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Protein

ADP-ribosylation factor 1

Gene

Arf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei160 – 1601GTP; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 329GTPCombined sources1 Publication
Nucleotide bindingi126 – 1294GTPCombined sources1 Publication

GO - Molecular functioni

  • GDP binding Source: Ensembl
  • GTP binding Source: MGI
  • magnesium ion binding Source: Ensembl
  • phospholipase D activator activity Source: Ensembl
  • poly(A) RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1660514. Synthesis of PIPs at the Golgi membrane.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-421837. Clathrin derived vesicle budding.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.
R-MMU-6811438. Intra-Golgi traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor 1
Gene namesi
Name:Arf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:99431. Arf1.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: MGI
  • COPI-coated vesicle Source: Ensembl
  • cytosol Source: MGI
  • endomembrane system Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • Golgi apparatus Source: MGI
  • Golgi membrane Source: Ensembl
  • late endosome Source: Ensembl
  • neuron projection Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • peroxisomal membrane Source: Ensembl
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-KW
  • sarcomere Source: MGI
  • trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 181180ADP-ribosylation factor 1PRO_0000207380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine; alternateBy similarity
Lipidationi2 – 21N-myristoyl glycine; alternateBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Myristate

Proteomic databases

EPDiP84078.
MaxQBiP84078.
PaxDbiP84078.
PRIDEiP84078.
TopDownProteomicsiP84078.

PTM databases

iPTMnetiP84078.
PhosphoSiteiP84078.
SwissPalmiP84078.

Expressioni

Gene expression databases

BgeeiP84078.
CleanExiMM_ARF1.
GenevisibleiP84078. MM.

Interactioni

Subunit structurei

Interacts with ARHGAP21, ASAP2, GGA1, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2. Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function. Interacts with PI4KB in the Golgi complex. Interacts with NCS1/FREQ in the Golgi and at the plasma membrane. Interacts with PLEKHA3. Interacts with PLEKHA8; the interaction, together with phosphatidylinositol 4-phosphate binding, is required for FAPP2-mediated glucosylceramide transfer activity. Interacts (activated) with PICK1 (via PDZ domain); the interaction blocks Arp2/3 complex inhibition. Interacts with IQSEC1 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGAP21Q5T5U33EBI-2308190,EBI-1642518From a different organism.

Protein-protein interaction databases

BioGridi198184. 2 interactions.
IntActiP84078. 4 interactions.
MINTiMINT-1862213.
STRINGi10090.ENSMUSP00000079905.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 236Combined sources
Helixi30 – 3910Combined sources
Beta strandi49 – 5810Combined sources
Beta strandi61 – 688Combined sources
Helixi72 – 8110Combined sources
Beta strandi87 – 937Combined sources
Helixi97 – 993Combined sources
Helixi100 – 11112Combined sources
Helixi114 – 1163Combined sources
Beta strandi120 – 1267Combined sources
Helixi136 – 1438Combined sources
Helixi145 – 1473Combined sources
Beta strandi153 – 1575Combined sources
Turni160 – 1634Combined sources
Helixi166 – 17712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O3YX-ray1.50A/B18-181[»]
2J59X-ray2.10A/B/C/D/E/F18-181[»]
ProteinModelPortaliP84078.
SMRiP84078. Positions 2-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84078.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Arf family.Curated

Phylogenomic databases

eggNOGiKOG0070. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121855.
HOVERGENiHBG002073.
InParanoidiP84078.
KOiK07937.
OMAiNDNERVS.
OrthoDBiEOG77WWDV.
PhylomeDBiP84078.
TreeFamiTF300808.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P84078-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG
60 70 80 90 100
FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV
110 120 130 140 150
NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH
160 170 180
RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K
Length:181
Mass (Da):20,697
Last modified:January 23, 2007 - v2
Checksum:iAAC773D4A60186B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681E → K in BAE31170 (PubMed:16141072).Curated
Sequence conflicti174 – 1741S → C in BAE28685 (PubMed:16141072).Curated
Sequence conflicti180 – 1801Q → R in BAE40054 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87898 mRNA. Translation: BAA13490.1.
AK148458 mRNA. Translation: BAE28566.1.
AK148873 mRNA. Translation: BAE28685.1.
AK150092 mRNA. Translation: BAE29300.1.
AK150699 mRNA. Translation: BAE29778.1.
AK151223 mRNA. Translation: BAE30215.1.
AK151225 mRNA. Translation: BAE30217.1.
AK151696 mRNA. Translation: BAE30620.1.
AK151821 mRNA. Translation: BAE30718.1.
AK152015 mRNA. Translation: BAE30877.1.
AK152382 mRNA. Translation: BAE31170.1.
AK152479 mRNA. Translation: BAE31253.1.
AK153132 mRNA. Translation: BAE31745.1.
AK159174 mRNA. Translation: BAE34874.1.
AK167000 mRNA. Translation: BAE39179.1.
AK167129 mRNA. Translation: BAE39276.1.
AK167543 mRNA. Translation: BAE39610.1.
AK167931 mRNA. Translation: BAE39935.1.
AK168081 mRNA. Translation: BAE40054.1.
AK168686 mRNA. Translation: BAE40532.1.
AK169166 mRNA. Translation: BAE40945.1.
AK170586 mRNA. Translation: BAE41895.1.
AL645854 Genomic DNA. Translation: CAM17105.1.
BC031986 mRNA. Translation: AAH31986.1.
CCDSiCCDS24765.1.
PIRiJC4945.
RefSeqiNP_001123880.1. NM_001130408.1.
NP_031502.1. NM_007476.3.
XP_011246983.1. XM_011248681.1.
UniGeneiMm.371546.

