ARF5_MOUSE
ID ARF5_MOUSE Reviewed; 180 AA.
AC P84084; A2RTC5; P26437;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ADP-ribosylation factor 5;
GN Name=Arf5;
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 TISSUE=Lung;
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 [3]
RP FUNCTION, INTERACTION WITH GGA1; GGA2 AND GGA3, AND SUBCELLULAR LOCATION.
RX PubMed=11950392; DOI=10.1042/bj20020428;
RA Takatsu H., Yoshino K., Toda K., Nakayama K.;
RT "GGA proteins associate with Golgi membranes through interaction between
RT their GGAH domains and ADP-ribosylation factors.";
RL Biochem. J. 365:369-378(2002).
RN [4]
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 involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC {ECO:0000269|PubMed:11950392}.
CC -!- SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the
CC interaction is required for proper subcellular location of GGA1, GGA2
CC and GGA3 (PubMed:11950392). Binds ASAP2 (By similarity). Interacts with
CC NCS1/FREQ at the Golgi complex. Interacts with RAB11FIP3 and RAB11FIP4
CC (By similarity). {ECO:0000250|UniProtKB:P84085,
CC ECO:0000269|PubMed:11950392}.
CC -!- INTERACTION:
CC P84084; Q8BYR5: Cadps2; NbExp=5; IntAct=EBI-7569461, EBI-7569313;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P84085}. Membrane
CC {ECO:0000250|UniProtKB:P84085}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84085}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; D87902; BAA13494.1; -; mRNA.
DR EMBL; BC132452; AAI32453.1; -; mRNA.
DR EMBL; BC138756; AAI38757.1; -; mRNA.
DR CCDS; CCDS19952.1; -.
DR PIR; JC4949; JC4949.
DR RefSeq; NP_031506.1; NM_007480.1.
DR AlphaFoldDB; P84084; -.
DR SMR; P84084; -.
DR BioGRID; 198188; 14.
DR IntAct; P84084; 6.
DR MINT; P84084; -.
DR STRING; 10090.ENSMUSP00000020717; -.
DR iPTMnet; P84084; -.
DR PhosphoSitePlus; P84084; -.
DR SwissPalm; P84084; -.
DR EPD; P84084; -.
DR jPOST; P84084; -.
DR MaxQB; P84084; -.
DR PaxDb; P84084; -.
DR PeptideAtlas; P84084; -.
DR PRIDE; P84084; -.
DR ProteomicsDB; 273920; -.
DR TopDownProteomics; P84084; -.
DR Antibodypedia; 31827; 249 antibodies from 32 providers.
DR DNASU; 11844; -.
DR Ensembl; ENSMUST00000020717; ENSMUSP00000020717; ENSMUSG00000020440.
DR Ensembl; ENSMUST00000169841; ENSMUSP00000127281; ENSMUSG00000020440.
DR GeneID; 11844; -.
DR KEGG; mmu:11844; -.
DR UCSC; uc009bcq.1; mouse.
DR CTD; 381; -.
DR MGI; MGI:99434; Arf5.
DR VEuPathDB; HostDB:ENSMUSG00000020440; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000156878; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P84084; -.
DR OMA; TWHVEAT; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P84084; -.
DR TreeFam; TF300808; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 11844; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Arf5; mouse.
DR PRO; PR:P84084; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P84084; protein.
DR Bgee; ENSMUSG00000020440; Expressed in lip and 223 other tissues.
DR Genevisible; P84084; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; TAS:MGI.
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 Cytoplasm; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P84085"
FT CHAIN 2..180
FT /note="ADP-ribosylation factor 5"
FT /id="PRO_0000207397"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P84085"
SQ SEQUENCE 180 AA; 20530 MW; 25EF3D4895408147 CRC64;
MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV
LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA TQGTGLYDGL DWLSHELSKR
