SH3G2_HUMAN
ID SH3G2_HUMAN Reviewed; 352 AA.
AC Q99962; B2R618; Q9NQK5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Endophilin-A1;
DE AltName: Full=EEN-B1;
DE AltName: Full=Endophilin-1;
DE AltName: Full=SH3 domain protein 2A;
DE AltName: Full=SH3 domain-containing GRB2-like protein 2;
GN Name=SH3GL2; Synonyms=CNSA2, SH3D2A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=9169142; DOI=10.1006/geno.1997.4645;
RA Giachino C., Lantelme E., Lanzetti L., Saccone S., Della Valle G.,
RA Migone N.;
RT "A novel SH3-containing human gene family preferentially expressed in the
RT central nervous system.";
RL Genomics 41:427-434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA So C.W., So C.K.C., Sham M.H., Chan L.C.;
RT "A family of EEN-like genes coding for SH3-domain containing proteins are
RT preferentially expressed in human brain.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH ADAM9 AND ADAM15.
RX PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL J. Biol. Chem. 274:31693-31699(1999).
RN [9]
RP INTERACTION WITH SYNJ1.
RX PubMed=10542231; DOI=10.1074/jbc.274.45.32001;
RA Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A., Migone N.,
RA Hoffmueller U., Schneider-Mergener J., Cesareni G.;
RT "The SH3 domains of endophilin and amphiphysin bind to the proline-rich
RT region of synaptojanin 1 at distinct sites that display an unconventional
RT binding specificity.";
RL J. Biol. Chem. 274:32001-32007(1999).
RN [10]
RP INTERACTION WITH PDCD6IP.
RX PubMed=17350572; DOI=10.1016/j.cell.2007.01.035;
RA Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., Hill C.P.;
RT "Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus
RT budding.";
RL Cell 128:841-852(2007).
RN [11]
RP INTERACTION WITH ATXN2.
RX PubMed=18602463; DOI=10.1016/j.cellsig.2008.05.018;
RA Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J.,
RA Auburger G.;
RT "Ataxin-2 associates with the endocytosis complex and affects EGF receptor
RT trafficking.";
RL Cell. Signal. 20:1725-1739(2008).
RN [12]
RP INTERACTION WITH BIN2.
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-247, DOMAIN, AND MUTAGENESIS OF
RP ALA-63; ALA-66; MET-70 AND PHE-202.
RX PubMed=16763557; DOI=10.1038/sj.emboj.7601176;
RA Masuda M., Takeda S., Sone M., Ohki T., Mori H., Kamioka Y., Mochizuki N.;
RT "Endophilin BAR domain drives membrane curvature by two newly identified
RT structure-based mechanisms.";
RL EMBO J. 25:2889-2897(2006).
RN [14]
RP STRUCTURE BY NMR OF 293-352.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the SH3 domain of human SH3-containing GRB2-like
RT protein 2.";
RL Submitted (DEC-2006) to the PDB data bank.
RN [15]
RP INTERACTION WITH ADGRB2.
RX PubMed=28891236; DOI=10.1002/humu.23336;
RA Purcell R.H., Toro C., Gahl W.A., Hall R.A.;
RT "A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases
RT receptor signaling activity.";
RL Hum. Mutat. 38:1751-1760(2017).
CC -!- FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other
CC proteins to membranes with high curvature. Required for BDNF-dependent
CC dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early
CC endocytic trafficking and signaling from early endosomes.
CC {ECO:0000250|UniProtKB:Q62420}.
CC -!- SUBUNIT: Monomer; in cytoplasm. Homodimer; when associated with
CC membranes (By similarity). Interacts with OPHN1 (By similarity).
CC Interacts with SYNJ1 (PubMed:10542231). Interacts with DNM1 (By
CC similarity). Interacts with MAP4K3; the interaction appears to regulate
CC MAP4K3-mediated JNK activation (By similarity). Interacts with PDCD6IP
CC (PubMed:17350572). Interacts with ATXN2 (PubMed:18602463). Interacts
CC with ADAM9 and ADAM15 cytoplasmic tails (PubMed:10531379). Interacts
CC with BIN2 (PubMed:23285027). Interacts with TMEM108 (By similarity).
CC Interacts with ADGRB2 (PubMed:28891236). {ECO:0000250|UniProtKB:Q62420,
CC ECO:0000250|UniProtKB:Q62910, ECO:0000269|PubMed:10531379,
CC ECO:0000269|PubMed:10542231, ECO:0000269|PubMed:17350572,
CC ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:23285027,
CC ECO:0000269|PubMed:28891236}.
