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O35179

- SH3G2_RAT

UniProt

O35179 - SH3G2_RAT

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Protein

Endophilin-A1

Gene

Sh3gl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.2 Publications

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of receptor internalization Source: Ensembl
  2. synaptic vesicle endocytosis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_198830. MHC class II antigen presentation.
REACT_235514. Retrograde neurotrophin signalling.
REACT_241654. EGFR downregulation.
REACT_249039. Lysosome Vesicle Biogenesis.
REACT_261496. Golgi Associated Vesicle Biogenesis.
REACT_262886. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Endophilin-A1
Alternative name(s):
Endophilin-1
SH3 domain protein 2A
SH3 domain-containing GRB2-like protein 2
SH3p4
Gene namesi
Name:Sh3gl2
Synonyms:Sh3d2a, Sh3p4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620276. Sh3gl2.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication
Note: Concentrated in presynaptic nerve terminals in neurons.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi263 – 2631L → P: Confers inhibition of transferrin uptake comparable to Sh3gl3 upon overexpression. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Endophilin-A1PRO_0000146749Add
BLAST

Proteomic databases

PaxDbiO35179.
PRIDEiO35179.

Expressioni

Tissue specificityi

Brain. Expressed at low level in the kidney.1 Publication

Gene expression databases

ExpressionAtlasiO35179. baseline and differential.
GenevestigatoriO35179.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Dnm1P215756EBI-1149197,EBI-80070
Synj1Q629102EBI-1149197,EBI-1149123

Protein-protein interaction databases

BioGridi250599. 2 interactions.
IntActiO35179. 5 interactions.
MINTiMINT-1037287.
STRINGi10116.ENSRNOP00000008999.

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi89 – 10416Combined sources
Beta strandi106 – 1094Combined sources
Helixi110 – 13829Combined sources
Helixi140 – 17334Combined sources
Turni174 – 1774Combined sources
Helixi180 – 20526Combined sources
Helixi208 – 24538Combined sources
Beta strandi294 – 2996Combined sources
Beta strandi316 – 3227Combined sources
Beta strandi324 – 3329Combined sources
Beta strandi335 – 3406Combined sources
Helixi341 – 3433Combined sources
Beta strandi344 – 3485Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C08X-ray2.90A25-67[»]
A87-247[»]
2KNBNMR-B291-352[»]
3IQLX-ray1.40A/B291-352[»]
ProteinModelPortaliO35179.
SMRiO35179. Positions 9-247, 293-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35179.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 249232BARPROSITE-ProRule annotationAdd
BLAST
Domaini290 – 34960SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 125125Binds and tubulates liposomesAdd
BLAST
Regioni1 – 2121Membrane-binding amphipathic helixAdd
BLAST
Regioni60 – 8728Required for dimerization upon membrane associationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili181 – 25070Sequence AnalysisAdd
BLAST

Domaini

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.3 Publications

Sequence similaritiesi

Belongs to the endophilin family.Curated
Contains 1 BAR domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG307129.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiO35179.
KOiK11247.
PhylomeDBiO35179.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR028501. Endophilin-A.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERiPTHR10661:SF113. PTHR10661:SF113. 1 hit.
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35179-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI
60 70 80 90 100
MTKTIEYLQP NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF
110 120 130 140 150
GRELGDDCNF GPALGEVGEA MRELSEVKDS LDMEVKQNFI DPLQNLHDKD
160 170 180 190 200
LREIQHHLKK LEGRRLDFDY KKKRQGKIPD EELRQALEKF DESKEIAESS
210 220 230 240 250
MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL EERIRQASSQ
260 270 280 290 300
PRREYQPKPR MSLEFATGDG TQPNGGLSHT GTPKPAGVQM DQPCCRALYD
310 320 330 340 350
FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGQSGFFP INYVEILVAL

PH
Length:352
Mass (Da):39,899
Last modified:October 23, 2007 - v2
Checksum:i382B6F651885B679
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781R → H in AI044966. (PubMed:8889548)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AI044966 mRNA. No translation available.
AC112121 mRNA. No translation available.
AF009603 mRNA. Translation: AAC14883.1.
RefSeqiNP_446387.1. NM_053935.1.
UniGeneiRn.10787.

Genome annotation databases

GeneIDi116743.
KEGGirno:116743.
UCSCiRGD:620276. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AI044966 mRNA. No translation available.
AC112121 mRNA. No translation available.
AF009603 mRNA. Translation: AAC14883.1 .
RefSeqi NP_446387.1. NM_053935.1.
UniGenei Rn.10787.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C08 X-ray 2.90 A 25-67 [» ]
A 87-247 [» ]
2KNB NMR - B 291-352 [» ]
3IQL X-ray 1.40 A/B 291-352 [» ]
ProteinModelPortali O35179.
SMRi O35179. Positions 9-247, 293-352.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250599. 2 interactions.
IntActi O35179. 5 interactions.
MINTi MINT-1037287.
STRINGi 10116.ENSRNOP00000008999.

Proteomic databases

PaxDbi O35179.
PRIDEi O35179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 116743.
KEGGi rno:116743.
UCSCi RGD:620276. rat.

Organism-specific databases

CTDi 6456.
RGDi 620276. Sh3gl2.

Phylogenomic databases

eggNOGi NOG307129.
HOGENOMi HOG000231641.
HOVERGENi HBG052866.
InParanoidi O35179.
KOi K11247.
PhylomeDBi O35179.

Enzyme and pathway databases

Reactomei REACT_198830. MHC class II antigen presentation.
REACT_235514. Retrograde neurotrophin signalling.
REACT_241654. EGFR downregulation.
REACT_249039. Lysosome Vesicle Biogenesis.
REACT_261496. Golgi Associated Vesicle Biogenesis.
REACT_262886. Recycling pathway of L1.

Miscellaneous databases

EvolutionaryTracei O35179.
NextBioi 619680.
PROi O35179.

Gene expression databases

ExpressionAtlasi O35179. baseline and differential.
Genevestigatori O35179.

Family and domain databases

Gene3Di 1.20.1270.60. 1 hit.
InterProi IPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR028501. Endophilin-A.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view ]
PANTHERi PTHR10661:SF113. PTHR10661:SF113. 1 hit.
Pfami PF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTi SM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSH3G2_RAT
AccessioniPrimary (citable) accession number: O35179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 23, 2007
Last modified: November 26, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3