BI2L1_MOUSE
ID BI2L1_MOUSE Reviewed; 514 AA.
AC Q9DBJ3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1;
DE Short=BAI1-associated protein 2-like protein 1;
DE AltName: Full=Insulin receptor tyrosine kinase substrate;
GN Name=Baiap2l1; Synonyms=Irtks;
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=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261;
RP SER-281 AND SER-421, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Testis;
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 [5]
RP STRUCTURE BY NMR OF 343-401.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-010, an SH3 domain from mouse cDNA.";
RL Submitted (SEP-2004) to the PDB data bank.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=17430976; DOI=10.1242/jcs.001776;
RA Millard T.H., Dawson J., Machesky L.M.;
RT "Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with
RT distinct filament bundling properties.";
RL J. Cell Sci. 120:1663-1672(2007).
CC -!- FUNCTION: May function as adapter protein. Involved in the formation of
CC clusters of actin bundles. Plays a role in the reorganization of the
CC actin cytoskeleton in response to bacterial infection (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAC1. Binds to F-actin. Interacts with FASLG
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Recruited to actin pedestals that are formed upon infection by
CC bacteria at bacterial attachment sites. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in bladder, liver, testes, heart, lung,
CC spleen, brain and skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:17430976}.
CC -!- DOMAIN: The IMD domain is predicted to have a helical structure. It may
CC induce actin bundling and filopodia formation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine in response to insulin. {ECO:0000250}.
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DR EMBL; AK004918; BAB23669.1; -; mRNA.
DR EMBL; BC015459; AAH15459.1; -; mRNA.
DR CCDS; CCDS39378.1; -.
DR RefSeq; NP_080109.1; NM_025833.3.
DR PDB; 1SPK; NMR; -; A=343-401.
DR PDBsum; 1SPK; -.
DR AlphaFoldDB; Q9DBJ3; -.
DR SMR; Q9DBJ3; -.
DR BioGRID; 211796; 5.
DR STRING; 10090.ENSMUSP00000053129; -.
DR iPTMnet; Q9DBJ3; -.
DR PhosphoSitePlus; Q9DBJ3; -.
DR jPOST; Q9DBJ3; -.
DR MaxQB; Q9DBJ3; -.
DR PaxDb; Q9DBJ3; -.
DR PeptideAtlas; Q9DBJ3; -.
DR PRIDE; Q9DBJ3; -.
DR ProteomicsDB; 273738; -.
DR Antibodypedia; 16001; 206 antibodies from 31 providers.
DR DNASU; 66898; -.
DR Ensembl; ENSMUST00000055190; ENSMUSP00000053129; ENSMUSG00000038859.
DR GeneID; 66898; -.
DR KEGG; mmu:66898; -.
DR UCSC; uc009alq.1; mouse.
DR CTD; 55971; -.
DR MGI; MGI:1914148; Baiap2l1.
DR VEuPathDB; HostDB:ENSMUSG00000038859; -.
DR eggNOG; ENOG502QQC6; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR HOGENOM; CLU_025877_0_1_1; -.
DR InParanoid; Q9DBJ3; -.
DR OMA; KQFHKEI; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q9DBJ3; -.
DR TreeFam; TF325648; -.
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 Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 66898; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Baiap2l1; mouse.
DR EvolutionaryTrace; Q9DBJ3; -.
DR PRO; PR:Q9DBJ3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DBJ3; protein.
DR Bgee; ENSMUSG00000038859; Expressed in secondary oocyte and 196 other tissues.
DR Genevisible; Q9DBJ3; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR CDD; cd11913; SH3_BAIAP2L1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR030060; IRTKS.
DR InterPro; IPR035592; IRTKS_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF4; PTHR14206:SF4; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF14604; SH3_9; 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 3D-structure; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..514
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 1"
FT /id="PRO_0000247855"
FT DOMAIN 1..249
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 340..403
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 306..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..514
FT /note="Binds F-actin"
FT /evidence="ECO:0000250"
FT COILED 115..148
FT /evidence="ECO:0000255"
FT COMPBIAS 466..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR4"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:1SPK"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1SPK"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:1SPK"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:1SPK"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:1SPK"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:1SPK"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1SPK"
SQ SEQUENCE 514 AA; 57188 MW; AF9974A0696812EC CRC64;
MSRGPEEVNR LTENTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA YYDGVAKIGE
IATGSPVSTE LGHVLIEISS THKKLNETLD ENFKKFHKDI IHELEKKTEL DVKYMNATLK
RYQAEHRNKL DSLEKSQAEL KKIRRKSQGG RNALKYEHKE IEYVETVTSR QSEIQKFIAD
GCKEALLEEK RRFCFLVDKH CSFASHIHYY HMQSAELLNS KLPRWQETCC DATKVPEKIM
NMIEEIKTPI STPVSGTPQP SPMIERSKMI GKDYDTLSKY SPKMPPAPSV KAYTSPLIDM
FNNPATAAQS SEKTNNSTAN TGEDPSLQRS VSVATGLNMM KKQKVKTIFP HTAGNNKTLL
SFAQGDVLTL LIPEEKDGWL YGEHDTTKAR GWFPSSYTKL LEENEAMSVP TPSPAPVRSI
STVDLTEKSS VVIPPPDYLE CLSMGATSDK KAGAPKVPSA STFRAPVSRP DATSTSPSDA
NGTAKPPFLS GENPFATVKL RPTVTNDRSA PIIR
