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Protein

Brefeldin A-inhibited guanine nucleotide-exchange protein 2

Gene

Arfgef2

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

Functioni

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.1 Publication

Enzyme regulationi

Inhibited by brefeldin A.By similarity

GO - Molecular functioni

  • ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
  • GABA receptor binding Source: RGD
  • guanyl-nucleotide exchange factor activity Source: RGD
  • myosin binding Source: UniProtKB
  • protein kinase A regulatory subunit binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Arfgef2
Synonyms:Arfgep2, Big2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi631430. Arfgef2.

Subcellular locationi

GO - Cellular componenti

  • asymmetric synapse Source: UniProtKB
  • axonemal microtubule Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: RGD
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: Ensembl
  • dendritic spine Source: UniProtKB
  • Golgi membrane Source: UniProtKB
  • microtubule organizing center Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • recycling endosome Source: UniProtKB
  • symmetric synapse Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Golgi apparatus, Membrane, Synapse

Pathology & Biotechi

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17911791Brefeldin A-inhibited guanine nucleotide-exchange protein 2PRO_0000419333Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei623 – 6231PhosphothreonineBy similarity
Modified residuei624 – 6241PhosphoserineBy similarity
Modified residuei633 – 6331PhosphothreonineBy similarity
Modified residuei707 – 7071PhosphoserineBy similarity
Modified residuei1518 – 15181PhosphoserineCombined sources
Modified residuei1520 – 15201PhosphoserineCombined sources
Modified residuei1521 – 15211PhosphoserineCombined sources
Modified residuei1532 – 15321PhosphoserineCombined sources
Modified residuei1535 – 15351PhosphoserineCombined sources
Modified residuei1541 – 15411PhosphoserineCombined sources
Modified residuei1788 – 17881PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ7TSU1.
PRIDEiQ7TSU1.

PTM databases

iPTMnetiQ7TSU1.
PhosphoSiteiQ7TSU1.

Expressioni

Tissue specificityi

Expressed in brain (at protein level).

Gene expression databases

GenevisibleiQ7TSU1. RN.

Interactioni

Subunit structurei

Homodimer. Interacts with ARFGEF1/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 (By similarity). Interacts with GABRB1, GABRB2 and GABRB3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Gabrb3P630793EBI-6257913,EBI-6257937

GO - Molecular functioni

  • GABA receptor binding Source: RGD
  • myosin binding Source: UniProtKB
  • protein kinase A regulatory subunit binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ7TSU1. 6 interactions.
STRINGi10116.ENSRNOP00000010054.

