3BP1_RAT
ID 3BP1_RAT Reviewed; 689 AA.
AC D3ZFJ3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=SH3 domain-binding protein 1;
GN Name=Sh3bp1 {ECO:0000312|RGD:1306275};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21658605; DOI=10.1016/j.molcel.2011.03.032;
RA Parrini M.C., Sadou-Dubourgnoux A., Aoki K., Kunida K., Biondini M.,
RA Hatzoglou A., Poullet P., Formstecher E., Yeaman C., Matsuda M., Rosse C.,
RA Camonis J.;
RT "SH3BP1, an exocyst-associated RhoGAP, inactivates Rac1 at the front to
RT drive cell motility.";
RL Mol. Cell 42:650-661(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-539 AND SER-545, 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: GTPase activating protein/GAP which specifically converts
CC GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive
CC GDP-bound form. By specifically inactivating RAC1 at the leading edge
CC of migrating cells, it regulates the spatiotemporal organization of
CC cell protrusions which is important for proper cell migration
CC (PubMed:21658605). Also negatively regulates CDC42 in the process of
CC actin remodeling and the formation of epithelial cell junctions.
CC Through its GAP activity toward RAC1 and/or CDC42 plays a specific role
CC in 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:21658605}.
CC -!- SUBUNIT: Interacts with RAC1. Interacts with the exocyst via EXOC4 and
CC EXOC8; required for the localization of both SH3BP1 and the exocyst to
CC the leading edge of migrating cells. Interacts with CD2AP and CGNL1;
CC probably part of a complex at cell junctions. Interacts with CAPZA1;
CC recruits CAPZA1 to forming cell junctions. May interact with AFDN.
CC Interacts with PLXND1; they dissociate upon SEMA3E binding to PLXND1
CC allowing SH3BP1 to transduce downstream signal through RAC1
CC inactivation. Interacts with ABL1, GRB2 and SRC (via SH3 domain).
CC {ECO:0000250|UniProtKB:P55194, ECO:0000250|UniProtKB:Q9Y3L3}.
CC -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000269|PubMed:21658605}.
CC Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Y3L3}. 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 (PubMed:21658605). Accumulation at forming phagocytic
CC cups is PI3 kinase/bPI3K-dependent and is specific for sites of large
CC particles engagement and their phosphatidylinositol 3,4,5-triphosphate
CC membrane content (By similarity). {ECO:0000250|UniProtKB:Q9Y3L3,
CC ECO:0000269|PubMed:21658605}.
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}.
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DR EMBL; AC096473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001165452.1; NM_001171981.1.
DR AlphaFoldDB; D3ZFJ3; -.
DR SMR; D3ZFJ3; -.
DR IntAct; D3ZFJ3; 1.
DR STRING; 10116.ENSRNOP00000012480; -.
DR iPTMnet; D3ZFJ3; -.
DR PaxDb; D3ZFJ3; -.
DR PeptideAtlas; D3ZFJ3; -.
DR PRIDE; D3ZFJ3; -.
DR Ensembl; ENSRNOT00000012480; ENSRNOP00000012480; ENSRNOG00000009360.
DR GeneID; 300067; -.
DR KEGG; rno:300067; -.
DR CTD; 23616; -.
DR RGD; 1306275; Sh3bp1.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000158369; -.
DR HOGENOM; CLU_013806_2_1_1; -.
DR InParanoid; D3ZFJ3; -.
DR OMA; IESPRYG; -.
DR OrthoDB; 821331at2759; -.
DR TreeFam; TF316514; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:D3ZFJ3; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009360; Expressed in spleen and 19 other tissues.
DR Genevisible; D3ZFJ3; RN.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000145; C:exocyst; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
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; IMP:UniProtKB.
DR GO; GO:0030215; F:semaphorin receptor binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
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; IMP:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; ISO:RGD.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; ISO:RGD.
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 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 Cell junction; Cell projection; Cytoplasm; GTPase activation; Nucleus;
KW Phagocytosis; Phosphoprotein; Reference proteome; SH3-binding;
KW Tight junction.
FT CHAIN 1..689
FT /note="SH3 domain-binding protein 1"
FT /id="PRO_0000441925"
FT DOMAIN 17..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 470..689
FT /note="Interaction with CD2AP"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3L3"
FT REGION 507..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 611..620
FT /note="SH3-binding"
FT /evidence="ECO:0000250|UniProtKB:P55194"
FT COMPBIAS 565..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3L3"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55194"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55194"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55194"
SQ SEQUENCE 689 AA; 74852 MW; 2366217DE1382348 CRC64;
MMKRQLHRMR QLAHTGSSGR TPETAEFLGE DLLQVEQRLE PAKRAAHNVH KRLQACLQGQ
SGADMDKRVK KLPLMALSTA MAESFKELDP DSSMGKALEM SCAIQNQLAR ILAEFEMTLE
RDVLQPLNRL SEEELPAILK RKKSLQKLVS DWNTLKSRLS QAAKNSGSSQ SLGGGSSSHT
HMATANKVET LKEDEEELKR KVEQCKDEYL ADLYHFSTKE DSYANYFTHL LEIQADYHRK
SLTSLDTALA ELRDNHSQAD SSPLTTAAPF SRVYGVSLRT HLQDLGRDIA LPIEACVLLL
LSEGMQEEGL FRLAAGASVL KRLKQTMASD PHSLEEFCSD PHAVAGALKS YLRELPEPLM
TSDLYDDWMR AASLKEPGAR LEALHDVCSR LPQENFNNLR YLMKFLALLA EEQDVNKMTP
SNIAIVLGPN LLWPPEKEGD QAQLDAASVS SIQVVGVVEV LIQNADTLFP GDINFSVSGI
FSGLAPQEKP NSQQVSEELA PVAVPATAAT PTPTPAPTPA PASMTVKERT ESELPKPASP
KVSRSPTDTT ALAEDMTRKT KRPAPARPTM PPPQPSSSRS SPPALSLPAG SVSPGTPQAL
PRRLVGTSLR APTVPPPLPP APPQPARRQS RRLPVSPCPA SPVISNMPAQ VDQGAATEDR
GGPEAVGGHP PTPVLPPQPR PRGLISETD
