ARF4_MOUSE
ID ARF4_MOUSE Reviewed; 180 AA.
AC P61750; P36403; Q3TGC2; Q9CXX3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ADP-ribosylation factor 4;
GN Name=Arf4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=8947846; DOI=10.1093/oxfordjournals.jbchem.a021484;
RA Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT "Structure and intracellular localization of mouse ADP-ribosylation factors
RT type 1 to type 6 (ARF1-ARF6).";
RL J. Biochem. 120:813-819(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: GTP-binding protein that functions as an allosteric activator
CC of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
CC Involved in protein trafficking; may modulate vesicle budding and
CC uncoating within the Golgi apparatus.
CC -!- INTERACTION:
CC P61750; Q8BYR5: Cadps2; NbExp=2; IntAct=EBI-7569554, EBI-7569313;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Membrane
CC {ECO:0000250|UniProtKB:P18085}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P18085}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; D87901; BAA13493.1; -; mRNA.
DR EMBL; AK013892; BAB29041.1; -; mRNA.
DR EMBL; AK081686; BAC38292.1; -; mRNA.
DR EMBL; AK153011; BAE31650.1; -; mRNA.
DR EMBL; AK168793; BAE40626.1; -; mRNA.
DR CCDS; CCDS26881.1; -.
DR PIR; JC4948; JC4948.
DR RefSeq; NP_031505.1; NM_007479.3.
DR AlphaFoldDB; P61750; -.
DR SMR; P61750; -.
DR BioGRID; 198187; 11.
DR IntAct; P61750; 4.
DR MINT; P61750; -.
DR STRING; 10090.ENSMUSP00000022429; -.
DR iPTMnet; P61750; -.
DR PhosphoSitePlus; P61750; -.
DR SwissPalm; P61750; -.
DR EPD; P61750; -.
DR jPOST; P61750; -.
DR PaxDb; P61750; -.
DR PeptideAtlas; P61750; -.
DR PRIDE; P61750; -.
DR ProteomicsDB; 277273; -.
DR Antibodypedia; 46310; 240 antibodies from 32 providers.
DR DNASU; 11843; -.
DR Ensembl; ENSMUST00000022429; ENSMUSP00000022429; ENSMUSG00000021877.
DR GeneID; 11843; -.
DR KEGG; mmu:11843; -.
DR UCSC; uc007sta.1; mouse.
DR CTD; 378; -.
DR MGI; MGI:99433; Arf4.
DR VEuPathDB; HostDB:ENSMUSG00000021877; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000156297; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P61750; -.
DR OMA; CATQGEG; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P61750; -.
DR TreeFam; TF300808; -.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 11843; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Arf4; mouse.
DR PRO; PR:P61750; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P61750; protein.
DR Bgee; ENSMUSG00000021877; Expressed in undifferentiated genital tubercle and 270 other tissues.
DR ExpressionAtlas; P61750; baseline and differential.
DR Genevisible; P61750; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0031584; P:activation of phospholipase D activity; ISO:MGI.
DR GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0060996; P:dendritic spine development; IMP:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04150; Arf1_5_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P18085"
FT CHAIN 2..180
FT /note="ADP-ribosylation factor 4"
FT /id="PRO_0000207392"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18085"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P18085"
FT CONFLICT 108
FT /note="Q -> E (in Ref. 2; BAB29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> R (in Ref. 2; BAB29041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20397 MW; 09112917D8CE15D6 CRC64;
MGLTISSLFS RLFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERI QEGAAVLQKM LLEDELQDAV
LLLFANKQDL PNAMAISEMT DKLGLQSLRN RTWYVQATCA TQGTGLYEGL DWLSNELSKR
