GenomeNet

Database: UniProt
Entry: Q99963
LinkDB: Q99963
Original site: Q99963 
ID   SH3G3_HUMAN             Reviewed;         347 AA.
AC   Q99963; O43553; O43554;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   09-JUL-2014, entry version 136.
DE   RecName: Full=Endophilin-A3;
DE   AltName: Full=EEN-B2;
DE   AltName: Full=Endophilin-3;
DE   AltName: Full=SH3 domain protein 2C;
DE   AltName: Full=SH3 domain-containing GRB2-like protein 3;
GN   Name=SH3GL3; Synonyms=CNSA3, SH3D2C;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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
RT   the central nervous system.";
RL   Genomics 41:427-434(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
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
RT   are preferentially expressed in human brain.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH HUNTINGTIN EXON 1 PROTEIN.
RX   PubMed=9809064; DOI=10.1016/S1097-2765(00)80142-2;
RA   Sittler A., Walter S., Wedemeyer N., Hasenbank R., Scherzinger E.,
RA   Eickhoff H., Bates G.P., Lehrach H., Wanker E.E.;
RT   "SH3GL3 associates with the Huntingtin exon 1 protein and promotes the
RT   formation of polygln-containing protein aggregates.";
RL   Mol. Cell 2:427-436(1998).
RN   [4]
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.,
RA   Migone N., Hoffmueller U., Schneider-Mergener J., Cesareni G.;
RT   "The SH3 domains of endophilin and amphiphysin bind to the proline-
RT   rich region of synaptojanin 1 at distinct sites that display an
RT   unconventional binding specificity.";
RL   J. Biol. Chem. 274:32001-32007(1999).
RN   [5]
RP   INTERACTION WITH SGIP1.
RX   PubMed=15919751; DOI=10.1210/en.2005-0282;
RA   Trevaskis J., Walder K., Foletta V., Kerr-Bayles L., McMillan J.,
RA   Cooper A., Lee S., Bolton K., Prior M., Fahey R., Whitecross K.,
RA   Morton G.J., Schwartz M.W., Collier G.R.;
RT   "Src homology 3-domain growth factor receptor-bound 2-like
RT   (endophilin) interacting protein 1, a novel neuronal protein that
RT   regulates energy balance.";
RL   Endocrinology 146:3757-3764(2005).
RN   [6]
RP   INTERACTION WITH ATX2.
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
RT   receptor trafficking.";
RL   Cell. Signal. 20:1725-1739(2008).
RN   [7]
RP   INTERACTION WITH FASLG.
RX   PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA   Voss M., Lettau M., Janssen O.;
RT   "Identification of SH3 domain interaction partners of human FasL
RT   (CD178) by phage display screening.";
RL   BMC Immunol. 10:53-53(2009).
RN   [8]
RP   INTERACTION WITH DYDC1.
RX   PubMed=19545932; DOI=10.1016/j.ejcb.2009.05.001;
RA   Li S., Qiao Y., Di Q., Le X., Zhang L., Zhang X., Zhang C., Cheng J.,
RA   Zong S., Koide S.S., Miao S., Wang L.;
RT   "Interaction of SH3P13 and DYDC1 protein: a germ cell component that
RT   regulates acrosome biogenesis during spermiogenesis.";
RL   Eur. J. Cell Biol. 88:509-520(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 22-256.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of BAR domain of endophilin-III.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC       membranes with high curvature (By similarity).
CC   -!- SUBUNIT: Interacts with ARC (By similarity). Interacts with DNM1,
CC       SGIP1 and SYNJ1. Interacts with the huntingtin exon 1 protein
CC       (HDEX1P) containing a glutamine repeat in the pathological range
CC       and promotes formation of insoluble polyglutamine-containing
CC       aggregates in vivo. Interacts with DYDC1. Interacts with FASLG.
CC       Interacts with ATX2. Interacts with BIN2.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-473910, EBI-473910;
CC       Q99700:ATXN2; NbExp=11; IntAct=EBI-473910, EBI-697691;
CC       P42858:HTT; NbExp=9; IntAct=EBI-473910, EBI-466029;
CC       Q99961:SH3GL1; NbExp=4; IntAct=EBI-473910, EBI-697911;
CC       Q99962:SH3GL2; NbExp=5; IntAct=EBI-473910, EBI-77938;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC       Note=Associated with postsynaptic endosomes in hippocampal
CC       neurons. Associated with presynaptic endosomes in olfactory
CC       neurons (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=EEN-B2-L1;
CC         IsoId=Q99963-1; Sequence=Displayed;
CC       Name=2; Synonyms=EEN-B2-L2;
CC         IsoId=Q99963-2; Sequence=VSP_001441;
CC       Name=3; Synonyms=EEN-B2-L3;
CC         IsoId=Q99963-3; Sequence=VSP_001440;
CC       Name=4; Synonyms=EEN-B2-L4;
CC         IsoId=Q99963-4; Sequence=VSP_001442;
CC   -!- TISSUE SPECIFICITY: Brain and testis.
CC   -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a
CC       second amphipathic helix inserted into helix 1 of the BAR domain
CC       (N-BAR domain) induce membrane curvature and bind curved membranes
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the endophilin family.
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; X99664; CAA67978.1; -; mRNA.
DR   EMBL; AF036269; AAC04765.1; -; mRNA.
DR   EMBL; AF036270; AAC04766.1; -; mRNA.
DR   EMBL; AF036271; AAC04767.1; -; mRNA.
DR   EMBL; AF036272; AAC04768.1; -; mRNA.
