SH3G1_RAT
ID SH3G1_RAT Reviewed; 368 AA.
AC O35964;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
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=Sh3p8;
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 [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH DNM1
RP AND SYNJ1.
RC TISSUE=Brain;
RX PubMed=9238017; DOI=10.1073/pnas.94.16.8569;
RA Ringstad N., Nemoto Y., De Camilli P.;
RT "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin
RT and dynamin via a Grb2-like Src homology 3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8569-8574(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamagata K.;
RT "Rattus norvegicus SH3P8 mRNA, complete cds.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ARC.
RX PubMed=17088211; DOI=10.1016/j.neuron.2006.08.033;
RA Chowdhury S., Shepherd J.D., Okuno H., Lyford G., Petralia R.S., Plath N.,
RA Kuhl D., Huganir R.L., Worley P.F.;
RT "Arc/Arg3.1 interacts with the endocytic machinery to regulate AMPA
RT receptor trafficking.";
RL Neuron 52:445-459(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP 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).
RN [6]
RP INTERACTION WITH BIN2, AND TISSUE SPECIFICITY.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 303-368.
RX PubMed=18391417; DOI=10.1107/s1744309108007574;
RA Loll P.J., Swain E., Chen Y., Turner B.T., Zhang J.F.;
RT "Structure of the SH3 domain of rat endophilin A2.";
RL Acta Crystallogr. F 64:243-246(2008).
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 (By
CC similarity). Interacts with BIN2. {ECO:0000250,
CC ECO:0000269|PubMed:17088211, ECO:0000269|PubMed:23285027,
CC ECO:0000269|PubMed:9238017}.
CC -!- INTERACTION:
CC O35964; Q70E73: RAPH1; Xeno; NbExp=13; IntAct=EBI-1149235, EBI-3940924;
CC O35964; O43295: SRGAP3; Xeno; NbExp=3; IntAct=EBI-1149235, EBI-368166;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17088211}. Early
CC endosome membrane {ECO:0000269|PubMed:17088211}; Peripheral membrane
CC protein {ECO:0000269|PubMed:17088211}. Cell projection, podosome
CC {ECO:0000250}. Note=Associated with postsynaptic endosomes in
CC hippocampal neurons.
CC -!- TISSUE SPECIFICITY: Detected in brain and testis (at protein level).
CC Ubiquitous. {ECO:0000269|PubMed:23285027, ECO:0000269|PubMed:9238017}.
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; AF009602; AAC14882.1; -; mRNA.
DR EMBL; AB008161; BAA22921.1; -; mRNA.
DR EMBL; BC070893; AAH70893.1; -; mRNA.
DR RefSeq; NP_112518.1; NM_031239.2.
DR PDB; 3C0C; X-ray; 1.70 A; A=303-368.
DR PDBsum; 3C0C; -.
DR AlphaFoldDB; O35964; -.
DR SMR; O35964; -.
DR BioGRID; 249697; 4.
DR CORUM; O35964; -.
DR ELM; O35964; -.
DR IntAct; O35964; 10.
DR MINT; O35964; -.
DR STRING; 10116.ENSRNOP00000066789; -.
DR iPTMnet; O35964; -.
DR PhosphoSitePlus; O35964; -.
DR SwissPalm; O35964; -.
DR jPOST; O35964; -.
DR PaxDb; O35964; -.
DR PRIDE; O35964; -.
DR ABCD; O35964; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000074695; ENSRNOP00000066789; ENSRNOG00000049683.
DR Ensembl; ENSRNOT00000110808; ENSRNOP00000084032; ENSRNOG00000049683.
DR GeneID; 81922; -.
DR KEGG; rno:81922; -.
DR CTD; 6455; -.
DR RGD; 708456; Sh3gl1.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000154737; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; O35964; -.
DR OMA; QYLSETM; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; O35964; -.
DR Reactome; R-RNO-182971; EGFR downregulation.
DR Reactome; R-RNO-6807004; Negative regulation of MET activity.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; O35964; -.
DR PRO; PR:O35964; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000049683; Expressed in lung and 20 other tissues.
DR Genevisible; O35964; RN.
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:RGD.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; IMP:RGD.
DR GO; GO:0051020; F:GTPase binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IMP:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IMP:RGD.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:0016191; P:synaptic vesicle uncoating; ISO:RGD.
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 3D-structure; Cell junction; Cell projection; Coiled coil; Cytoplasm;
KW Endocytosis; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..368
FT /note="Endophilin-A2"
FT /id="PRO_0000146746"
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:0000269|PubMed:17088211"
FT REGION 243..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..250
FT /evidence="ECO:0000255"
FT COMPBIAS 243..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99961"
FT MOD_RES 315
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62419"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:3C0C"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3C0C"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:3C0C"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3C0C"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3C0C"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3C0C"
SQ SEQUENCE 368 AA; 41492 MW; C14F4357386F35FE CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFREMEKKV DITSKAVAEV LVRTIEYLQP
NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMVRH GKELGGESNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILEELADKL
KRRVREASSR PRREFKPRPQ EPFELGELEQ PNGGFPCASA PKITASSSFR SGDKPTRTPS
KSMPPLDQPS CKALYDFEPE NDGELGFREG DLITLTNQID ENWYEGMLHG QSGFFPLSYV
QVLVPLPQ
