ID   B1AZ46_MOUSE            Unreviewed;       521 AA.
AC   B1AZ46;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
GN   Name=Baiap2 {ECO:0000313|Ensembl:ENSMUSP00000101840.2,
GN   ECO:0000313|MGI:MGI:2137336};
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 {ECO:0000313|Ensembl:ENSMUSP00000101840.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:15592455}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [2] {ECO:0007829|PubMed:16452087}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000101840.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101840.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] {ECO:0000313|Ensembl:ENSMUSP00000101840.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101840.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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.
CC       {ECO:0000256|ARBA:ARBA00025545}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC       {ECO:0000256|ARBA:ARBA00004486}. Cell projection, ruffle
CC       {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_006532029.1; XM_006531966.3.
DR   RefSeq; XP_006532030.1; XM_006531967.3.
DR   RefSeq; XP_006532031.1; XM_006531968.3.
DR   AlphaFoldDB; B1AZ46; -.
DR   SMR; B1AZ46; -.
DR   EPD; B1AZ46; -.
DR   jPOST; B1AZ46; -.
DR   MaxQB; B1AZ46; -.
DR   PeptideAtlas; B1AZ46; -.
DR   ProteomicsDB; 336902; -.
DR   Antibodypedia; 19790; 605 antibodies from 38 providers.
DR   DNASU; 108100; -.
DR   Ensembl; ENSMUST00000106233.2; ENSMUSP00000101840.2; ENSMUSG00000025372.17.
DR   GeneID; 108100; -.
DR   AGR; MGI:2137336; -.
DR   CTD; 10458; -.
DR   MGI; MGI:2137336; Baiap2.
DR   VEuPathDB; HostDB:ENSMUSG00000025372; -.
DR   GeneTree; ENSGT00940000153560; -.
DR   OrthoDB; 3059844at2759; -.
DR   BioGRID-ORCS; 108100; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Baiap2; mouse.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000025372; Expressed in superior frontal gyrus and 187 other cell types or tissues.
DR   ExpressionAtlas; B1AZ46; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR   GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR   CDD; cd07646; I-BAR_IMD_IRSp53; 1.
DR   CDD; cd11915; SH3_Irsp53; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR013606; I-BAR_dom.
DR   InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR   InterPro; IPR030128; IRSp53_I-BAR_dom.
DR   InterPro; IPR035594; Irsp53_SH3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR14206; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1.
DR   PANTHER; PTHR14206:SF3; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1.
DR   Pfam; PF08397; IMD; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51338; IMD; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Proteomics identification {ECO:0007829|EPD:B1AZ46,
KW   ECO:0007829|MaxQB:B1AZ46};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..250
FT                   /note="IMD"
FT                   /evidence="ECO:0000259|PROSITE:PS51338"
FT   DOMAIN          375..438
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          299..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   521 AA;  57682 MW;  A3148E52079536AA CRC64;
     MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG
     ELASESQGSK ELGDVLFQMA EVHRQIQNQL EETLKSFHNE LLTQLEQKVE LDSRYLSAAL
     KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
     DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA
     VQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
     NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK
     TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
     KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLALPPP DYGTSSRAFP
     TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSADVEVAR F
//