ARF5_RAT
ID ARF5_RAT Reviewed; 180 AA.
AC P84083; P26437;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ADP-ribosylation factor 5;
GN Name=Arf5;
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=Ovary;
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 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).
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 -!- 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). Binds ASAP2 (By similarity). Interacts with
CC NCS1/FREQ at the Golgi complex. Interacts with RAB11FIP3 and RAB11FIP4
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P84084,
CC ECO:0000250|UniProtKB:P84085}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P84084}.
CC Cytoplasm, perinuclear region {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:0000250|UniProtKB:P84084}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84084}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L12384; AAA40689.1; -; mRNA.
DR EMBL; BC087692; AAH87692.1; -; mRNA.
DR RefSeq; NP_077063.1; NM_024149.1.
DR AlphaFoldDB; P84083; -.
DR SMR; P84083; -.
DR BioGRID; 249402; 1.
DR IntAct; P84083; 3.
DR STRING; 10116.ENSRNOP00000010429; -.
DR iPTMnet; P84083; -.
DR PhosphoSitePlus; P84083; -.
DR SwissPalm; P84083; -.
DR jPOST; P84083; -.
DR PaxDb; P84083; -.
DR PRIDE; P84083; -.
DR GeneID; 79117; -.
DR KEGG; rno:79117; -.
DR UCSC; RGD:621278; rat.
DR CTD; 381; -.
DR RGD; 621278; Arf5.
DR VEuPathDB; HostDB:ENSRNOG00000007806; -.
DR eggNOG; KOG0070; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P84083; -.
DR OMA; TWHVEAT; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P84083; -.
DR TreeFam; TF300808; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P84083; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007806; Expressed in pancreas and 19 other tissues.
DR Genevisible; P84083; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:RGD.
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_0000207398"
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
