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Protein

Endophilin-A1

Gene

Sh3gl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.
R-RNO-182971. EGFR downregulation.
R-RNO-2132295. MHC class II antigen presentation.
R-RNO-432720. Lysosome Vesicle Biogenesis.
R-RNO-432722. Golgi Associated Vesicle Biogenesis.
R-RNO-437239. Recycling pathway of L1.
R-RNO-6807004. Negative regulation of MET activity.
R-RNO-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-RNO-8856828. Clathrin-mediated endocytosis.

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
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi620276. Sh3gl2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi263L → P: Confers inhibition of transferrin uptake comparable to Sh3gl3 upon overexpression. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467491 – 352Endophilin-A1Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei262PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35179.
PRIDEiO35179.

PTM databases

iPTMnetiO35179.
PhosphoSitePlusiO35179.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000006761.
ExpressionAtlasiO35179. baseline and differential.
GenevisibleiO35179. RN.

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
SRGAP3O432953EBI-1149197,EBI-368166From a different organism.
Synj1Q629102EBI-1149197,EBI-1149123

Protein-protein interaction databases

BioGridi250599. 2 interactors.
IntActiO35179. 10 interactors.
MINTiMINT-1037287.
STRINGi10116.ENSRNOP00000008999.

Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi89 – 104Combined sources16
Beta strandi106 – 109Combined sources4
Helixi110 – 138Combined sources29
Helixi140 – 173Combined sources34
Turni174 – 177Combined sources4
Helixi180 – 205Combined sources26
Helixi208 – 245Combined sources38
Beta strandi294 – 299Combined sources6
Beta strandi316 – 322Combined sources7
Beta strandi324 – 332Combined sources9
Beta strandi335 – 340Combined sources6
Helixi341 – 343Combined sources3
Beta strandi344 – 348Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO35179.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 249BARPROSITE-ProRule annotationAdd BLAST232
Domaini290 – 349SH3PROSITE-ProRule annotationAdd BLAST60

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 125Binds and tubulates liposomesAdd BLAST125
Regioni1 – 21Membrane-binding amphipathic helixAdd BLAST21
Regioni60 – 87Required for dimerization upon membrane associationAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili181 – 250Sequence analysisAdd BLAST70

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

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiO35179.
KOiK11247.
OMAiGGLSHTS.
OrthoDBiEOG091G16FW.
PhylomeDBiO35179.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00018. SH3_1. 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)DescriptionActionsGraphical viewLength
Sequence conflicti78R → H in AI044966 (PubMed:8889548).Curated1

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

EnsembliENSRNOT00000008999; ENSRNOP00000008999; ENSRNOG00000006761.
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.
RefSeqiNP_446387.1. NM_053935.1.
UniGeneiRn.10787.

3D structure databases

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

Protein-protein interaction databases

BioGridi250599. 2 interactors.
IntActiO35179. 10 interactors.
MINTiMINT-1037287.
STRINGi10116.ENSRNOP00000008999.

PTM databases

iPTMnetiO35179.
PhosphoSitePlusiO35179.

Proteomic databases

PaxDbiO35179.
PRIDEiO35179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008999; ENSRNOP00000008999; ENSRNOG00000006761.
GeneIDi116743.
KEGGirno:116743.
UCSCiRGD:620276. rat.

Organism-specific databases

CTDi6456.
RGDi620276. Sh3gl2.

Phylogenomic databases

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiO35179.
KOiK11247.
OMAiGGLSHTS.
OrthoDBiEOG091G16FW.
PhylomeDBiO35179.

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.
R-RNO-182971. EGFR downregulation.
R-RNO-2132295. MHC class II antigen presentation.
R-RNO-432720. Lysosome Vesicle Biogenesis.
R-RNO-432722. Golgi Associated Vesicle Biogenesis.
R-RNO-437239. Recycling pathway of L1.
R-RNO-6807004. Negative regulation of MET activity.
R-RNO-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-RNO-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

EvolutionaryTraceiO35179.
PROiO35179.

Gene expression databases

BgeeiENSRNOG00000006761.
ExpressionAtlasiO35179. baseline and differential.
GenevisibleiO35179. RN.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00018. SH3_1. 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]
ProtoNetiSearch...

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 30, 2016
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.