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A2A5R2 (BIG2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brefeldin A-inhibited guanine nucleotide-exchange protein 2

Short name=Brefeldin A-inhibited GEP 2
Alternative name(s):
ADP-ribosylation factor guanine nucleotide-exchange factor 2
Gene names
Name:Arfgef2
Synonyms:Arfgep2, Big2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1792 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extend on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways By similarity.

Enzyme regulation

Inhibited by brefeldin A By similarity.

Subunit structure

Homodimer. Interacts with BIG1; both proteins are probably part of the same or very similar macromolecular complexes. Interacts with PRKAR1A, PRKAR2A, PRKAR1B, PRKAR2B, PPP1CC, PDE3A, TNFRSF1A, MYCBP and EXOC7. Interacts with GABRB1, GABRB2 and GABRB3 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane By similarity. Golgi apparatus By similarity. Cytoplasmperinuclear region By similarity. Golgi apparatustrans-Golgi network By similarity. Endosome By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cell projectiondendrite By similarity. Cytoplasmic vesicle By similarity. Cell junctionsynapse By similarity. Cytoplasmcytoskeleton By similarity. Note: Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes By similarity.

Post-translational modification

In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 By similarity.

Sequence similarities

Contains 1 SEC7 domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endosome
Golgi apparatus
Membrane
Synapse
   Molecular functionGuanine-nucleotide releasing factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

endomembrane system organization

Inferred from sequence or structural similarity. Source: UniProtKB

endosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

exocytosis

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

receptor recycling

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ARF protein signal transduction

Inferred from electronic annotation. Source: InterPro

regulation of GTPase activity

Inferred from Biological aspect of Ancestor. Source: GOC

vesicle-mediated transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentGolgi membrane

Inferred from sequence or structural similarity. Source: UniProtKB

asymmetric synapse

Inferred from sequence or structural similarity. Source: UniProtKB

axonemal microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule organizing center

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

symmetric synapse

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionARF guanyl-nucleotide exchange factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

GABA receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase A regulatory subunit binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17921792Brefeldin A-inhibited guanine nucleotide-exchange protein 2
PRO_0000419332

Regions

Domain661 – 792132SEC7
Region2 – 224223DCB; DCB:DCB domain and DCB:HUS domain interaction By similarity
Region515 – 53521HUS; DCB:HUS domain interaction By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2181Phosphoserine Ref.4
Modified residue2271Phosphoserine Ref.4
Modified residue6211Phosphoserine Ref.4
Modified residue6231Phosphothreonine Ref.4
Modified residue15321Phosphoserine By similarity
Modified residue15351Phosphoserine By similarity
Modified residue17891Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2A5R2 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 23DF06EA23A34A71

FASTA1,792202,240
        10         20         30         40         50         60 
MQESQTKSMF VSRALEKILA DKEVKRPQHS QLRRACQVAL DEIKAELEKQ RLGAAAPPKA 

        70         80         90        100        110        120 
NFIEADKYFL PFELACQSKS PRVVSTSLDC LQKLIAYGHI TGNAPDSGAP GKRLIDRIVE 

       130        140        150        160        170        180 
TICNCFQGPQ TDEGVQLQII KALLTAVTSP HIEIHEGTIL QTVRTCYNIY LASKNLINQT 

       190        200        210        220        230        240 
TAKATLTQML NVIFTRMENQ VLQEARELEK PMQSKPQSPV IQATAGSPKF SRLKQSQAQS 

       250        260        270        280        290        300 
KPTTPEKAEL PNGDHAQSGL GKVSLENGEA PRERGSPVSG RAEPSRGTDS GAQEVVKDIL 

       310        320        330        340        350        360 
EDVVTSAVKE AAEKHGLPEP DRALGALECQ ECAVPPGVDE NSQTNGIADD RQSLSSADNL 

       370        380        390        400        410        420 
EPDVQGHQVA ARFSHILQKD AFLVFRSLCK LSMKPLGEGP PDPKSHELRS KVVSLQLLLS 

       430        440        450        460        470        480 
VLQNAGPVFR SHEMFVTAIK QYLCVALSKN GVSSVPDVFE LSLAIFLTLL SNFKMHLKMQ 

       490        500        510        520        530        540 
IEVFFKEIFL NILETSTSSF EHRWMVIQTL TRICADAQCV VDIYVNYDCD LNAANIFERL 

       550        560        570        580        590        600 
VNDLSKIAQG RSGHELGMTP LQELSLRKKG LECLVSILKC MVEWSKDLYV NPNHQATLGQ 

       610        620        630        640        650        660 
ERLPDQEMGD GKGLDMARRC SVTSVESTVS SGTQTAIQDD PEQFEVIKQQ KEIIEHGIEL 

       670        680        690        700        710        720 
FNKKPKRGIQ FLQEQGMLGA AVEDIAQFLH QEERLDSTQV GEFLGDSTRF NKEVMYAYVD 

       730        740        750        760        770        780 
QLDFCEKEFV SALRTFLEGF RLPGEAQKID RLMEKFAARY IECNQGQTLF ASADTAYVLA 

       790        800        810        820        830        840 
YSIIMLTTDL HSPQVKNKMT KEQYIKMNRG INDSKDLPEE YLSSIYDEIE GKKIAMKETK 