DR   CCDS; CCDS10325.2; -. [Q99963-1]
DR   RefSeq; NP_003018.3; NM_003027.3. [Q99963-1]
DR   RefSeq; XP_006720701.1; XM_006720638.1. [Q99963-3]
DR   UniGene; Hs.270055; -.
DR   UniGene; Hs.666365; -.
DR   PDB; 2EW3; NMR; -; A=285-345.
DR   PDB; 2Z0V; X-ray; 2.49 A; A/B=24-256.
DR   PDBsum; 2EW3; -.
DR   PDBsum; 2Z0V; -.
DR   ProteinModelPortal; Q99963; -.
DR   SMR; Q99963; 30-252, 285-344.
DR   BioGrid; 112354; 40.
DR   IntAct; Q99963; 38.
DR   MINT; MINT-128532; -.
DR   STRING; 9606.ENSP00000391372; -.
DR   PhosphoSite; Q99963; -.
DR   DMDM; 12643798; -.
DR   MaxQB; Q99963; -.
DR   PaxDb; Q99963; -.
DR   PRIDE; Q99963; -.
DR   DNASU; 6457; -.
DR   Ensembl; ENST00000324537; ENSP00000320092; ENSG00000140600. [Q99963-3]
DR   Ensembl; ENST00000427482; ENSP00000391372; ENSG00000140600. [Q99963-1]
DR   Ensembl; ENST00000434347; ENSP00000397871; ENSG00000140600. [Q99963-3]
DR   GeneID; 6457; -.
DR   KEGG; hsa:6457; -.
DR   UCSC; uc002bju.3; human. [Q99963-3]
DR   UCSC; uc002bjw.3; human. [Q99963-1]
DR   CTD; 6457; -.
DR   GeneCards; GC15P084115; -.
DR   H-InvDB; HIX0026775; -.
DR   HGNC; HGNC:10832; SH3GL3.
DR   HPA; HPA039381; -.
DR   MIM; 603362; gene.
DR   neXtProt; NX_Q99963; -.
DR   PharmGKB; PA35738; -.
DR   eggNOG; NOG307129; -.
DR   HOGENOM; HOG000231641; -.
DR   HOVERGEN; HBG052866; -.
DR   InParanoid; Q99963; -.
DR   KO; K11247; -.
DR   OMA; ENDTEHV; -.
DR   OrthoDB; EOG7G1V6H; -.
DR   PhylomeDB; Q99963; -.
DR   TreeFam; TF313281; -.
DR   EvolutionaryTrace; Q99963; -.
DR   GeneWiki; SH3GL3; -.
DR   GenomeRNAi; 6457; -.
DR   NextBio; 25097; -.
DR   PRO; PR:Q99963; -.
DR   ArrayExpress; Q99963; -.
DR   Bgee; Q99963; -.
DR   CleanEx; HS_SH3GL3; -.
DR   Genevestigator; Q99963; -.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR-dom.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR028501; Endophilin-A.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10661:SF120; PTHR10661:SF120; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 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; Alternative splicing; Coiled coil; Complete proteome;
KW   Cytoplasm; Endocytosis; Endosome; Lipid-binding; Membrane;
KW   Reference proteome; SH3 domain.
FT   CHAIN         1    347       Endophilin-A3.
FT                                /FTId=PRO_0000146750.
FT   DOMAIN       18    249       BAR.
FT   DOMAIN      285    344       SH3.
FT   REGION        1     21       Membrane-binding amphipathic helix (By
FT                                similarity).
FT   REGION       60     87       Required for dimerization upon membrane
FT                                association (By similarity).
FT   REGION      218    254       Interaction with ARC (By similarity).
FT   COILED      181    201       Potential.
FT   VAR_SEQ       1     69       Missing (in isoform 2).
FT                                /FTId=VSP_001441.
FT   VAR_SEQ       1     14       MSVAGLKKQFHKAS -> MDGIFAGIICNQANRCLTWTSQ
FT                                (in isoform 3).
FT                                /FTId=VSP_001440.
FT   VAR_SEQ     311    347       IITLTNQIDENWYEGMIHGESGFFPINYVEVIVPLPQ ->
FT                                GTFRKIKRETKIKMCRKKIVNIYKLKDQQH (in
FT                                isoform 4).
FT                                /FTId=VSP_001442.
FT   HELIX        31     58
FT   HELIX        62     69
FT   HELIX        89    104
FT   HELIX       109    138
FT   HELIX       140    148
FT   HELIX       150    172
FT   TURN        173    176
FT   HELIX       180    206
FT   HELIX       209    246
FT   STRAND      289    294
FT   STRAND      311    327
FT   STRAND      330    335
FT   HELIX       336    338
FT   STRAND      339    342
SQ   SEQUENCE   347 AA;  39285 MW;  D68DA7B28574C4E6 CRC64;
     MSVAGLKKQF HKASQLFSEK ISGAEGTKLD DEFLDMERKI DVTNKVVAEI LSKTTEYLQP
     NPAYRAKLGM LNTVSKIRGQ VKTTGYPQTE GLLGDCMLKY GKELGEDSTF GNALIEVGES
     MKLMAEVKDS LDINVKQTFI DPLQLLQDKD LKEIGHHLKK LEGRRLDYDY KKKRVGKIPD
     EEVRQAVEKF EESKELAERS MFNFLENDVE QVSQLAVFIE AALDYHRQST EILQELQSKL
     QMRISAASSV PRREYKPRPV KRSSSELNGV STTSVVKTTG SNIPMDQPCC RGLYDFEPEN
     QGELGFKEGD IITLTNQIDE NWYEGMIHGE SGFFPINYVE VIVPLPQ
//
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