BAIP2_RAT
ID BAIP2_RAT Reviewed; 535 AA.
AC Q6GMN2; Q923H3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
DE Short=BAI-associated protein 2;
DE Short=BAI1-associated protein 2;
DE AltName: Full=Insulin receptor substrate protein of 53 kDa;
DE Short=IRSp53;
DE Short=Insulin receptor substrate p53;
DE AltName: Full=Insulin receptor tyrosine kinase substrate protein p53;
GN Name=Baiap2;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11514062; DOI=10.1016/s0304-3940(01)02064-x;
RA Thomas E.A., Foye P.E., Alvarez C.E., Usui H., Sutcliffe J.G.;
RT "Insulin receptor substrate protein p53 localization in rats suggests
RT mechanism for specific polyglutamine neurodegeneration.";
RL Neurosci. Lett. 309:145-148(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 12-18 AND 41-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION, MUTAGENESIS OF TYR-17; TYR-115 AND TYR-178, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11741283; DOI=10.1006/bbrc.2001.6102;
RA Okamura-Oho Y., Miyashita T., Yamada M.;
RT "Distinctive tissue distribution and phosphorylation of IRSp53 isoforms.";
RL Biochem. Biophys. Res. Commun. 289:957-960(2001).
RN [5]
RP INTERACTION WITH TIAM1.
RX PubMed=15899863; DOI=10.1128/mcb.25.11.4602-4614.2005;
RA Connolly B.A., Rice J., Feig L.A., Buchsbaum R.J.;
RT "Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin
RT cytoskeleton regulation.";
RL Mol. Cell. Biol. 25:4602-4614(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-367 AND SER-455, 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: Adapter protein that links membrane-bound small G-proteins to
CC cytoplasmic effector proteins. Necessary for CDC42-mediated
CC reorganization of the actin cytoskeleton and for RAC1-mediated membrane
CC ruffling. Involved in the regulation of the actin cytoskeleton by WASF
CC family members and the Arp2/3 complex. Plays a role in neurite growth.
CC Acts syngeristically with ENAH to promote filipodia formation. Plays a
CC role in the reorganization of the actin cytoskeleton in response to
CC bacterial infection. Participates in actin bundling when associated
CC with EPS8, promoting filopodial protrusions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
CC activated by GTP binding. Binds TIAM1. Interacts with ATN1, ADGRB1,
CC DIAPH1, EPS8, SHANK1, SHANK2, SHANK3, WASF1 and WASF2. Interacts with
CC ENAH after recruitment of CDC42 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6GMN2; Q9Z252: Lin7b; NbExp=3; IntAct=EBI-6997402, EBI-7001699;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in
CC the absence of specific binding partners. Detected in filopodia and
CC close to membrane ruffles. Recruited to actin pedestals that are formed
CC upon infection by bacteria at bacterial attachment sites (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=IRS-58;
CC IsoId=Q6GMN2-1; Sequence=Displayed;
CC Name=2; Synonyms=IRSp53S, BAIAP2-alpha;
CC IsoId=Q6GMN2-2; Sequence=VSP_015510;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11514062,
CC ECO:0000269|PubMed:11741283}.
CC -!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain can
CC induce actin bundling and filopodia formation. In the absence of G-
CC proteins intramolecular interaction between the IMD and the SH3 domain
CC gives rise to an auto-inhibited state of the protein. Interaction of
CC the IMD with RAC1 or CDC42 leads to activation (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
CC SHANK1, DIAPH1 and ENAH. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by INSR in response to insulin
CC treatment. {ECO:0000269|PubMed:11741283}.
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DR EMBL; AY037934; AAK72488.1; -; mRNA.
DR EMBL; BC074009; AAH74009.1; -; mRNA.
DR RefSeq; NP_476544.1; NM_057196.1. [Q6GMN2-2]
DR RefSeq; XP_006247931.1; XM_006247869.3. [Q6GMN2-1]
DR AlphaFoldDB; Q6GMN2; -.
DR SMR; Q6GMN2; -.
DR BioGRID; 250757; 9.
DR CORUM; Q6GMN2; -.
DR IntAct; Q6GMN2; 10.
DR MINT; Q6GMN2; -.
DR STRING; 10116.ENSRNOP00000005687; -.
DR iPTMnet; Q6GMN2; -.
DR PhosphoSitePlus; Q6GMN2; -.
DR jPOST; Q6GMN2; -.
DR PaxDb; Q6GMN2; -.
DR PRIDE; Q6GMN2; -.
DR ABCD; Q6GMN2; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000005687; ENSRNOP00000005687; ENSRNOG00000004049. [Q6GMN2-1]
DR Ensembl; ENSRNOT00000068437; ENSRNOP00000060172; ENSRNOG00000004049. [Q6GMN2-2]
DR GeneID; 117542; -.
DR KEGG; rno:117542; -.
DR CTD; 10458; -.
DR RGD; 619814; Baiap2.
DR eggNOG; ENOG502QUM6; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR HOGENOM; CLU_025877_0_1_1; -.
DR InParanoid; Q6GMN2; -.
DR OMA; EYAVHSH; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q6GMN2; -.
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-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q6GMN2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004049; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q6GMN2; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0061846; C:dendritic spine cytoplasm; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0061845; C:neuron projection branch point; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:RGD.
DR GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:1905232; P:cellular response to L-glutamate; IEP:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0099564; P:modification of synaptic structure, modulating synaptic transmission; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0035418; P:protein localization to synapse; IMP:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR CDD; cd11915; SH3_Irsp53; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR030128; IRSp53.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR035594; Irsp53_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..535
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2"
FT /id="PRO_0000064818"
FT DOMAIN 1..250
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 375..438
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 308..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..251
FT /evidence="ECO:0000250"
FT COMPBIAS 323..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKX1"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 513..535
FT /note="RNPFANVHLKPTVTNDRSAPLLS -> SGSGTLVSTV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11514062"
FT /id="VSP_015510"
FT MUTAGEN 17
FT /note="Y->F: Loss of phosphorylation; when associated with
FT F-115 and F-178."
FT /evidence="ECO:0000269|PubMed:11741283"
FT MUTAGEN 115
FT /note="Y->F: Loss of phosphorylation; when associated with
FT F-17 and F-178."
FT /evidence="ECO:0000269|PubMed:11741283"
FT MUTAGEN 178
FT /note="Y->F: Loss of phosphorylation; when associated with
FT F-17 and F-115."
FT /evidence="ECO:0000269|PubMed:11741283"
SQ 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