Structurei

3D structure databases

ProteinModelPortaliQ7TSU1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini661 – 792132SEC7PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 224223DCB; DCB:DCB domain and DCB:HUS domain interactionBy similarityAdd
BLAST
Regioni515 – 53521HUS; DCB:HUS domain interactionBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 SEC7 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0929. Eukaryota.
COG5307. LUCA.
GeneTreeiENSGT00760000119036.
HOGENOMiHOG000181045.
HOVERGENiHBG004846.
InParanoidiQ7TSU1.
KOiK18442.
OMAiPEVWDET.
OrthoDBiEOG7QVM1S.
PhylomeDBiQ7TSU1.
TreeFamiTF300714.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032629. DCB_dom.
IPR023394. Sec7_alpha_orthog.
IPR015403. Sec7_C.
IPR000904. Sec7_dom.
IPR032691. Sec7_N.
[Graphical view]
PfamiPF16213. DCB. 1 hit.
PF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
PF12783. Sec7_N. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TSU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQESQTKSMF VSRALEKILA DKEVKRPQHS QLRRACQVAL DEIKAELEKQ
60 70 80 90 100
RLGAAAPPKA NFIEADKYFL PFELACQSKS PRVVSTSLDC LQKLIAYGHI
110 120 130 140 150
TGNAPDSGAP GKRLIDRIVE TVCNCFQGPQ TDEGVQLQII KALLTAVTSP
160 170 180 190 200
HIEIHEGTIL QTVRTCYNIY LASKNLINQT TAKATLTQML NVIFTRMENQ
210 220 230 240 250
VLQEARELEK PIQSKPQSPV IQATAGSPKF SRLKQSQAQS KPTTPEKTEL
260 270 280 290 300
PNGDHARSSL GKVNSENGEA HRERGSSISG RAEPSGGSDN GAQEVVKDIL
310 320 330 340 350
EDVVTSAVKE AAEKQGLPEP DQAPGVPECQ ECTVPPAVDE NSQTNGIADD
360 370 380 390 400
RQSLSSADNL EPDAQGHPVA ARFSHILQKD AFLVFRSLCK LSMKPLGEGP
410 420 430 440 450
PDPKSHELRS KVVSLQLLLS VLQNAGPVFR SHEMFVTAIK QYLCVALSKN
460 470 480 490 500
GVSSVPDVFE LSLAIFLTLL SNFKMHLKMQ IEVFFKEIFL NILETSTSSF
510 520 530 540 550
EHRWMVIQTL TRICADAQCV VDIYVNYDCD LNAANIFERL VNDLSKIAQG
560 570 580 590 600
RSGHELGMTP LQELSLRKKG LECLVSILKC MVEWSKDLYV NPNHQATLGQ
610 620 630 640 650
ERLPDQEMGD GKGLDMARRC SVTSVESTVS SGTQTAIPDD PEQFEVIKQQ
660 670 680 690 700
KEIIEHGIEL FNKKPKRGIQ FLQEQGMLGA AVEDIAQFLH QEERLDSTQV
710 720 730 740 750
GEFLGDSTRF NKEVMYAYVD QLDFCEKEFV SALRTFLEGF RLPGEAQKID
760 770 780 790 800
RLMEKFAARY IECNQGQTLF ASADTAYVLA YSIIMLTTDL HSPQVKNKMT
810 820 830 840 850
KEQYIKMNRG INDSKDLPEE YLSSIYEEIE GKKIAMKETK EHTMATKSTK
860 870 880 890 900
QNVASEKQRR LLYNVEMEQM AKTAKALMEA VSHAKAPFTS ATHLDHVRPM
910 920 930 940 950
FKLVWTPLLA AYSIGLQNCD DTEVASLCLE GIRCAVRIAC IFGMQLERDA
960 970 980 990 1000
YVQALARFSL LTASSSITEM KQKNIDTIKT LITVAHTDGN YLGNSWHEIL
1010 1020 1030 1040 1050
KCISQLELAQ LIGTGVKTRY LSGSGREREG SLKGHSLAGE EFMGLGLGNL
1060 1070 1080 1090 1100
VSGGVDKRQM ASFQESVGET SSQSVVVAVD RIFTGSTRLD GNAIVDFVRW
1110 1120 1130 1140 1150
LCAVSMDELA SPHHPRMFSL QKIVEISYYN MNRIRLQWSR IWHVIGDHFN
1160 1170 1180 1190 1200
KVGCNPNEDV AIFAVDSLRQ LSMKFLEKGE LANFRFQKDF LRPFEHIMKK
1210 1220 1230 1240 1250
NRSPTIRDMV IRCIAQMVSS QAANIRSGWK NIFAVFHQAA SDHDGNIVEL
1260 1270 1280 1290 1300
AFQTTGHIVS TIFQHHFPAA IDSFQDAVKC LSEFACNAAF PDTSMEAIRL
1310 1320 1330 1340 1350
IRFCGKYVSE RPRVLQEYTS DDMNVAPGDR VWVRGWFPIL FELSCIINRC
1360 1370 1380 1390 1400
KLDVRTRGLT VMFEIMKSYG HTFAKHWWQD LFRIVFRIFD NMKLPEQQSE
1410 1420 1430 1440 1450
KSEWMTTTCN HALYAICDVF TQFYEALHEV LLSDVFAQLQ WCVKQDNEQL
1460 1470 1480 1490 1500
ARSGTNCLEN LVISNGEKFS PAVWDETCNC MLDIFRTTIP HVLLTWRPAG
1510 1520 1530 1540 1550
MEEEVSDRHL DVDLDRQSLS SIDRNASERG QSQLSNPTDD SWKGAPYANQ
1560 1570 1580 1590 1600
KLLASLLIKC VVQLELIQTI DNIVFYPATS KKEDAEHMVA AQQDTLDADI
1610 1620 1630 1640 1650
HIETENQGMY KFMSSQHLFK LLDCLQESHS FSKAFNSNYE QRTVLWRAGF
1660 1670 1680 1690 1700
KGKSKPNLLK QETSSLACCL RILFRMYVDE NRRDSWGEIQ QRLLTVCSEA
1710 1720 1730 1740 1750
LAYFITVNSE SHREAWTSLL LLLLTKTLKI NDEKFKAHAS VYYPYLCEMM
1760 1770 1780 1790
QFDLIPELRA VLRKFFLRIG LVYKIWVPEE PSQVPAASTA W
Length:1,791
Mass (Da):201,974
Last modified:October 1, 2003 - v1
Checksum:i397CB889C2ABF569
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY255526 mRNA. Translation: AAP04588.2.
AABR06027654 Genomic DNA. No translation available.
AABR06027655 Genomic DNA. No translation available.
AABR06027656 Genomic DNA. No translation available.
RefSeqiNP_851597.2. NM_181083.2.
UniGeneiRn.161866.

