ID   ARF1_MACFA              Reviewed;         181 AA.
AC   Q4R5P2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ADP-ribosylation factor 1;
GN   Name=ARF1; ORFNames=QccE-11717;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 among different compartments. Modulates
CC       vesicle budding and uncoating within the Golgi complex. Deactivation
CC       induces the redistribution of the entire Golgi complex to the
CC       endoplasmic reticulum, suggesting a crucial role in protein
CC       trafficking. In its GTP-bound form, its triggers the association with
CC       coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound
CC       GTP, which is mediated by ARFGAPs proteins, is required for
CC       dissociation of coat proteins from Golgi membranes and vesicles. The
CC       GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition
CC       of Arp2/3 complex activity; the function is linked to AMPA receptor
CC       (AMPAR) trafficking, regulation of synaptic plasicity of excitatory
CC       synapses and spine shrinkage during long-term depression (LTD) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ARHGAP21, ASAP2, GGA1, HERC1, PRKCABP, PIP5K1B,
CC       TMED2, PSCD2, TMED10 and GRIA2. Interacts with ARFGAP1, which
CC       hydrolyzes GTP and thus, regulates its function. Interacts with PI4KB
CC       in the Golgi complex. Interacts with NCS1/FREQ in the Golgi and at the
CC       plasma membrane. Interacts with PLEKHA3. Interacts with PLEKHA8; the
CC       interaction, together with phosphatidylinositol 4-phosphate binding, is
CC       required for FAPP2-mediated glucosylceramide transfer activity.
CC       Interacts (activated) with PICK1 (via PDZ domain); the interaction
CC       blocks Arp2/3 complex inhibition. Interacts with IQSEC1. Interacts with
CC       C9orf72. {ECO:0000250|UniProtKB:P84078, ECO:0000250|UniProtKB:P84080}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm,
CC       perinuclear region {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC       Postsynaptic density {ECO:0000250}. Membrane
CC       {ECO:0000250|UniProtKB:P84077}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P84077}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; AB169501; BAE01583.1; -; mRNA.
DR   RefSeq; NP_001270621.1; NM_001283692.1.
DR   RefSeq; XP_005541113.1; XM_005541056.2.
DR   AlphaFoldDB; Q4R5P2; -.
DR   SMR; Q4R5P2; -.
DR   STRING; 9541.XP_005541111.1; -.
DR   PRIDE; Q4R5P2; -.
DR   Ensembl; ENSMFAT00000028433; ENSMFAP00000000267; ENSMFAG00000034073.
DR   GeneID; 101926228; -.
DR   KEGG; mcf:101926228; -.
DR   CTD; 375; -.
DR   VEuPathDB; HostDB:ENSMFAG00000034073; -.
DR   eggNOG; KOG0070; Eukaryota.
DR   GeneTree; ENSGT00950000183080; -.
DR   OMA; VEYRNIQ; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000034073; Expressed in temporal lobe and 13 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB.
DR   GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR   GO; GO:0002090; P:regulation of receptor internalization; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Membrane; Myristate; Nucleotide-binding; Protein transport;
KW   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_0000207379"
FT   BINDING         24..32
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P84080"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P84080"
FT   BINDING         160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P84080"
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"
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