ARF1_RAT
ID ARF1_RAT Reviewed; 181 AA.
AC P84079; P10947; P32889;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ADP-ribosylation factor 1;
GN Name=Arf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8813705; DOI=10.1007/bf00226058;
RA Price S.R., Nightingale M.S., Tsuchiya M., Moss J., Vaughan M.;
RT "Interspecies relationships among ADP-ribosylation factors (ARFs): evidence
RT of evolutionary pressure to maintain individual identities.";
RL Mol. Cell. Biochem. 159:15-23(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 INTERACTION WITH ARFGAP1.
RX PubMed=7890632; DOI=10.1074/jbc.270.10.5232;
RA Makler V., Cukierman E., Rotman M., Admon A., Cassel D.;
RT "ADP-ribosylation factor-directed GTPase-activating protein. Purification
RT and partial characterization.";
RL J. Biol. Chem. 270:5232-5237(1995).
RN [4]
RP INTERACTION WITH PRKCABP.
RX PubMed=10623590; DOI=10.1006/bbrc.1999.1932;
RA Takeya R., Takeshige K., Sumimoto H.;
RT "Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation
RT factors.";
RL Biochem. Biophys. Res. Commun. 267:149-155(2000).
RN [5]
RP INTERACTION WITH ASAP2.
RX PubMed=10022920; DOI=10.1128/mcb.19.3.2338;
RA Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G., Randazzo P.A.,
RA Schlessinger J.;
RT "Identification of a new Pyk2 target protein with Arf-GAP activity.";
RL Mol. Cell. Biol. 19:2338-2350(1999).
RN [6]
RP INTERACTION WITH PIP5K1B.
RX PubMed=10747863; DOI=10.1074/jbc.c901019199;
RA Jones D.H., Morris J.B., Morgan C.P., Kondo H., Irvine R.F., Cockcroft S.;
RT "Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with
RT ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-
RT bisphosphate synthesis in the Golgi compartment.";
RL J. Biol. Chem. 275:13962-13966(2000).
RN [7]
RP FUNCTION, INTERACTION WITH PICK1 AND GRIA2, AND SUBCELLULAR LOCATION.
RX PubMed=23889934; DOI=10.1016/j.neuron.2013.05.003;
RA Rocca D.L., Amici M., Antoniou A., Suarez E.B., Halemani N., Murk K.,
RA McGarvey J., Jaafari N., Mellor J.R., Collingridge G.L., Hanley J.G.;
RT "The small GTPase Arf1 modulates Arp2/3-mediated actin polymerization via
RT PICK1 to regulate synaptic plasticity.";
RL Neuron 79:293-307(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=7552752; DOI=10.1038/nsb0995-797;
RA Greasley S.E., Jhoti H., Teahan C., Solari R., Fensome A., Thomas G.M.,
RA Cockcroft S., Bax B.;
RT "The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP
RT determined from two different crystal forms.";
RL Nat. Struct. Biol. 2:797-806(1995).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking among
CC different compartments. Modulates vesicle budding and uncoating within
CC the Golgi complex. Deactivation induces the redistribution of the
CC entire Golgi complex to the endoplasmic reticulum, suggesting a crucial
CC role in protein trafficking. In its GTP-bound form, its triggers the
CC association with coat proteins with the Golgi membrane. The hydrolysis
CC of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required
CC for dissociation of coat proteins from Golgi membranes and vesicles.
CC The GTP-bound form interacts with PICK1 to limit PICK1-mediated
CC inhibition of Arp2/3 complex activity; the function is linked to AMPA
CC receptor (AMPAR) trafficking, regulation of synaptic plasicity of
CC excitatory synapses and spine shrinkage during long-term depression
CC (LTD). {ECO:0000250|UniProtKB:P84077, ECO:0000269|PubMed:23889934}.
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 (By similarity). Interacts with ARHGAP21, ASAP2, HERC1,
CC PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 (PubMed:10022920,
CC PubMed:10623590, PubMed:10747863, PubMed:23889934). Interacts with
CC ARFGAP1, which hydrolyzes GTP and thus, regulates its function
CC (PubMed:7890632). Interacts with PI4KB in the Golgi complex. Interacts
CC with NCS1/FREQ in the Golgi and at the plasma membrane. Interacts with
CC PLEKHA3. Interacts with PLEKHA8; the interaction, together with
CC phosphatidylinositol 4-phosphate binding, is required for FAPP2-
CC mediated glucosylceramide transfer activity (By similarity). Interacts
CC (activated) with PICK1 (via PDZ domain); the interaction blocks Arp2/3
CC complex inhibition (PubMed:23889934). Interacts with IQSEC1 (By
CC similarity). Interacts with C9orf72 (By similarity).
