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O35179

- SH3G2_RAT

UniProt

O35179 - SH3G2_RAT

Protein

Endophilin-A1

Gene

Sh3gl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (23 Oct 2007)
      Previous versions | rss
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    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
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_198830. MHC class II antigen presentation.

    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-SubCell
    2. plasma membrane Source: Reactome

    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

    ArrayExpressiO35179.
    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 – 10416
    Beta strandi106 – 1094
    Helixi110 – 13829
    Helixi140 – 17334
    Turni174 – 1774
    Helixi180 – 20526
    Helixi208 – 24538
    Beta strandi294 – 2996
    Beta strandi316 – 3227
    Beta strandi324 – 3329
    Beta strandi335 – 3406
    Helixi341 – 3433
    Beta strandi344 – 3485

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C08X-ray2.90A25-247[»]
    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

    MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI    50
    MTKTIEYLQP NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF 100
    GRELGDDCNF GPALGEVGEA MRELSEVKDS LDMEVKQNFI DPLQNLHDKD 150
    LREIQHHLKK LEGRRLDFDY KKKRQGKIPD EELRQALEKF DESKEIAESS 200
    MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL EERIRQASSQ 250
    PRREYQPKPR MSLEFATGDG TQPNGGLSHT GTPKPAGVQM DQPCCRALYD 300
    FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGQSGFFP INYVEILVAL 350
    PH 352
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C08 X-ray 2.90 A 25-247 [» ]
    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.

    Miscellaneous databases

    EvolutionaryTracei O35179.
    NextBioi 619680.
    PROi O35179.

    Gene expression databases

    ArrayExpressi O35179.
    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

    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: October 1, 2014
    This is version 126 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