3BP1_MOUSE
ID 3BP1_MOUSE Reviewed; 680 AA.
AC P55194; A2A5V4; E9QMQ2; Q99KK8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=SH3 domain-binding protein 1 {ECO:0000312|MGI:MGI:104603};
DE Short=3BP-1 {ECO:0000303|PubMed:1379745};
GN Name=Sh3bp1 {ECO:0000312|MGI:MGI:104603}; Synonyms=3bp1;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-680.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 70-680, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7621827; DOI=10.1002/j.1460-2075.1995.tb07315.x;
RA Cicchetti P., Ridley A.J., Zheng Y., Cerione R.A., Baltimore D.;
RT "3BP-1, an SH3 domain binding protein, has GAP activity for Rac and
RT inhibits growth factor-induced membrane ruffling in fibroblasts.";
RL EMBO J. 14:3127-3135(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 342-680, AND SUBUNIT.
RX PubMed=1379745; DOI=10.1126/science.1379745;
RA Cicchetti P., Mayer B.J., Thiel G., Baltimore D.;
RT "Identification of a protein that binds to the SH3 region of Abl and is
RT similar to Bcr and GAP-rho.";
RL Science 257:803-806(1992).
RN [5]
RP INTERACTION WITH RAC1.
RX PubMed=10508610; DOI=10.1016/s0960-9822(99)80447-3;
RA Vaestrik I., Eickholt B.J., Walsh F.S., Ridley A., Doherty P.;
RT "Sema3A-induced growth-cone collapse is mediated by Rac1 amino acids 17-
RT 32.";
RL Curr. Biol. 9:991-998(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-582 AND THR-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22891260; DOI=10.1083/jcb.201202094;
RA Elbediwy A., Zihni C., Terry S.J., Clark P., Matter K., Balda M.S.;
RT "Epithelial junction formation requires confinement of Cdc42 activity by a
RT novel SH3BP1 complex.";
RL J. Cell Biol. 198:677-693(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 607-616 IN COMPLEX WITH ABL1 SH3
RP DOMAIN, AND MOTIF.
RX PubMed=8438166; DOI=10.1126/science.8438166;
RA Ren R., Mayer B.J., Cicchetti P., Baltimore D.;
RT "Identification of a ten-amino acid proline-rich SH3 binding site.";
RL Science 259:1157-1161(1993).
CC -!- FUNCTION: GTPase activating protein (GAP) which specifically converts
CC GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive
CC GDP-bound form (PubMed:7621827). By specifically inactivating RAC1 at
CC the leading edge of migrating cells, it regulates the spatiotemporal
CC organization of cell protrusions which is important for proper cell
CC migration. Also negatively regulates CDC42 in the process of actin
CC remodeling and the formation of epithelial cell junctions. Through its
CC GAP activity toward RAC1 and/or CDC42 plays a specific role in
CC phagocytosis of large particles. Specifically recruited by a PI3
CC kinase/PI3K-dependent mechanism to sites of large particles engagement,
CC inactivates RAC1 and/or CDC42 allowing the reorganization of the
CC underlying actin cytoskeleton required for engulfment. It also plays a
CC role in angiogenesis and the process of repulsive guidance as part of a
CC semaphorin-plexin signaling pathway. Following the binding of PLXND1 to
CC extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1,
CC inducing the intracellular reorganization of the actin cytoskeleton and
CC the collapse of cells (By similarity). {ECO:0000250|UniProtKB:Q9Y3L3,
CC ECO:0000269|PubMed:7621827}.
CC -!- SUBUNIT: Interacts with RAC1 (PubMed:10508610). Interacts with the
CC exocyst via EXOC4 and EXOC8; required for the localization of both
CC SH3BP1 and the exocyst to the leading edge of migrating cells.
CC Interacts with CD2AP and CGNL1; probably part of a complex at cell
CC junctions. Interacts with CAPZA1; recruits CAPZA1 to forming cell
CC junctions. May interact with AFDN. Interacts with PLXND1; they
CC dissociate upon SEMA3E binding to PLXND1 allowing SH3BP1 to transduce
CC downstream signal through RAC1 inactivation (By similarity). Interacts
CC with ABL1, GRB2 and SRC (via SH3 domain) (PubMed:8438166,
CC PubMed:1379745). {ECO:0000250|UniProtKB:Q9Y3L3,
CC ECO:0000269|PubMed:10508610, ECO:0000269|PubMed:1379745,
CC ECO:0000269|PubMed:8438166}.
CC -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000250|UniProtKB:Q9Y3L3}.
CC Cell junction, tight junction {ECO:0000269|PubMed:22891260}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell
CC projection, phagocytic cup {ECO:0000250|UniProtKB:Q9Y3L3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y3L3}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y3L3}. Note=Localizes at the leading edge of
CC migrating cells. Accumulation at forming phagocytic cups is PI3
CC kinase/PI3K-dependent and is specific for sites of large particles
CC engagement and their phosphatidylinositol 3,4,5-triphosphate membrane
CC content. {ECO:0000250|UniProtKB:Q9Y3L3}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels
CC found in spleen and brain, lowest in heart and liver.
CC {ECO:0000269|PubMed:7621827}.