Genome annotation databases

EnsembliENSMUST00000061242; ENSMUSP00000079905; ENSMUSG00000048076.
ENSMUST00000163300; ENSMUSP00000126120; ENSMUSG00000048076.
GeneIDi11840.
KEGGimmu:11840.
UCSCiuc007jdm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87898 mRNA. Translation: BAA13490.1.
AK148458 mRNA. Translation: BAE28566.1.
AK148873 mRNA. Translation: BAE28685.1.
AK150092 mRNA. Translation: BAE29300.1.
AK150699 mRNA. Translation: BAE29778.1.
AK151223 mRNA. Translation: BAE30215.1.
AK151225 mRNA. Translation: BAE30217.1.
AK151696 mRNA. Translation: BAE30620.1.
AK151821 mRNA. Translation: BAE30718.1.
AK152015 mRNA. Translation: BAE30877.1.
AK152382 mRNA. Translation: BAE31170.1.
AK152479 mRNA. Translation: BAE31253.1.
AK153132 mRNA. Translation: BAE31745.1.
AK159174 mRNA. Translation: BAE34874.1.
AK167000 mRNA. Translation: BAE39179.1.
AK167129 mRNA. Translation: BAE39276.1.
AK167543 mRNA. Translation: BAE39610.1.
AK167931 mRNA. Translation: BAE39935.1.
AK168081 mRNA. Translation: BAE40054.1.
AK168686 mRNA. Translation: BAE40532.1.
AK169166 mRNA. Translation: BAE40945.1.
AK170586 mRNA. Translation: BAE41895.1.
AL645854 Genomic DNA. Translation: CAM17105.1.
BC031986 mRNA. Translation: AAH31986.1.
CCDSiCCDS24765.1.
PIRiJC4945.
RefSeqiNP_001123880.1. NM_001130408.1.
NP_031502.1. NM_007476.3.
XP_011246983.1. XM_011248681.1.
UniGeneiMm.371546.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O3YX-ray1.50A/B18-181[»]
2J59X-ray2.10A/B/C/D/E/F18-181[»]
ProteinModelPortaliP84078.
SMRiP84078. Positions 2-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198184. 2 interactions.
IntActiP84078. 4 interactions.
MINTiMINT-1862213.
STRINGi10090.ENSMUSP00000079905.

Chemistry

ChEMBLiCHEMBL1075273.

PTM databases

iPTMnetiP84078.
PhosphoSiteiP84078.
SwissPalmiP84078.

Proteomic databases

EPDiP84078.
MaxQBiP84078.
PaxDbiP84078.
PRIDEiP84078.
TopDownProteomicsiP84078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061242; ENSMUSP00000079905; ENSMUSG00000048076.
ENSMUST00000163300; ENSMUSP00000126120; ENSMUSG00000048076.
GeneIDi11840.
KEGGimmu:11840.
UCSCiuc007jdm.2. mouse.

Organism-specific databases

CTDi375.
MGIiMGI:99431. Arf1.

Phylogenomic databases

eggNOGiKOG0070. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121855.
HOVERGENiHBG002073.
InParanoidiP84078.
KOiK07937.
OMAiNDNERVS.
OrthoDBiEOG77WWDV.
PhylomeDBiP84078.
TreeFamiTF300808.

Enzyme and pathway databases

ReactomeiR-MMU-1660514. Synthesis of PIPs at the Golgi membrane.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-421837. Clathrin derived vesicle budding.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.
R-MMU-6811438. Intra-Golgi traffic.

Miscellaneous databases

EvolutionaryTraceiP84078.
PROiP84078.
SOURCEiSearch...

Gene expression databases

BgeeiP84078.
CleanExiMM_ARF1.
GenevisibleiP84078. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6)."
    Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.
    J. Biochem. 120:813-819(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ, C57BL/6J, DBA/2J and NOD.
    Tissue: Bone marrow, Heart, Kidney, Pancreas, Placenta and Sympathetic ganglion.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
  5. Lubec G., Kang S.U., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-30; 39-73; 80-97 AND 110-127, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.
  7. "Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport."
    Shiba T., Kawasaki M., Takatsu H., Nogi T., Matsugaki N., Igarashi N., Suzuki M., Kato R., Nakayama K., Wakatsuki S.
    Nat. Struct. Biol. 10:386-393(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-182 IN COMPLEX WITH GTP AND GGA1.
  8. "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes."
    Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N., El Khadali F., Franco M., Chavrier P., Houdusse A.
    EMBO J. 26:1953-1962(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-180 IN COMPLEX WITH ARHGAP21.

Entry informationi

Entry nameiARF1_MOUSE
AccessioniPrimary (citable) accession number: P84078
Secondary accession number(s): P10947
, P32889, Q3THZ2, Q3U849, Q3UDG1, Q3UF76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.