CC {ECO:0000250|UniProtKB:P84077, ECO:0000250|UniProtKB:P84078,
CC ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10623590,
CC ECO:0000269|PubMed:10747863, ECO:0000269|PubMed:23889934,
CC ECO:0000269|PubMed:7890632}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:23889934}.
CC Cytoplasm, perinuclear region {ECO:0000250}. Synapse, synaptosome
CC {ECO:0000269|PubMed:23889934}. Postsynaptic density
CC {ECO:0000269|PubMed:23889934}. Membrane {ECO:0000250|UniProtKB:P84077};
CC Lipid-anchor {ECO:0000250|UniProtKB:P84077}. Golgi apparatus, trans-
CC Golgi network membrane {ECO:0000250|UniProtKB:P84078}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84078}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; L12380; AAA40685.1; -; mRNA.
DR EMBL; BC061552; AAH61552.1; -; mRNA.
DR RefSeq; NP_071963.1; NM_022518.3.
DR RefSeq; XP_006246587.1; XM_006246525.3.
DR PDB; 1RRF; X-ray; 3.00 A; A=1-181.
DR PDB; 1RRG; X-ray; 2.40 A; A/B=1-181.
DR PDBsum; 1RRF; -.
DR PDBsum; 1RRG; -.
DR AlphaFoldDB; P84079; -.
DR BMRB; P84079; -.
DR SMR; P84079; -.
DR BioGRID; 249023; 1.
DR CORUM; P84079; -.
DR IntAct; P84079; 2.
DR STRING; 10116.ENSRNOP00000064960; -.
DR iPTMnet; P84079; -.
DR PhosphoSitePlus; P84079; -.
DR SwissPalm; P84079; -.
DR World-2DPAGE; 0004:P84079; -.
DR jPOST; P84079; -.
DR PaxDb; P84079; -.
DR PRIDE; P84079; -.
DR Ensembl; ENSRNOT00000080028; ENSRNOP00000072575; ENSRNOG00000060229.
DR GeneID; 64310; -.
DR KEGG; rno:64310; -.
DR UCSC; RGD:621270; rat.
DR CTD; 375; -.
DR RGD; 621270; Arf1.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P84079; -.
DR OMA; VEYRNIQ; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P84079; -.
DR TreeFam; TF300808; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-RNO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR EvolutionaryTrace; P84079; -.
DR PRO; PR:P84079; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000060229; Expressed in jejunum and 19 other tissues.
DR Genevisible; P84079; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0012505; C:endomembrane system; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0019003; F:GDP binding; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:1990583; F:phospholipase D activator activity; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IMP:RGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISO:RGD.
DR GO; GO:0098586; P:cellular response to virus; ISO:RGD.
DR GO; GO:0097061; P:dendritic spine organization; IMP:UniProtKB.
DR GO; GO:0055108; P:Golgi to transport vesicle transport; IDA:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; IDA:UniProtKB.
DR GO; GO:0097212; P:lysosomal membrane organization; IDA:RGD.
DR GO; GO:1990386; P:mitotic cleavage furrow ingression; ISO:RGD.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IMP:RGD.
DR GO; GO:1902824; P:positive regulation of late endosome to lysosome transport; IMP:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
DR GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; IMP:RGD.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:1903725; P:regulation of phospholipid metabolic process; IDA:RGD.
DR GO; GO:0002090; P:regulation of receptor internalization; IDA:UniProtKB.
DR GO; GO:0070142; P:synaptic vesicle budding; IMP:RGD.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
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 3D-structure; Acetylation; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Protein transport; Reference proteome; Synapse; Synaptosome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P84077"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 1"
FT /id="PRO_0000207381"
FT BINDING 24..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1RRF, ECO:0007744|PDB:1RRG"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1RRF, ECO:0007744|PDB:1RRG"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1RRG"
FT MOD_RES 2
FT /note="N-acetylglycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84077"
FT LIPID 2
FT /note="N-myristoyl glycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84077"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1RRG"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1RRG"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1RRG"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1RRG"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1RRF"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1RRG"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1RRG"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1RRG"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1RRG"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:1RRG"
SQ SEQUENCE 181 AA; 20697 MW; AAC773D4A60186B6 CRC64;
MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ
K
