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   27-MAR-2024, entry version 158.
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,
RC   Pancreas, 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. Part of the ciliary targeting
CC       complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4,
CC       which direct preciliary vesicle trafficking to mother centriole and
CC       ciliogenesis initiation (By similarity).
CC       {ECO:0000250|UniProtKB:P18085}.
CC   -!- SUBUNIT: Forms a complex containing RAB11A, ASAP1, RAB3IP, RAP11FIP3
CC       and ARF4; the complex promotes preciliary trafficking; the complex
CC       binds to RHO in photoreceptor cells and promotes RHO ciliary transport.
CC       {ECO:0000250|UniProtKB:P18085}.
CC   -!- INTERACTION:
CC       P61750; Q8BYR5: Cadps2; NbExp=2; IntAct=EBI-7569554, EBI-7569313;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P18085}.
CC       Membrane {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; 13.
DR   IntAct; P61750; 4.
DR   MINT; P61750; -.
DR   STRING; 10090.ENSMUSP00000022429; -.
DR   GlyGen; P61750; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61750; -.
DR   PhosphoSitePlus; P61750; -.
DR   SwissPalm; P61750; -.
DR   EPD; P61750; -.
DR   jPOST; P61750; -.
DR   PaxDb; 10090-ENSMUSP00000022429; -.
DR   PeptideAtlas; P61750; -.
DR   ProteomicsDB; 277273; -.
DR   Pumba; P61750; -.
DR   Antibodypedia; 46310; 269 antibodies from 33 providers.
DR   DNASU; 11843; -.
DR   Ensembl; ENSMUST00000022429.9; ENSMUSP00000022429.3; ENSMUSG00000021877.13.
DR   GeneID; 11843; -.
DR   KEGG; mmu:11843; -.
DR   UCSC; uc007sta.1; mouse.
DR   AGR; MGI:99433; -.
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; GRKWYIQ; -.
DR   OrthoDB; 5474610at2759; -.
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; 11 hits in 78 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 273 other cell types or tissues.
DR   ExpressionAtlas; P61750; baseline and differential.
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:0000139; C:Golgi membrane; ISS:UniProtKB.
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:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; ISO:MGI.
DR   GO; GO:1990583; F:phospholipase D activator activity; IEA:Ensembl.
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:0061512; P:protein localization to cilium; IMP:MGI.
DR   GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045872; Arf1-5-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR   PANTHER; PTHR11711:SF110; ADP-RIBOSYLATION FACTOR 4; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51417; ARF; 1.
DR   Genevisible; P61750; MM.
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
//