CC -!- INTERACTION:
CC Q99962; Q13444: ADAM15; NbExp=2; IntAct=EBI-77938, EBI-77818;
CC Q99962; Q13443: ADAM9; NbExp=2; IntAct=EBI-77938, EBI-77903;
CC Q99962; Q99700: ATXN2; NbExp=9; IntAct=EBI-77938, EBI-697691;
CC Q99962; P50570: DNM2; NbExp=2; IntAct=EBI-77938, EBI-346547;
CC Q99962; P50402: EMD; NbExp=2; IntAct=EBI-77938, EBI-489887;
CC Q99962; Q5S007: LRRK2; NbExp=4; IntAct=EBI-77938, EBI-5323863;
CC Q99962; Q9H3S7: PTPN23; NbExp=2; IntAct=EBI-77938, EBI-724478;
CC Q99962; Q70E73: RAPH1; NbExp=5; IntAct=EBI-77938, EBI-3940924;
CC Q99962; Q99961: SH3GL1; NbExp=4; IntAct=EBI-77938, EBI-697911;
CC Q99962; Q99962: SH3GL2; NbExp=4; IntAct=EBI-77938, EBI-77938;
CC Q99962; Q99963: SH3GL3; NbExp=5; IntAct=EBI-77938, EBI-473910;
CC Q99962; Q96B97: SH3KBP1; NbExp=2; IntAct=EBI-77938, EBI-346595;
CC Q99962; Q62910: Synj1; Xeno; NbExp=2; IntAct=EBI-77938, EBI-1149123;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35179}.
CC Membrane {ECO:0000250|UniProtKB:O35179}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O35179}. Early endosome
CC {ECO:0000250|UniProtKB:Q62420}. Presynapse
CC {ECO:0000250|UniProtKB:O35179}.
CC -!- TISSUE SPECIFICITY: Brain, mostly in frontal cortex. Expressed at high
CC level in fetal cerebellum.
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. The BAR
CC domain dimer forms a rigid crescent shaped bundle of helices with the
CC pair of second amphipathic helices protruding towards the membrane-
CC binding surface. {ECO:0000269|PubMed:16763557}.
CC -!- MISCELLANEOUS: HeLa cells expressing the N-BAR domain of SH3GL2 show
CC tubulation of the plasma membrane. The N-BAR domain binds liposomes and
CC induces formation of tubules from liposomes. The N-terminal amphipathic
CC helix is required for liposome binding. The second amphipathic helix
CC enhances liposome tubulation.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SH3GL2ID44345ch9p22.html";
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DR EMBL; X99657; CAA67971.1; -; mRNA.
DR EMBL; AF036268; AAC04764.1; -; mRNA.
DR EMBL; CR542086; CAG46883.1; -; mRNA.
DR EMBL; CR542102; CAG46899.1; -; mRNA.
DR EMBL; BT019682; AAV38488.1; -; mRNA.
DR EMBL; AK312400; BAG35315.1; -; mRNA.
DR EMBL; AL139115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58661.1; -; Genomic_DNA.
DR CCDS; CCDS6483.1; -.
DR RefSeq; NP_003017.1; NM_003026.3.
DR PDB; 1X03; X-ray; 3.10 A; A=1-247.
DR PDB; 1X04; X-ray; 2.90 A; A=1-58, A=89-247.
DR PDB; 2D4C; X-ray; 2.40 A; A/B/C/D=1-247.
DR PDB; 2DBM; NMR; -; A=293-352.
DR PDBsum; 1X03; -.
DR PDBsum; 1X04; -.
DR PDBsum; 2D4C; -.
DR PDBsum; 2DBM; -.
DR AlphaFoldDB; Q99962; -.
DR BMRB; Q99962; -.
DR SMR; Q99962; -.
DR BioGRID; 112353; 72.
DR CORUM; Q99962; -.
DR DIP; DIP-30996N; -.
DR IntAct; Q99962; 71.
DR MINT; Q99962; -.
DR STRING; 9606.ENSP00000369981; -.
DR iPTMnet; Q99962; -.
DR PhosphoSitePlus; Q99962; -.
DR BioMuta; SH3GL2; -.
DR DMDM; 10720276; -.
DR EPD; Q99962; -.
DR jPOST; Q99962; -.
DR MassIVE; Q99962; -.
DR MaxQB; Q99962; -.
DR PaxDb; Q99962; -.
DR PeptideAtlas; Q99962; -.
DR PRIDE; Q99962; -.
DR ProteomicsDB; 78546; -.
DR Antibodypedia; 4106; 345 antibodies from 37 providers.
DR DNASU; 6456; -.
DR Ensembl; ENST00000380607.5; ENSP00000369981.4; ENSG00000107295.10.
DR GeneID; 6456; -.
DR KEGG; hsa:6456; -.
