ARF5_HUMAN
ID ARF5_HUMAN Reviewed; 180 AA.
AC P84085; P26437;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ADP-ribosylation factor 5;
GN Name=ARF5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1993656; DOI=10.1016/s0021-9258(18)49913-9;
RA Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.;
RT "Molecular identification of ADP-ribosylation factor mRNAs and their
RT expression in mammalian cells.";
RL J. Biol. Chem. 266:2772-2777(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9169151; DOI=10.1006/geno.1997.4689;
RA McGuire R.E., Daiger S.P., Green E.D.;
RT "Localization and characterization of the human ADP-ribosylation factor 5
RT (ARF5) gene.";
RL Genomics 41:481-484(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [6]
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 [7]
RP INTERACTION WITH GGA1; GGA2 AND GGA3.
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 [8]
RP INTERACTION WITH RAB11FIP3 AND RAB11FIP4.
RX PubMed=17030804; DOI=10.1073/pnas.0605357103;
RA Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K.,
RA Wakatsuki S.;
RT "Structural basis for Rab11-dependent membrane recruitment of a family of
RT Rab11-interacting protein 3 (FIP3)/Arfophilin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006).
RN [9]
RP INTERACTION WITH NCS1, AND SUBCELLULAR LOCATION.
RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT "Specificity, promiscuity and localization of ARF protein interactions with
RT NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL Traffic 8:1080-1092(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 8-180 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Structure of human ADP-ribosylation factor 5.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC {ECO:0000250|UniProtKB:P84084}.
CC -!- FUNCTION: (Microbial infection) Functions as an allosteric activator of
CC the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
CC {ECO:0000305}.
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 (PubMed:10022920). Interacts
CC with NCS1/FREQ at the Golgi complex (PubMed:17555535). Interacts with
CC RAB11FIP3 and RAB11FIP4 (PubMed:17030804).
CC {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:11950392,
CC ECO:0000269|PubMed:17030804, ECO:0000269|PubMed:17555535}.
CC -!- INTERACTION:
CC P84085; Q96HD9: ACY3; NbExp=3; IntAct=EBI-4289908, EBI-3916242;
CC P84085; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-4289908, EBI-2340258;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17555535}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. Membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:P84084}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84084}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; M57567; AAA90927.1; -; mRNA.
DR EMBL; U73002; AAC51299.1; -; Genomic_DNA.
DR EMBL; AF493884; AAM12598.1; -; mRNA.
DR EMBL; BT007087; AAP35750.1; -; mRNA.
DR EMBL; BC003043; AAH03043.1; -; mRNA.
DR EMBL; BC033104; AAH33104.1; -; mRNA.
DR CCDS; CCDS34745.1; -.
DR PIR; A23741; A23741.
DR RefSeq; NP_001653.1; NM_001662.3.
DR PDB; 2B6H; X-ray; 1.76 A; A=8-180.
DR PDBsum; 2B6H; -.
DR AlphaFoldDB; P84085; -.
DR SMR; P84085; -.
DR BioGRID; 106876; 157.
DR DIP; DIP-61289N; -.
DR IntAct; P84085; 41.
DR MINT; P84085; -.
DR STRING; 9606.ENSP00000000233; -.
DR ChEMBL; CHEMBL5986; -.
DR GlyGen; P84085; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P84085; -.
DR MetOSite; P84085; -.
DR PhosphoSitePlus; P84085; -.
DR SwissPalm; P84085; -.
DR BioMuta; ARF5; -.
DR DMDM; 51316990; -.
DR EPD; P84085; -.
DR jPOST; P84085; -.
DR MassIVE; P84085; -.
DR MaxQB; P84085; -.
DR PaxDb; P84085; -.
DR PeptideAtlas; P84085; -.
DR PRIDE; P84085; -.
DR ProteomicsDB; 57748; -.
DR TopDownProteomics; P84085; -.
DR Antibodypedia; 31827; 249 antibodies from 32 providers.
DR DNASU; 381; -.
DR Ensembl; ENST00000000233.10; ENSP00000000233.5; ENSG00000004059.11.
DR GeneID; 381; -.
DR KEGG; hsa:381; -.
DR MANE-Select; ENST00000000233.10; ENSP00000000233.5; NM_001662.4; NP_001653.1.
DR UCSC; uc003vmb.3; human.
DR CTD; 381; -.
DR DisGeNET; 381; -.
DR GeneCards; ARF5; -.
DR HGNC; HGNC:658; ARF5.
DR HPA; ENSG00000004059; Low tissue specificity.
DR MIM; 103188; gene.
DR neXtProt; NX_P84085; -.
DR OpenTargets; ENSG00000004059; -.
DR PharmGKB; PA24941; -.
DR VEuPathDB; HostDB:ENSG00000004059; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000156878; -.
DR InParanoid; P84085; -.
DR OMA; TWHVEAT; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P84085; -.
DR TreeFam; TF300808; -.
DR PathwayCommons; P84085; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; P84085; -.
DR BioGRID-ORCS; 381; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; ARF5; human.
DR EvolutionaryTrace; P84085; -.
DR GeneWiki; ARF5; -.
DR GenomeRNAi; 381; -.
DR Pharos; P84085; Tbio.
DR PRO; PR:P84085; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P84085; protein.
DR Bgee; ENSG00000004059; Expressed in lower esophagus mucosa and 92 other tissues.
DR ExpressionAtlas; P84085; baseline and differential.
DR Genevisible; P84085; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IGI:WormBase.
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; Cytoplasm; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..180
FT /note="ADP-ribosylation factor 5"
FT /id="PRO_0000207396"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:2B6H"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2B6H"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2B6H"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:2B6H"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2B6H"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2B6H"
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
