BIN2_MOUSE
ID BIN2_MOUSE Reviewed; 489 AA.
AC D3Z6Q9;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Bridging integrator 2;
GN Name=Bin2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-420; SER-422;
RP SER-424; SER-430; SER-435; SER-439 AND SER-443, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, Spleen, 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
CC -!- FUNCTION: Promotes cell motility and migration, probably via its
CC interaction with the cell membrane and with podosome proteins that
CC mediate interaction with the cytoskeleton. Modulates membrane curvature
CC and mediates membrane tubulation. Inhibits phagocytosis (By
CC similarity). Plays a role in podosome formation. {ECO:0000250,
CC ECO:0000269|PubMed:23285027}.
CC -!- SUBUNIT: Homodimer. Interacts with BIN1. Interacts with ARHGEF6 (via
CC SH3 domain), ARHGEF7 (via SH3 domain), SH3GL1, SH3GL2 and SH3GL3.
CC Identified in a complex with ARHGEF6 and GIT2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBW5}. Cell
CC projection, podosome membrane {ECO:0000269|PubMed:23285027}; Peripheral
CC membrane protein {ECO:0000269|PubMed:23285027}; Cytoplasmic side
CC {ECO:0000269|PubMed:23285027}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9UBW5}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:Q9UBW5}. Note=Associates with membranes enriched
CC in phosphoinositides. Detected in the actin-rich cell cortex at the
CC leading edge of migrating cells. Detected at podosomes, at an actin-
CC rich ring-like structure. {ECO:0000250|UniProtKB:Q9UBW5}.
CC -!- DOMAIN: The BAR domain mediates dimerization and interaction with
CC membranes enriched in phosphatidylinositides. {ECO:0000250}.
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DR EMBL; AC123724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3Z6Q9; -.
DR SMR; D3Z6Q9; -.
DR IntAct; D3Z6Q9; 1.
DR STRING; 10090.ENSMUSP00000138523; -.
DR iPTMnet; D3Z6Q9; -.
DR PhosphoSitePlus; D3Z6Q9; -.
DR SwissPalm; D3Z6Q9; -.
DR EPD; D3Z6Q9; -.
DR jPOST; D3Z6Q9; -.
DR MaxQB; D3Z6Q9; -.
DR PeptideAtlas; D3Z6Q9; -.
DR PRIDE; D3Z6Q9; -.
DR ProteomicsDB; 273674; -.
DR MGI; MGI:3611448; Bin2.
DR eggNOG; KOG3771; Eukaryota.
DR InParanoid; D3Z6Q9; -.
DR PhylomeDB; D3Z6Q9; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR PRO; PR:D3Z6Q9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; D3Z6Q9; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:MGI.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR028827; BIN2.
DR PANTHER; PTHR46514:SF1; PTHR46514:SF1; 1.
DR Pfam; PF03114; BAR; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR SMART; SM00721; BAR; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51021; BAR; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..489
FT /note="Bridging integrator 2"
FT /id="PRO_0000416099"
FT DOMAIN 28..244
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT REGION 267..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 489 AA; 52554 MW; 8E207C53B1D31A99 CRC64;
MAEGKAGGAA GLFAKQMQKK FSRAQEKVLQ KLGKTVETKD ERFEQSASNF YQQQAEGHKL
YKDLKNFLSA VKVMHESSKR VSETLQEVYS SDWDGHEDLK AIVGNNDLLW EDYEEKLADQ
ALRTMENYVS QFSEIKERIA KRGRKLVDYD SARHHLEAVQ NAKKKDDAKM AKAEEDFSKA
QIVFEDLNQE LLEELPILYN SRIGCYVTVF QNISNLRDVF YREMSKLNHN LYEVMSKLEK
QHSNKVFVVK GLSSSSRRSL VISPPVQSCA ASSPVSPVSP VSPVTSPTSP SATSEPESVS
ATGEELTSEA GGEDSCESQE SLKDEEADEA QSETSSSLPA CNGPTPAPAS PAAEVGSQEE
ALSSSAQSPG RGQTGKDTPS PGDVVLRARA SSEGAEQSKR AASIQRTSAP PSRPPPPRAS
GSGSCNAPGS PEGSSQLCSP RASPDASSNP EPAETREKEG AGSSGPEEPR AVSTKSATQA
SGGLVGLFL
