SH3G1_MOUSE
ID SH3G1_MOUSE Reviewed; 368 AA.
AC Q62419;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Endophilin-A2;
DE AltName: Full=Endophilin-2;
DE AltName: Full=SH3 domain protein 2B;
DE AltName: Full=SH3 domain-containing GRB2-like protein 1;
DE AltName: Full=SH3p8;
GN Name=Sh3gl1; Synonyms=Sh3d2b;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [2]
RP PROTEIN SEQUENCE OF 228-239, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-315, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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).
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARC, SYNJ1 and DNM1. Interacts with PDCD6IP.
CC Interacts with BIN2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q62419; P35545: Fau; NbExp=3; IntAct=EBI-642935, EBI-309546;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell
CC projection, podosome {ECO:0000250}. Note=Associated with postsynaptic
CC endosomes in hippocampal neurons. {ECO:0000250}.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second
CC amphipathic helix inserted into helix 1 of the BAR domain (N-BAR
CC domain) induce membrane curvature and bind curved membranes.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
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DR EMBL; U58885; AAC71775.1; -; mRNA.
DR CCDS; CCDS28891.1; -.
DR RefSeq; NP_038692.1; NM_013664.3.
DR AlphaFoldDB; Q62419; -.
DR SMR; Q62419; -.
DR BioGRID; 203207; 9.
DR IntAct; Q62419; 7.
DR MINT; Q62419; -.
DR STRING; 10090.ENSMUSP00000003268; -.
DR iPTMnet; Q62419; -.
DR PhosphoSitePlus; Q62419; -.
DR EPD; Q62419; -.
DR jPOST; Q62419; -.
DR MaxQB; Q62419; -.
DR PaxDb; Q62419; -.
DR PRIDE; Q62419; -.
DR ProteomicsDB; 261023; -.
DR Antibodypedia; 11454; 389 antibodies from 35 providers.
DR DNASU; 20405; -.
DR Ensembl; ENSMUST00000003268; ENSMUSP00000003268; ENSMUSG00000003200.
DR GeneID; 20405; -.
DR KEGG; mmu:20405; -.
DR UCSC; uc008daq.2; mouse.
DR CTD; 6455; -.
DR MGI; MGI:700010; Sh3gl1.
DR VEuPathDB; HostDB:ENSMUSG00000003200; -.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000154737; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q62419; -.
DR OMA; QYLSETM; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q62419; -.
DR TreeFam; TF313281; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-6807004; Negative regulation of MET activity.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 20405; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Sh3gl1; mouse.
DR PRO; PR:Q62419; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q62419; protein.
DR Bgee; ENSMUSG00000003200; Expressed in spermatocyte and 260 other tissues.
DR ExpressionAtlas; Q62419; baseline and differential.
DR Genevisible; Q62419; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IMP:SynGO.
DR CDD; cd11803; SH3_Endophilin_A; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR028501; Endophilin-A.
DR InterPro; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF63; PTHR14167:SF63; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Endocytosis; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..368
FT /note="Endophilin-A2"
FT /id="PRO_0000146745"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 306..365
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..21
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250"
FT REGION 60..87
FT /note="Required for dimerization upon membrane association"
FT /evidence="ECO:0000250"
FT REGION 218..254
FT /note="Interaction with ARC"
FT /evidence="ECO:0000250"
FT REGION 244..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..250
FT /evidence="ECO:0000255"
FT COMPBIAS 244..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99961"
FT MOD_RES 315
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
SQ SEQUENCE 368 AA; 41518 MW; 3F753B1669086353 CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKDMEKKV DVTSKAVAEV LVRTIEYLQP
NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMVRH GKELGGESNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILEELADKL
KRRVREASSR PKREFKPRPR EPFELGELEQ PNGGFPCAPA PKITASSSFR SSDKPIRMPS
KSMPPLDQPS CKALYDFEPE NDGELGFREG DLITLTNQID ENWYEGMLHG QSGFFPLSYV
QVLVPLPQ
