., Feig L.A., Buchsbaum R.J.;
"Tiam1-IRSp53 complex formation directs specificity of rac-mediated
actin cytoskeleton regulation.";
Mol. Cell. Biol. 25:4602-4614(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-367 AND
SER-455, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Adapter protein that links membrane-bound small G-
proteins to cytoplasmic effector proteins. Necessary for CDC42-
mediated reorganization of the actin cytoskeleton and for RAC1-
mediated membrane ruffling. Involved in the regulation of the
actin cytoskeleton by WASF family members and the Arp2/3 complex.
Plays a role in neurite growth. Acts syngeristically with ENAH to
promote filipodia formation. Plays a role in the reorganization of
the actin cytoskeleton in response to bacterial infection.
Participates in actin bundling when associated with EPS8,
promoting filopodial protrusions (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
activated by GTP binding. Binds TIAM1. Interacts with ATN1,
ADGRB1, DIAPH1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2.
Interacts with ENAH after recruitment of CDC42 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q9Z252:Lin7b; NbExp=3; IntAct=EBI-6997402, EBI-7001699;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell
projection, filopodium {ECO:0000250}. Cell projection, ruffle
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Note=Detected throughout the cytoplasm in the absence of specific
binding partners. Detected in filopodia and close to membrane
ruffles. Recruited to actin pedestals that are formed upon
infection by bacteria at bacterial attachment sites (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=IRS-58;
IsoId=Q6GMN2-1; Sequence=Displayed;
Name=2; Synonyms=IRSp53S, BAIAP2-alpha;
IsoId=Q6GMN2-2; Sequence=VSP_015510;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11514062,
ECO:0000269|PubMed:11741283}.
-!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain
can induce actin bundling and filopodia formation. In the absence
of G-proteins intramolecular interaction between the IMD and the
SH3 domain gives rise to an auto-inhibited state of the protein.
Interaction of the IMD with RAC1 or CDC42 leads to activation (By
similarity). {ECO:0000250}.
-!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
SHANK1, DIAPH1 and ENAH. {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues by INSR in response to
insulin treatment. {ECO:0000269|PubMed:11741283}.
-----------------------------------------------------------------------
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EMBL; AY037934; AAK72488.1; -; mRNA.
EMBL; BC074009; AAH74009.1; -; mRNA.
RefSeq; NP_476544.1; NM_057196.1. [Q6GMN2-2]
RefSeq; XP_006247931.1; XM_006247869.3. [Q6GMN2-1]
UniGene; Rn.95155; -.
ProteinModelPortal; Q6GMN2; -.
SMR; Q6GMN2; -.
BioGrid; 250757; 7.
CORUM; Q6GMN2; -.
IntAct; Q6GMN2; 8.
MINT; MINT-93063; -.
STRING; 10116.ENSRNOP00000005687; -.
iPTMnet; Q6GMN2; -.
PhosphoSitePlus; Q6GMN2; -.
PaxDb; Q6GMN2; -.
PRIDE; Q6GMN2; -.
Ensembl; ENSRNOT00000005687; ENSRNOP00000005687; ENSRNOG00000004049. [Q6GMN2-1]
Ensembl; ENSRNOT00000068437; ENSRNOP00000060172; ENSRNOG00000004049. [Q6GMN2-2]
GeneID; 117542; -.
KEGG; rno:117542; -.
CTD; 10458; -.
RGD; 619814; Baiap2.
eggNOG; ENOG41110CD; LUCA.
GeneTree; ENSGT00390000005995; -.
HOGENOM; HOG000038005; -.
HOVERGEN; HBG054462; -.
InParanoid; Q6GMN2; -.
KO; K05627; -.
OMA; EDYSPWA; -.
OrthoDB; EOG091G05ZV; -.
PhylomeDB; Q6GMN2; -.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
PRO; PR:Q6GMN2; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000004049; -.
Genevisible; Q6GMN2; RN.
GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0061846; C:dendritic spine cytoplasm; IDA:RGD.
GO; GO:0060076; C:excitatory synapse; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005874; C:microtubule; IDA:RGD.
GO; GO:0061845; C:neuron projection branch point; IDA:RGD.
GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0098794; C:postsynapse; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0098793; C:presynapse; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0097060; C:synaptic membrane; IDA:RGD.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IEA:Ensembl.
GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
GO; GO:0001221; F:transcription cofactor binding; IPI:RGD.
GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
GO; GO:1905232; P:cellular response to L-glutamate; IEP:RGD.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0035418; P:protein localization to synapse; IMP:RGD.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
CDD; cd11915; SH3_Irsp53; 1.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR013606; I-BAR_dom.
InterPro; IPR030128; IRSp53.
InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
InterPro; IPR035594; Irsp53_SH3.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR14206; PTHR14206; 1.
PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
Pfam; PF08397; IMD; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51338; IMD; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 535 Brain-specific angiogenesis inhibitor 1-
associated protein 2.
/FTId=PRO_0000064818.
DOMAIN 1 250 IMD. {ECO:0000255|PROSITE-
ProRule:PRU00668}.
DOMAIN 375 438 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 1 251 {ECO:0000250}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 341 341 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 361 361 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BKX1}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 513 535 RNPFANVHLKPTVTNDRSAPLLS -> SGSGTLVSTV (in
isoform 2).
{ECO:0000303|PubMed:11514062}.
/FTId=VSP_015510.
MUTAGEN 17 17 Y->F: Loss of phosphorylation; when
associated with F-115 and F-178.
{ECO:0000269|PubMed:11741283}.
MUTAGEN 115 115 Y->F: Loss of phosphorylation; when
associated with F-17 and F-178.
{ECO:0000269|PubMed:11741283}.
MUTAGEN 178 178 Y->F: Loss of phosphorylation; when
associated with F-17 and F-115.
{ECO:0000269|PubMed:11741283}.
SEQUENCE 535 AA; 59183 MW; 606CED16E5DFD212 CRC64;
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKAFHNE LLTQLEQKVE LDSRYLSAAL
KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA
AQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
NGVAGADSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK
TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLALPPP DYGTSSRAFP
SQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS


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