Genome annotation databases

EnsembliENSRNOT00000010054; ENSRNOP00000010054; ENSRNOG00000007485.
GeneIDi296380.
KEGGirno:296380.
UCSCiRGD:631430. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY255526 mRNA. Translation: AAP04588.2.
AABR06027654 Genomic DNA. No translation available.
AABR06027655 Genomic DNA. No translation available.
AABR06027656 Genomic DNA. No translation available.
RefSeqiNP_851597.2. NM_181083.2.
UniGeneiRn.161866.

3D structure databases

ProteinModelPortaliQ7TSU1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7TSU1. 6 interactions.
STRINGi10116.ENSRNOP00000010054.

PTM databases

iPTMnetiQ7TSU1.
PhosphoSiteiQ7TSU1.

Proteomic databases

PaxDbiQ7TSU1.
PRIDEiQ7TSU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010054; ENSRNOP00000010054; ENSRNOG00000007485.
GeneIDi296380.
KEGGirno:296380.
UCSCiRGD:631430. rat.

Organism-specific databases

CTDi10564.
RGDi631430. Arfgef2.

Phylogenomic databases

eggNOGiKOG0929. Eukaryota.
COG5307. LUCA.
GeneTreeiENSGT00760000119036.
HOGENOMiHOG000181045.
HOVERGENiHBG004846.
InParanoidiQ7TSU1.
KOiK18442.
OMAiPEVWDET.
OrthoDBiEOG7QVM1S.
PhylomeDBiQ7TSU1.
TreeFamiTF300714.

Miscellaneous databases

PROiQ7TSU1.

Gene expression databases

GenevisibleiQ7TSU1. RN.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032629. DCB_dom.
IPR023394. Sec7_alpha_orthog.
IPR015403. Sec7_C.
IPR000904. Sec7_dom.
IPR032691. Sec7_N.
[Graphical view]
PfamiPF16213. DCB. 1 hit.
PF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
PF12783. Sec7_N. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The brefeldin A-inhibited GDP/GTP exchange factor 2, a protein involved in vesicular trafficking, interacts with the beta subunits of the GABA receptors."
    Charych E.I., Yu W., Miralles C.P., Serwanski D.R., Li X., Rubio M., De Blas A.L.
    J. Neurochem. 90:173-189(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GABRB1; GABRB2 AND GABRB3.
    Strain: Sprague-Dawley.
  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].
    Strain: Brown Norway.
  3. "Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic."
    Zhao X., Lasell T.K., Melancon P.
    Mol. Biol. Cell 13:119-133(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-227; SER-355; SER-356; SER-1518; SER-1520; SER-1521; SER-1532; SER-1535 AND SER-1541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBIG2_RAT
AccessioniPrimary (citable) accession number: Q7TSU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: October 1, 2003
Last modified: June 8, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.