SH3G3_MOUSE
ID SH3G3_MOUSE Reviewed; 347 AA.
AC Q62421; Q8R0B7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Endophilin-A3;
DE AltName: Full=Endophilin-3;
DE AltName: Full=SH3 domain protein 2C;
DE AltName: Full=SH3 domain-containing GRB2-like protein 3;
DE AltName: Full=SH3p13;
GN Name=Sh3gl3; Synonyms=Sh3d2c, Sh3d2c2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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, DNM1, SGIP1, SYNJ1 and DYDC1. Interacts
CC with FASLG (By similarity). Interacts with ATXN2. Interacts with BIN2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35180}. Early
CC endosome membrane {ECO:0000250|UniProtKB:O35180}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O35180}. Note=Associated with
CC postsynaptic endosomes in hippocampal neurons. Associated with
CC presynaptic endosomes in olfactory neurons.
CC {ECO:0000250|UniProtKB:O35180}.
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; U58887; AAC72268.1; -; mRNA.
DR EMBL; BC027096; AAH27096.1; -; mRNA.
DR CCDS; CCDS90263.1; -.
DR RefSeq; NP_059096.3; NM_017400.6.
DR AlphaFoldDB; Q62421; -.
DR SMR; Q62421; -.
DR BioGRID; 203210; 8.
DR IntAct; Q62421; 2.
DR MINT; Q62421; -.
DR STRING; 10090.ENSMUSP00000032874; -.
DR iPTMnet; Q62421; -.
DR PhosphoSitePlus; Q62421; -.
DR MaxQB; Q62421; -.
DR PaxDb; Q62421; -.
DR PeptideAtlas; Q62421; -.
DR PRIDE; Q62421; -.
DR ProteomicsDB; 257140; -.
DR DNASU; 20408; -.
DR GeneID; 20408; -.
DR KEGG; mmu:20408; -.
DR UCSC; uc029wml.2; mouse.
DR CTD; 6457; -.
DR MGI; MGI:700011; Sh3gl3.
DR eggNOG; KOG1118; Eukaryota.
DR InParanoid; Q62421; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q62421; -.
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; 20408; 0 hits in 52 CRISPR screens.
DR ChiTaRS; Sh3gl3; mouse.
DR PRO; PR:Q62421; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62421; protein.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; 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:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098845; C:postsynaptic endosome; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; 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:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IGI:SynGO.
DR CDD; cd07615; BAR_Endophilin_A3; 1.
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; IPR032469; Endophilin-A3_BAR.
DR InterPro; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF45; PTHR14167:SF45; 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 Coiled coil; Cytoplasm; Endocytosis; Endosome; Lipid-binding; Membrane;
KW Reference proteome; SH3 domain.
FT CHAIN 1..347
FT /note="Endophilin-A3"
FT /id="PRO_0000146751"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 285..344
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 255..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..201
FT /evidence="ECO:0000255"
FT COMPBIAS 261..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 285
FT /note="A -> S (in Ref. 2; AAH27096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38934 MW; A2174642F853B5EB CRC64;
MSVAGLKKQF HKASQLFSEK ISGAEGTKLD EEFLNMEKKI DITSKAVAEI LSKATEYLQP
NPAYRAKLGM LNTVSKLRGQ VKATGYPQTE GLLGDCMLKY GKELGEDSAF GNSLVDVGEA
LKLMAEVKDS LDINVKQTFI DPLQLLQDKD LKEIGHHLRK LEGRRLDYDY KKRRVGKIPE
EEIRQAVEKF EESKELAERS MFNFLENDVE QVSQLAVFVE AALDYHRQST EILQELQSKL
ELRISLASKV PKREFMPKPV NMSSTDANGV GPSSSSKTPG TDTPADQPCC RGLYDFEPEN
EGELGFKEGD IITLTNQIDE NWYEGMLRGE SGFFPINYVE VIVPLPP