DR MANE-Select; ENST00000380607.5; ENSP00000369981.4; NM_003026.5; NP_003017.1.
DR UCSC; uc003zna.4; human.
DR CTD; 6456; -.
DR DisGeNET; 6456; -.
DR GeneCards; SH3GL2; -.
DR HGNC; HGNC:10831; SH3GL2.
DR HPA; ENSG00000107295; Tissue enhanced (brain, retina).
DR MIM; 604465; gene.
DR neXtProt; NX_Q99962; -.
DR OpenTargets; ENSG00000107295; -.
DR PharmGKB; PA35737; -.
DR VEuPathDB; HostDB:ENSG00000107295; -.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000160529; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q99962; -.
DR OMA; XIRQASS; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q99962; -.
DR TreeFam; TF313281; -.
DR PathwayCommons; Q99962; -.
DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR SignaLink; Q99962; -.
DR SIGNOR; Q99962; -.
DR BioGRID-ORCS; 6456; 8 hits in 1063 CRISPR screens.
DR ChiTaRS; SH3GL2; human.
DR EvolutionaryTrace; Q99962; -.
DR GeneWiki; SH3GL2; -.
DR GenomeRNAi; 6456; -.
DR Pharos; Q99962; Tbio.
DR PRO; PR:Q99962; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q99962; protein.
DR Bgee; ENSG00000107295; Expressed in Brodmann (1909) area 23 and 132 other tissues.
DR Genevisible; Q99962; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0097484; P:dendrite extension; ISS:UniProtKB.
DR GO; GO:1905604; P:negative regulation of blood-brain barrier permeability; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
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; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF07653; SH3_2; 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 3D-structure; Cell projection; Coiled coil; Cytoplasm; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW SH3 domain; Synapse.
FT CHAIN 1..352
FT /note="Endophilin-A1"
FT /id="PRO_0000146747"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 290..349
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..125
FT /note="Binds and tubulates liposomes"
FT /evidence="ECO:0000250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..21
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000269|PubMed:16763557"
FT REGION 60..87
FT /note="Required for dimerization upon membrane association"
FT /evidence="ECO:0000250"
FT REGION 245..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..248
FT /evidence="ECO:0000255"
FT COMPBIAS 265..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62420"
FT MOD_RES 299
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62419"
FT MUTAGEN 63
FT /note="A->S: Reduced tubulation of liposomes, 3-fold
FT increase in tubule diameter, no effect on liposome binding;
FT when associated with S-66 or with S-66 and Q-70."
FT /evidence="ECO:0000269|PubMed:16763557"
FT MUTAGEN 66
FT /note="A->D: Loss of tubulation of liposomes, no effect on
FT liposome binding."
FT /evidence="ECO:0000269|PubMed:16763557"
FT MUTAGEN 66
FT /note="A->S: Reduced tubulation of liposomes, 3-fold
FT increase in tubule diameter, no effect on liposome binding;
FT when associated with S-63 or with S-63 and Q-70."
FT /evidence="ECO:0000269|PubMed:16763557"
FT MUTAGEN 66
FT /note="A->W: Vesiculation of liposomes, no effect on
FT liposome binding, indol ring located in hydrophobic core of
FT the membrane."
FT /evidence="ECO:0000269|PubMed:16763557"
FT MUTAGEN 70
FT /note="M->Q: Reduced tubulation of liposomes, 3-fold
FT increase in tubule diameter, no effect on liposome binding;
FT when associated with S-63 and S-66."
FT /evidence="ECO:0000269|PubMed:16763557"
FT MUTAGEN 202
FT /note="F->W: No effect. Indol ring not associated with the
FT membrane."
FT /evidence="ECO:0000269|PubMed:16763557"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 24..58
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1X03"
FT HELIX 89..104
FT /evidence="ECO:0007829|PDB:2D4C"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 110..138
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 150..175
FT /evidence="ECO:0007829|PDB:2D4C"
FT HELIX 180..246
FT /evidence="ECO:0007829|PDB:2D4C"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:2DBM"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2DBM"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:2DBM"
FT STRAND 335..348
FT /evidence="ECO:0007829|PDB:2DBM"
SQ SEQUENCE 352 AA; 39962 MW; F3AE2353E1EB7CF3 CRC64;
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI MTKTIEYLQP
NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF GRELGDDCNF GPALGEVGEA
MRELSEVKDS LDIEVKQNFI DPLQNLHDKD LREIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF DESKEIAESS MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL
EERIRQASSQ PRREYQPKPR MSLEFPTGDS TQPNGGLSHT GTPKPSGVQM DQPCCRALYD
FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGHSGFFP INYVEILVAL PH