CC -!- DOMAIN: The BAR domain mediates interaction with the exocyst components
CC EXOC4 and EXOC8 and is required for the function in cell migration. It
CC also mediates the interaction with PLXND1.
CC {ECO:0000250|UniProtKB:Q9Y3L3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04598.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA61011.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X87671; CAA61011.1; ALT_INIT; mRNA.
DR EMBL; AL592169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004598; AAH04598.1; ALT_INIT; mRNA.
DR CCDS; CCDS84176.1; -.
DR PIR; S56144; S56144.
DR RefSeq; NP_001303613.1; NM_001316684.1.
DR PDB; 1ABO; X-ray; 2.00 A; C/D=607-616.
DR PDBsum; 1ABO; -.
DR AlphaFoldDB; P55194; -.
DR SMR; P55194; -.
DR IntAct; P55194; 4.
DR MINT; P55194; -.
DR STRING; 10090.ENSMUSP00000052181; -.
DR iPTMnet; P55194; -.
DR PhosphoSitePlus; P55194; -.
DR EPD; P55194; -.
DR jPOST; P55194; -.
DR MaxQB; P55194; -.
DR PaxDb; P55194; -.
DR PeptideAtlas; P55194; -.
DR PRIDE; P55194; -.
DR ProteomicsDB; 286029; -.
DR Antibodypedia; 214; 242 antibodies from 33 providers.
DR Ensembl; ENSMUST00000001226; ENSMUSP00000001226; ENSMUSG00000022436.
DR GeneID; 20401; -.
DR KEGG; mmu:20401; -.
DR CTD; 23616; -.
DR MGI; MGI:104603; Sh3bp1.
DR VEuPathDB; HostDB:ENSMUSG00000022436; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000158369; -.
DR InParanoid; P55194; -.
DR OMA; IESPRYG; -.
DR OrthoDB; 821331at2759; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 20401; 3 hits in 58 CRISPR screens.
DR ChiTaRS; Sh3bp1; mouse.
DR EvolutionaryTrace; P55194; -.
DR PRO; PR:P55194; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P55194; protein.
DR Bgee; ENSMUSG00000022436; Expressed in granulocyte and 194 other tissues.
DR ExpressionAtlas; P55194; baseline and differential.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000145; C:exocyst; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0030215; F:semaphorin receptor binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISO:MGI.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; ISO:MGI.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR IDEAL; IID50285; -.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell projection; Cytoplasm; GTPase activation;
KW Nucleus; Phagocytosis; Phosphoprotein; Reference proteome; SH3-binding;
KW Tight junction.
FT CHAIN 1..680
FT /note="SH3 domain-binding protein 1"
FT /id="PRO_0000056724"
FT DOMAIN 81..262
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 276..469
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..275
FT /note="Interaction with CGNL1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3L3"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..680
FT /note="Interaction with CD2AP"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3L3"
FT REGION 488..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 607..616
FT /note="SH3-binding"
FT /evidence="ECO:0000269|PubMed:8438166"
FT COMPBIAS 561..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZFJ3"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3L3"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 592
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 126..128
FT /note="PLS -> RSG (in Ref. 3; CAA61011)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="S -> N (in Ref. 3; CAA61011 and 2; AAH04598)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="Q -> QE (in Ref. 3; CAA61011)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="D -> G (in Ref. 3; CAA61011)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="P -> L (in Ref. 3; CAA61011 and 2; AAH04598)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="G -> E (in Ref. 3; CAA61011 and 2; AAH04598)"
FT /evidence="ECO:0000305"
FT CONFLICT 671..672
FT /note="RP -> PA (in Ref. 3; CAA61011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 74172 MW; 97AB443D4350DE16 CRC64;
MMKRQLHRMR QLAHTGSSGR TPETAEFLGE DLLQVEQRLE PAKRAAHNVH KRLQACLQGQ
SGADMDKRVK KLPLMALSTT MAESFKELDP DSSMGKALEM TCAIQNQLAR ILAEFEMTLE
RDVLQPLSRL SEEELPAILK HKKSLQKLVS DWNTLKSRLS QAAKNSGSNQ GLGGASGSHT
HTTTANKVEM LKEEEEELKK KVEQCKDEYL ADLYHFSTKE DSYANYFIHL LEIQADYHRK
SLTSLDTALA ELRDNHSQAD HSPLTTAAPF SRVYGVSLRT HLQDLGRDIA LPIEACVLLL
LSEGMQEEGL FRLAAGASVL KRLKQTMASD PHSLEEFCSD PHAVAGALKS YLRELPEPLM
TSDLYDDWMR AASLKEPGAR LEALHDVCSR LPQENFNNLR YLMKFLALLA EEQDVNKMTP
SNIAIVLGPN LLWPPEKEGD QAQLDAASVS SIQVVGVVEA LIQNADTLFP GDINFNVSGI
FPGLAPQEKV SSQQVSEELP PVTVPAPATT PAPTPAPASM AVRERTEADL PKPTSPKVSR
NPTETAASAE DMTRKTKRPA PARPTMPPPQ PSSTRSSPPA PSLPPGSVSP GTPQALPRRL
VGTSLRAPTM PPPLPPVPPQ PARRQSRRLP ASPVISNMPA QVDQGVATED RGGPEAVGGH
PPPPALPPQP RPRGLISETE
