SH3G3_RAT
ID SH3G3_RAT Reviewed; 347 AA.
AC O35180; O35104;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=Sh3d2c1, Sh3p13;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 57-347, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH DNM1 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-347.
RA Yamagata K.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH DNM1 AND SYNJ1.
RX PubMed=15066995; DOI=10.1074/jbc.m312607200;
RA Sugiura H., Iwata K., Matsuoka M., Hayashi H., Takemiya T., Yasuda S.,
RA Ichikawa M., Yamauchi T., Mehlen P., Haga T., Yamagata K.;
RT "Inhibitory role of endophilin 3 in receptor-mediated endocytosis.";
RL J. Biol. Chem. 279:23343-23348(2004).
RN [5]
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).
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature. {ECO:0000269|PubMed:15066995}.
CC -!- SUBUNIT: Interacts with SGIP1 and DYDC1 (By similarity). Interacts with
CC FASLG. Interacts with ATXN2. Interacts with BIN2 (By similarity).
CC Interacts with ARC, DNM1 and SYNJ1. {ECO:0000250,
CC ECO:0000269|PubMed:15066995, ECO:0000269|PubMed:17088211,
CC ECO:0000269|PubMed:9238017}.
CC -!- INTERACTION:
CC O35180; P21575: Dnm1; NbExp=2; IntAct=EBI-1149266, EBI-80070;
CC O35180; Q62910: Synj1; NbExp=2; IntAct=EBI-1149266, EBI-1149123;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17088211,
CC ECO:0000269|PubMed:9238017}. Early endosome membrane
CC {ECO:0000269|PubMed:17088211}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17088211}. Note=Associated with postsynaptic
CC endosomes in hippocampal neurons. Associated with presynaptic endosomes
CC in olfactory neurons. {ECO:0000269|PubMed:17088211}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in testis and at lower
CC level in brain and liver. {ECO:0000269|PubMed:15066995,
CC 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 -!- MISCELLANEOUS: Cells overexpressing Sh3gl3 show inhibition of
CC transferrin uptake. Olfactory epithelium-derived cells overexpressing
CC SH3GL3, DRD2 and GRK2 show accelerated differentiation upon addition of
CC apomorphine due to reduced agonist-induced endocytosis of DRD2.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
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DR EMBL; AC128742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF009604; AAC14884.1; -; mRNA.
DR EMBL; AB008159; BAA22920.2; -; mRNA.
DR RefSeq; XP_006229542.1; XM_006229480.3.
DR RefSeq; XP_006229547.1; XM_006229485.1.
DR AlphaFoldDB; O35180; -.
DR SMR; O35180; -.
DR BioGRID; 249696; 1.
DR ELM; O35180; -.
DR IntAct; O35180; 3.
DR STRING; 10116.ENSRNOP00000026870; -.
DR iPTMnet; O35180; -.
DR PhosphoSitePlus; O35180; -.
DR PaxDb; O35180; -.
DR PRIDE; O35180; -.
DR Ensembl; ENSRNOT00000096616; ENSRNOP00000095576; ENSRNOG00000019776.
DR GeneID; 81921; -.
DR CTD; 6457; -.
DR RGD; 620578; Sh3gl3.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000157398; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; O35180; -.
DR OMA; NFLENDX; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; O35180; -.
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 PRO; PR:O35180; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019776; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; O35180; baseline and differential.
DR Genevisible; O35180; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:CACAO.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098845; C:postsynaptic endosome; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; IMP:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:RGD.
DR GO; GO:0016191; P:synaptic vesicle uncoating; ISO:RGD.
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_0000146752"
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..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..201
FT /evidence="ECO:0000255"
FT COMPBIAS 258..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 107
FT /note="D -> H (in Ref. 2; AAC14884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39166 MW; D229D63BC7DA3733 CRC64;
MSVAGLKKQF HKASQLFSEK ISGAEGTKLD EEFLDMEKKI DITSKAVAEI LSKATEYLQP
NPAYRAKLGM LNTMSKLRGQ VKATGYPQTE GLLGDCMLKY GRELGEDSAF GNSLVEVGEA
LKLMAEVKDS LDINVKQTFI DPLQLLQDKD LKEIGHHLRK LEGRRLDYDY KKKRVGKIPE
EEIRQAVEKF EESKELAERS MFNFLENDVE QVSQLAVFVE AALDYHRQST EILQELQNKL
ELRIALASQV PRRDYMPKPV NTSSTNANGV EPSSSSKLTG TDIPSDQPCC RGLYDFEPEN
EGELGFKEGD IITLTNQIDE NWYEGMLRGE SGFFPINYVE VIVPLPR
