ARFRP_MOUSE
ID ARFRP_MOUSE Reviewed; 201 AA.
AC Q8BXL7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ADP-ribosylation factor-related protein 1;
DE Short=ARF-related protein 1;
GN Name=Arfrp1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=11839814; DOI=10.1128/mcb.22.5.1488-1494.2002;
RA Mueller A.G., Moser M., Kluge R., Leder S., Blum M., Buttner R.,
RA Joost H.-G., Schurmann A.;
RT "Embryonic lethality caused by apoptosis during gastrulation in mice
RT lacking the gene of the ADP-ribosylation factor-related protein 1.";
RL Mol. Cell. Biol. 22:1488-1494(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Retina;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17127620; DOI=10.1080/09687860600840100;
RA Zahn C., Hommel A., Lu L., Hong W., Walther D.J., Florian S., Joost H.G.,
RA Schurmann A.;
RT "Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to
RT the trans-Golgi in mouse embryos and HeLa cells.";
RL Mol. Membr. Biol. 23:475-485(2006).
RN [5]
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).
RN [6]
RP FUNCTION AND DISRUPTION PHENOTYPE.
RX PubMed=22927645; DOI=10.1128/mcb.00522-12;
RA Hesse D., Jaschke A., Kanzleiter T., Witte N., Augustin R., Hommel A.,
RA Puschel G.P., Petzke K.J., Joost H.G., Schupp M., Schurmann A.;
RT "GTPase ARFRP1 is essential for normal hepatic glycogen storage and
RT insulin-like growth factor 1 secretion.";
RL Mol. Cell. Biol. 32:4363-4374(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22505585; DOI=10.1093/hmg/dds140;
RA Jaschke A., Chung B., Hesse D., Kluge R., Zahn C., Moser M., Petzke K.J.,
RA Brigelius-Flohe R., Puchkov D., Koepsell H., Heeren J., Joost H.G.,
RA Schurmann A.;
RT "The GTPase ARFRP1 controls the lipidation of chylomicrons in the Golgi of
RT the intestinal epithelium.";
RL Hum. Mol. Genet. 21:3128-3142(2012).
RN [8]
RP FUNCTION AND DISRUPTION PHENOTYPE.
RX PubMed=23033902; DOI=10.1042/bsr20120082;
RA Hesse D., Jaschke A., Chung B., Schuermann A.;
RT "Trans-Golgi proteins participate in the control of lipid droplet and
RT chylomicron formation.";
RL Biosci. Rep. 33:1-9(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24186947; DOI=10.1194/jlr.m040089;
RA Hesse D., Radloff K., Jaschke A., Lagerpusch M., Chung B., Tailleux A.,
RA Staels B., Schurmann A.;
RT "Hepatic trans-Golgi action coordinated by the GTPase ARFRP1 is crucial for
RT lipoprotein lipidation and assembly.";
RL J. Lipid Res. 55:41-52(2014).
CC -!- FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting.
CC Controls the targeting of ARL1 and its effector to the trans-Golgi.
CC Required for the lipidation of chylomicrons in the intestine and
CC required for VLDL lipidation in the liver.
CC {ECO:0000269|PubMed:22505585, ECO:0000269|PubMed:23033902,
CC ECO:0000269|PubMed:24186947}.
CC -!- SUBUNIT: Interacts with SYS1. {ECO:0000250|UniProtKB:Q13795}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17127620}.
CC Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17127620}.
CC Note=Located in the trans-Golgi in the GTP-bound active state.
CC {ECO:0000269|PubMed:17127620}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to embryonic
CC lethality during early gastrulation. Intestine-specific knockout mice
CC display severe growth retardation due to reduced fat absorption and
CC decrease in lipid release from the intestinal epithelium to the lymph
CC and blood. Liver-specific knockout mice display impaired VLDL
CC lipidation leading to reduced plasma triglyceride levels in the fasted
CC state. Liver-specific knockout mice also display a disturbed glucose
CC metabolism caused by a reduced plasma membrane localization of the
CC glucose transporter GLUT2. {ECO:0000269|PubMed:22505585,
CC ECO:0000269|PubMed:22927645, ECO:0000269|PubMed:23033902,
CC ECO:0000269|PubMed:24186947}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AJ413952; CAC88691.1; -; Genomic_DNA.
DR EMBL; AJ413953; CAC88692.1; -; mRNA.
DR EMBL; AK005174; BAB23861.1; -; mRNA.
DR EMBL; AK044759; BAC32069.1; -; mRNA.
DR EMBL; BC010713; AAH10713.1; -; mRNA.
DR CCDS; CCDS17209.1; -.
DR RefSeq; NP_001159463.1; NM_001165991.1.
DR RefSeq; NP_001159464.1; NM_001165992.1.
DR RefSeq; NP_083978.3; NM_029702.4.
DR RefSeq; XP_011238267.1; XM_011239965.2.
DR AlphaFoldDB; Q8BXL7; -.
DR SMR; Q8BXL7; -.
DR BioGRID; 218262; 2.
DR STRING; 10090.ENSMUSP00000104436; -.
DR PhosphoSitePlus; Q8BXL7; -.
DR EPD; Q8BXL7; -.
DR jPOST; Q8BXL7; -.
DR MaxQB; Q8BXL7; -.
DR PaxDb; Q8BXL7; -.
DR PeptideAtlas; Q8BXL7; -.
DR PRIDE; Q8BXL7; -.
DR ProteomicsDB; 273922; -.
DR Antibodypedia; 29845; 124 antibodies from 24 providers.
DR DNASU; 76688; -.
DR Ensembl; ENSMUST00000108808; ENSMUSP00000104436; ENSMUSG00000038671.
DR Ensembl; ENSMUST00000127988; ENSMUSP00000122066; ENSMUSG00000038671.
DR GeneID; 76688; -.
DR KEGG; mmu:76688; -.
DR UCSC; uc008oly.2; mouse.
DR CTD; 10139; -.
DR MGI; MGI:1923938; Arfrp1.
DR VEuPathDB; HostDB:ENSMUSG00000038671; -.
DR eggNOG; KOG0076; Eukaryota.
DR GeneTree; ENSGT00940000156407; -.
DR HOGENOM; CLU_040729_7_2_1; -.
DR InParanoid; Q8BXL7; -.
DR OMA; QCHGIIF; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; Q8BXL7; -.
DR TreeFam; TF105788; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 76688; 27 hits in 74 CRISPR screens.
DR PRO; PR:Q8BXL7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BXL7; protein.
DR Bgee; ENSMUSG00000038671; Expressed in saccule of membranous labyrinth and 258 other tissues.
DR ExpressionAtlas; Q8BXL7; baseline and differential.
DR Genevisible; Q8BXL7; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR Pfam; PF00025; Arf; 1.
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 Acetylation; Golgi apparatus; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..201
FT /note="ADP-ribosylation factor-related protein 1"
FT /id="PRO_0000207488"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13795"
FT CONFLICT 41
FT /note="F -> L (in Ref. 2; BAC32069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22659 MW; 7BB6D213946F597E CRC64;
MYTLLSGLYK YMFQKDEYCI LILGLDNAGK TTFLEQSKTR FNKNYKGMSL SKITTTVGLN
IGTVDVGKAR LMFWDLGGQE ELQSLWDKYY AECHGVIYVI DSTDEERLSE SKEAFEKVVS
SEALDGVPIL VLANKQDVET CLSIPDIKTA FSDCTCKIGR RDCLTQACSA LTGKGVREGI
EWMVKCVVRN VHRPPRQRDI T
