ARF1_BOVIN
ID ARF1_BOVIN Reviewed; 181 AA.
AC P84080; A5D7F1; P10947; P32889; Q3SZG1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ADP-ribosylation factor 1;
GN Name=ARF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3133654; DOI=10.1073/pnas.85.13.4620;
RA Sewell J., Kahn R.A.;
RT "Sequences of the bovine and yeast ADP-ribosylation factor and comparison
RT to other GTP-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4620-4624(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford; TISSUE=Basal ganglia, and Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH TMED2 AND TMED10, AND MUTAGENESIS OF GLN-71.
RX PubMed=11703931; DOI=10.1016/s1534-5807(01)00004-1;
RA Majoul I., Straub M., Hell S.W., Duden R., Soling H.D.;
RT "KDEL-cargo regulates interactions between proteins involved in COPI
RT vesicle traffic: measurements in living cells using FRET.";
RL Dev. Cell 1:139-153(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH PSCD2; GDP AND
RP BREFELDIN.
RX PubMed=14654833; DOI=10.1038/nature02197;
RA Renault L., Guibert B., Cherfils J.;
RT "Structural snapshots of the mechanism and inhibition of a guanine
RT nucleotide exchange factor.";
RL Nature 426:525-530(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 18-181 IN COMPLEX WITH GTP ANALOG
RP AND IQSEC1, AND INTERACTION WITH IQSEC1.
RX PubMed=24058294; DOI=10.1371/journal.pbio.1001652;
RA Aizel K., Biou V., Navaza J., Duarte L.V., Campanacci V., Cherfils J.,
RA Zeghouf M.;
RT "Integrated conformational and lipid-sensing regulation of endosomal ArfGEF
RT BRAG2.";
RL PLoS Biol. 11:E1001652-E1001652(2013).
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}.
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, GGA1, HERC1,
CC PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 (PubMed:11703931,
CC PubMed:14654833). Interacts with ARFGAP1, which hydrolyzes GTP and
CC thus, regulates its function. Interacts with PI4KB in the Golgi
CC complex. Interacts with NCS1/FREQ in the Golgi and at the plasma
CC 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 (By similarity). Interacts with IQSEC1
CC (PubMed:24058294). Interacts with C9orf72 (By similarity).
CC {ECO:0000250|UniProtKB:P84077, ECO:0000250|UniProtKB:P84078,
CC ECO:0000250|UniProtKB:P84079, ECO:0000269|PubMed:11703931,
CC ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294}.
CC -!- INTERACTION:
CC P84080; P62168: Ncs1; Xeno; NbExp=2; IntAct=EBI-449051, EBI-907774;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear region
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P84077}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84077}. Golgi apparatus, trans-Golgi network
CC 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; J03275; AAA30361.1; -; mRNA.
DR EMBL; BC102874; AAI02875.1; -; mRNA.
DR EMBL; BC140532; AAI40533.1; -; mRNA.
DR PIR; A36167; A36167.
DR RefSeq; NP_788826.1; NM_176653.4.
DR RefSeq; XP_005208456.1; XM_005208399.3.
DR RefSeq; XP_005208457.1; XM_005208400.3.
DR PDB; 1R8Q; X-ray; 1.86 A; A/B=1-181.
DR PDB; 1R8S; X-ray; 1.46 A; A=18-181.
DR PDB; 1S9D; X-ray; 1.80 A; A=18-181.
DR PDB; 4C0A; X-ray; 3.30 A; C/D/G/H=18-181.
DR PDBsum; 1R8Q; -.
DR PDBsum; 1R8S; -.
DR PDBsum; 1S9D; -.
DR PDBsum; 4C0A; -.
DR AlphaFoldDB; P84080; -.
DR BMRB; P84080; -.
DR SMR; P84080; -.
DR BioGRID; 160195; 1.
DR IntAct; P84080; 8.
DR MINT; P84080; -.
DR STRING; 9913.ENSBTAP00000010159; -.
DR PaxDb; P84080; -.
DR PeptideAtlas; P84080; -.
DR PRIDE; P84080; -.
DR Ensembl; ENSBTAT00000010159; ENSBTAP00000010159; ENSBTAG00000007725.
DR GeneID; 338058; -.
DR KEGG; bta:338058; -.
DR CTD; 375; -.
DR VEuPathDB; HostDB:ENSBTAG00000007725; -.
DR VGNC; VGNC:50209; ARF1.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P84080; -.
DR OMA; WEDVCRI; -.
DR OrthoDB; 1362554at2759; -.
DR TreeFam; TF300808; -.
DR Reactome; R-BTA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-BTA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-BTA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-BTA-6811438; Intra-Golgi traffic.
DR EvolutionaryTrace; P84080; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000007725; Expressed in thyroid gland and 105 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
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; IDA:AgBase.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
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; 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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Protein transport; Reference proteome;
KW 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_0000207377"
FT BINDING 24..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305, ECO:0007744|PDB:1R8Q,
FT ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D,
FT ECO:0007744|PDB:4C0A"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305, ECO:0007744|PDB:1R8Q,
FT ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D,
FT ECO:0007744|PDB:4C0A"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305, ECO:0007744|PDB:1R8Q,
FT ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D,
FT ECO:0007744|PDB:4C0A"
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 MUTAGEN 71
FT /note="Q->L: Mainly GTP-bound form; abolishes interaction
FT with TMED10."
FT /evidence="ECO:0000269|PubMed:11703931"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1R8Q"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:1R8S"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1R8Q"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1R8S"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:1R8S"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1R8S"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1R8S"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1R8S"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1R8S"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1R8S"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:1R8S"
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
