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Protein

ADP-ribosylation factor 4

Gene

Arf4

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; may modulate vesicle budding and uncoating within the Golgi apparatus.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 318GTPBy similarity
Nucleotide bindingi67 – 715GTPBy similarity
Nucleotide bindingi126 – 1294GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • activation of phospholipase D activity Source: MGI
  • apical protein localization Source: MGI
  • brain development Source: Ensembl
  • cell migration Source: MGI
  • dendritic spine development Source: MGI
  • epidermal growth factor receptor signaling pathway Source: Ensembl
  • establishment or maintenance of epithelial cell apical/basal polarity Source: MGI
  • learning Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein ADP-ribosylation Source: MGI
  • protein localization to cilium Source: MGI
  • protein transport Source: UniProtKB-KW
  • regulation of reactive oxygen species metabolic process Source: MGI
  • response to axon injury Source: Ensembl
  • small GTPase mediated signal transduction Source: InterPro
  • vesicle-mediated transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_358790. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor 4
Gene namesi
Name:Arf4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:99433. Arf4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • dendritic spine Source: MGI
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • ruffle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 180179ADP-ribosylation factor 4PRO_0000207392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

MaxQBiP61750.
PaxDbiP61750.
PRIDEiP61750.

PTM databases

PhosphoSiteiP61750.

Expressioni

Gene expression databases

BgeeiP61750.
CleanExiMM_ARF4.
ExpressionAtlasiP61750. baseline and differential.
GenevisibleiP61750. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Cadps2Q8BYR52EBI-7569554,EBI-7569313

Protein-protein interaction databases

BioGridi198187. 3 interactions.
IntActiP61750. 3 interactions.
MINTiMINT-1866425.
STRINGi10090.ENSMUSP00000022429.

Structurei

3D structure databases

ProteinModelPortaliP61750.
SMRiP61750. Positions 4-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Arf family.Curated

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiP61750.
KOiK07939.
OMAiWASSEIF.
OrthoDBiEOG77WWDV.
PhylomeDBiP61750.
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.
SMARTiSM00177. ARF. 1 hit.
[Graphical view]
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.

P61750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLTISSLFS RLFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG
60 70 80 90 100
FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERI
110 120 130 140 150
QEGAAVLQKM LLEDELQDAV LLLFANKQDL PNAMAISEMT DKLGLQSLRN
160 170 180
RTWYVQATCA TQGTGLYEGL DWLSNELSKR
Length:180
Mass (Da):20,397
Last modified:January 23, 2007 - v2
Checksum:i09112917D8CE15D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081Q → E in BAB29041 (PubMed:16141072).Curated
Sequence conflicti176 – 1761E → R in BAB29041 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87901 mRNA. Translation: BAA13493.1.
AK013892 mRNA. Translation: BAB29041.1.
AK081686 mRNA. Translation: BAC38292.1.
AK153011 mRNA. Translation: BAE31650.1.
AK168793 mRNA. Translation: BAE40626.1.
CCDSiCCDS26881.1.
PIRiJC4948.
RefSeqiNP_031505.1. NM_007479.3.
UniGeneiMm.297768.

Genome annotation databases

EnsembliENSMUST00000022429; ENSMUSP00000022429; ENSMUSG00000021877.
GeneIDi11843.
KEGGimmu:11843.
UCSCiuc007sta.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87901 mRNA. Translation: BAA13493.1.
AK013892 mRNA. Translation: BAB29041.1.
AK081686 mRNA. Translation: BAC38292.1.
AK153011 mRNA. Translation: BAE31650.1.
AK168793 mRNA. Translation: BAE40626.1.
CCDSiCCDS26881.1.
PIRiJC4948.
RefSeqiNP_031505.1. NM_007479.3.
UniGeneiMm.297768.

3D structure databases

ProteinModelPortaliP61750.
SMRiP61750. Positions 4-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198187. 3 interactions.
IntActiP61750. 3 interactions.
MINTiMINT-1866425.
STRINGi10090.ENSMUSP00000022429.

PTM databases

PhosphoSiteiP61750.

Proteomic databases

MaxQBiP61750.
PaxDbiP61750.
PRIDEiP61750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022429; ENSMUSP00000022429; ENSMUSG00000021877.
GeneIDi11843.
KEGGimmu:11843.
UCSCiuc007sta.1. mouse.

Organism-specific databases

CTDi378.
MGIiMGI:99433. Arf4.

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiP61750.
KOiK07939.
OMAiWASSEIF.
OrthoDBiEOG77WWDV.
PhylomeDBiP61750.
TreeFamiTF300808.

Enzyme and pathway databases

ReactomeiREACT_358790. VxPx cargo-targeting to cilium.

Miscellaneous databases

NextBioi279795.
PROiP61750.
SOURCEiSearch...

Gene expression databases

BgeeiP61750.
CleanExiMM_ARF4.
ExpressionAtlasiP61750. baseline and differential.
GenevisibleiP61750. 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.
SMARTiSM00177. ARF. 1 hit.
[Graphical view]
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: C57BL/6J.
    Tissue: Bone marrow, Head and Heart.

Entry informationi

Entry nameiARF4_MOUSE
AccessioniPrimary (citable) accession number: P61750
Secondary accession number(s): P36403, Q3TGC2, Q9CXX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 103 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.