Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O35179 (SH3G2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endophilin-A1
Alternative name(s):
Endophilin-1
SH3 domain protein 2A
SH3 domain-containing GRB2-like protein 2
SH3p4
Gene names
Name:Sh3gl2
Synonyms:Sh3d2a, Sh3p4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Ref.5 Ref.10

Subunit structure

Monomer; in cytoplasm. Homodimer; when associated with membranes By similarity. Interacts with SYNJ1 and DNM1. Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation. Interacts with PDCD6IP By similarity. Interacts with OPHN1. Interacts with ADAM9 and ADAM15 cytoplasmic tails. Interacts with BIN2 By similarity. Ref.3 Ref.4 Ref.8 Ref.10

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Note: Concentrated in presynaptic nerve terminals in neurons. Ref.3

Tissue specificity

Brain. Expressed at low level in the kidney. Ref.3

Domain

An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface. Ref.5 Ref.9 Ref.10

Miscellaneous

The N-BAR domain binds liposomes and mediates dimerization of BAR domains upon liposome binding. It induces formation of tubules from liposomes as well as fusion of liposome tubules. Cells overexpressing Sh3gl2 show no effect on transferrin uptake.

Sequence similarities

Belongs to the endophilin family.

Contains 1 BAR domain.

Contains 1 SH3 domain.

Ontologies

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Endophilin-A1
PRO_0000146749

Regions

Domain18 – 249232BAR
Domain290 – 34960SH3
Region1 – 125125Binds and tubulates liposomes
Region1 – 2121Membrane-binding amphipathic helix
Region60 – 8728Required for dimerization upon membrane association
Coiled coil181 – 25070 Potential

Experimental info

Mutagenesis2631L → P: Confers inhibition of transferrin uptake comparable to Sh3gl3 upon overexpression. Ref.6
Sequence conflict781R → H in AI044966. Ref.1

Secondary structure

....................... 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35179 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 382B6F651885B679

FASTA35239,899
        10         20         30         40         50         60 
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI MTKTIEYLQP 

        70         80         90        100        110        120 
NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF GRELGDDCNF GPALGEVGEA 

       130        140        150        160        170        180 
MRELSEVKDS LDMEVKQNFI DPLQNLHDKD LREIQHHLKK LEGRRLDFDY KKKRQGKIPD 

       190        200        210        220        230        240 
EELRQALEKF DESKEIAESS MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL 

       250        260        270        280        290        300 
EERIRQASSQ PRREYQPKPR MSLEFATGDG TQPNGGLSHT GTPKPAGVQM DQPCCRALYD 

       310        320        330        340        350 
FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGQSGFFP INYVEILVAL PH 

« Hide

References

« Hide 'large scale' references
[1]"Normalization and subtraction: two approaches to facilitate gene discovery."
Bonaldo M.F., Lennon G., Soares M.B.
Genome Res. 6:791-806(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 15-352.
Strain: Brown Norway.
[3]"The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain."
Ringstad N., Nemoto Y., De Camilli P.
Proc. Natl. Acad. Sci. U.S.A. 94:8569-8574(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-352, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH DNM1 AND SYNJ1.
Tissue: Brain.
[4]"Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase."
Ramjaun A.R., Angers A., Legendre-Guillemin V., Tong X.-K., McPherson P.S.
J. Biol. Chem. 276:28913-28919(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP4K3; SYNJ1 AND DNM1.
[5]"Generation of high curvature membranes mediated by direct endophilin bilayer interactions."
Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P.
J. Cell Biol. 155:193-200(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN.
[6]"Inhibitory role of endophilin 3 in receptor-mediated endocytosis."
Sugiura H., Iwata K., Matsuoka M., Hayashi H., Takemiya T., Yasuda S., Ichikawa M., Yamauchi T., Mehlen P., Haga T., Yamagata K.
J. Biol. Chem. 279:23343-23348(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-263.
[7]"Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission."
Gallop J.L., Butler P.J., McMahon H.T.
Nature 438:675-678(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT SH3GL2 HAS NO LYSOPHOSPHATIDIC ACID ACYLTRANSFERASE ACTIVITY.
[8]"The Rho-linked mental retardation protein OPHN1 controls synaptic vesicle endocytosis via endophilin A1."
Nakano-Kobayashi A., Kasri N.N., Newey S.E., Van Aelst L.
Curr. Biol. 19:1133-1139(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OPHN1.
[9]"Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms."
Masuda M., Takeda S., Sone M., Ohki T., Mori H., Kamioka Y., Mochizuki N.
EMBO J. 25:2889-2897(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 291-352, DOMAIN.
[10]"Mechanism of endophilin N-BAR domain-mediated membrane curvature."
Gallop J.L., Jao C.C., Kent H.M., Butler P.J., Evans P.R., Langen R., McMahon H.T.
EMBO J. 25:2898-2910(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 25-247, FUNCTION, SUBUNIT, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AI044966 mRNA. No translation available.
AC112121 mRNA. No translation available.
AF009603 mRNA. Translation: AAC14883.1.
RefSeqNP_446387.1. NM_053935.1.
UniGeneRn.10787.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C08X-ray2.90A25-247[»]
2KNBNMR-B291-352[»]
3IQLX-ray1.40A/B291-352[»]
ProteinModelPortalO35179.
SMRO35179. Positions 9-247, 293-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250599. 2 interactions.
IntActO35179. 5 interactions.
MINTMINT-1037287.
STRING10116.ENSRNOP00000008999.

Proteomic databases

PaxDbO35179.
PRIDEO35179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116743.
KEGGrno:116743.
UCSCRGD:620276. rat.

Organism-specific databases

CTD6456.
RGD620276. Sh3gl2.

Phylogenomic databases

eggNOGNOG307129.
HOGENOMHOG000231641.
HOVERGENHBG052866.
InParanoidO35179.
KOK11247.
PhylomeDBO35179.

Enzyme and pathway databases

ReactomeREACT_212996. Signal Transduction.

Gene expression databases

ArrayExpressO35179.
GenevestigatorO35179.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR028501. Endophilin-A.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERPTHR10661:SF113. PTHR10661:SF113. 1 hit.
PfamPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO35179.
NextBio619680.
PROO35179.

Entry information

Entry nameSH3G2_RAT
AccessionPrimary (citable) accession number: O35179
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 23, 2007
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references