       850        860        870        880        890        900 
EHTIATKSTK QSVASEKQRR LLYNVEMEQM AKTAKALMEA VSHAKAPFTS ATHLDHVRPM 

       910        920        930        940        950        960 
FKLVWTPLLA AYSIGLQNCD DTEVASLCLE GIRCAVRIAC IFGMQLERDA YVQALARFSL 

       970        980        990       1000       1010       1020 
LTASSSITEM KQKNIDTIKT LITVAHTDGN YLGNSWHEIL KCISQLELAQ LIGTGVKTRY 

      1030       1040       1050       1060       1070       1080 
LSGSGREREG SLKGHSLAGE EFMGLGLGNL VSGGVDKRQM ASFQESVGET SSQSVVVAVD 

      1090       1100       1110       1120       1130       1140 
RIFTGSTRLD GNAIVDFVRW LCAVSMDELA SPHHPRMFSL QKIVEISYYN MNRIRLQWSR 

      1150       1160       1170       1180       1190       1200 
IWHVIGDHFN KVGCNPNEDV AIFAVDSLRQ LSMKFLEKGE LANFRFQKDF LRPFEHIMKK 

      1210       1220       1230       1240       1250       1260 
NRSPTIRDMV IRCIAQMVSS QAANIRSGWK NIFAVFHQAA SDHDGNIVEL AFQTTGHIVS 

      1270       1280       1290       1300       1310       1320 
TIFQHHFPAA IDSFQDAVKC LSEFACNAAF PDTSMEAIRL IRFCGKYVSE RPRVLQEYTS 

      1330       1340       1350       1360       1370       1380 
DDMNVAPGDR VWVRGWFPIL FELSCIINRC KLDVRTRGLT VMFEIMKSYG HTFAKHWWQD 

      1390       1400       1410       1420       1430       1440 
LFRIVFRIFD NMKLPEQQSE KSEWMTTTCN HALYAICDVF TQFYEALHEV LLSDVFAQLQ 

      1450       1460       1470       1480       1490       1500 
WCVKQDNEQL ARSGTNCLEN LVISNGEKFS PAVWDETCNC MLDIFKTTIP HVLLTWRPAG 

      1510       1520       1530       1540       1550       1560 
MEEEVSDRHL DVDLDRQSLS SIDRNASERG QSQLSNPTDD SWKGAPYAHQ KLLASLLIKC 

      1570       1580       1590       1600       1610       1620 
VVQLELIQTI DNIVFYPATS KKEDAEHMVA AQQDTLDAEI HIETENQGMY KFMSSQHLFK 

      1630       1640       1650       1660       1670       1680 
LLDCLQESHS FSKAFNSNYE QRTVLWRAGF KGKSKPNLLK QETSSLACCL RILFRMYVDE 

      1690       1700       1710       1720       1730       1740 
NRRDSWDEIQ QRLLRVCSEA LAYFITVNSE SHREAWTSLL LLLLTKTLKI SDEKFKAHAS 

      1750       1760       1770       1780       1790 
MYYPYLCEIM QFDLIPELRA VLRKFFLRIG LVYKIWIPEE PSQVPAALSS TW 

« Hide

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-227; SER-621 AND THR-623, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591703, AL591911 Genomic DNA. Translation: CAM24646.1.
AL591911 Genomic DNA. Translation: CAM17723.1.
CH466551 Genomic DNA. Translation: EDL06489.1.
BC158012 mRNA. Translation: AAI58013.1.
CCDSCCDS38335.1.
RefSeqNP_001078964.1. NM_001085495.2.
UniGeneMm.297192.
Mm.488805.

3D structure databases

ProteinModelPortalA2A5R2.
SMRA2A5R2. Positions 644-835.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA2A5R2. 1 interaction.
STRING10090.ENSMUSP00000096677.

PTM databases

PhosphoSiteA2A5R2.

Proteomic databases

MaxQBA2A5R2.
PaxDbA2A5R2.
PRIDEA2A5R2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099078; ENSMUSP00000096677; ENSMUSG00000074582.
GeneID99371.
KEGGmmu:99371.
UCSCuc008nyr.2. mouse.

Organism-specific databases

CTD10564.
MGIMGI:2139354. Arfgef2.

Phylogenomic databases

eggNOGCOG5307.
GeneTreeENSGT00660000095162.
HOGENOMHOG000181045.
HOVERGENHBG004846.
InParanoidA2A5R2.
OMAEQGMLGA.
OrthoDBEOG7QVM1S.
PhylomeDBA2A5R2.
TreeFamTF300714.

Gene expression databases

ArrayExpressA2A5R2.
BgeeA2A5R2.
GenevestigatorA2A5R2.

Family and domain databases

Gene3D1.10.1000.11. 1 hit.
1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015403. DUF1981_Sec7_assoc.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamPF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view]
SMARTSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
SSF48425. SSF48425. 1 hit.
PROSITEPS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARFGEF2. mouse.
NextBio353893.
PROA2A5R2.
SOURCESearch...

Entry information

Entry nameBIG2_MOUSE
AccessionPrimary (citable) accession number: A2A5R2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 65 of the entry and version 1 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot