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P84078 (ARF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
ADP-ribosylation factor 1
Gene names
Name:Arf1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with PRKCABP, PSCD2, ASAP2, HERC1 and PIP5K1B By similarity. Interacts with GGA1 and ARHGAP21. 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 TMED2 and TMED10 By similarity.

Subcellular location

Golgi apparatus. Cytoplasmperinuclear region By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 181180ADP-ribosylation factor 1
PRO_0000207380

Regions

Nucleotide binding24 – 318GTP
Nucleotide binding126 – 1294GTP

Amino acid modifications

Modified residue1471Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Experimental info

Sequence conflict1681E → K in BAE31170. Ref.2
Sequence conflict1741S → C in BAE28685. Ref.2
Sequence conflict1801Q → R in BAE40054. Ref.2

Secondary structure

.............................. 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84078 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AAC773D4A60186B6

FASTA18120,697
        10         20         30         40         50         60 
MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 

        70         80         90        100        110        120 
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV 

       130        140        150        160        170        180 
LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ 


K 

« Hide

References

« Hide 'large scale' references
[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: 8947846] [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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c, C57BL/6J, DBA/2 and NOD.
Tissue: Bone marrow, Heart, Kidney, Pancreas, Placenta and Sympathetic ganglion.
[3]"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: 19468303] [Abstract]
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: 15489334] [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, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"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: 12679809] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-182 IN COMPLEX WITH GTP AND GGA1.
[7]"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: 17347647] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-180 IN COMPLEX WITH ARHGAP21.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00221613.
PIRJC4945.
RefSeqNP_001123880.1. NM_001130408.1.
NP_031502.1. NM_007476.3.
UniGeneMm.371546.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O3YX-ray1.50A/B18-181[»]
2J59X-ray2.10A/B/C/D/E/F18-181[»]
ProteinModelPortalP84078.
SMRP84078. Positions 2-180.
ModBaseSearch...

Protein-protein interaction databases

IntActP84078. 1 interaction.
MINTMINT-1862213.
STRINGP84078.

PTM databases

PhosphoSiteP84078.

Proteomic databases

PRIDEP84078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061242; ENSMUSP00000079905; ENSMUSG00000048076.
ENSMUST00000163300; ENSMUSP00000126120; ENSMUSG00000048076.
GeneID11840.
KEGGmmu:11840.
UCSCuc007jdm.2. mouse.

Organism-specific databases

CTD375.
MGIMGI:99431. Arf1.

Phylogenomic databases

eggNOGroNOG06163.
GeneTreeENSGT00570000078761.
HOVERGENHBG002073.
InParanoidP84078.
OMANDRDRMR.
OrthoDBEOG4PZJ7Q.
PhylomeDBP84078.

Gene expression databases

ArrayExpressP84078.
BgeeP84078.
CleanExMM_ARF1.
GenevestigatorP84078.
GermOnlineENSMUSG00000048076. Mus musculus.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
KOK07937.
PANTHERPTHR11711. ARF/SAR. 1 hit.
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. Small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279783.
SOURCESearch...

Entry information

Entry nameARF1_MOUSE
AccessionPrimary (citable) accession number: P84078
Secondary accession number(s): P10947 expand/collapse secondary AC list , P32889, Q3THZ2, Q3U849, Q3UDG1, Q3UF76
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families