ARF4_RAT
ID ARF4_RAT Reviewed; 180 AA.
AC P61751; P36403;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ADP-ribosylation factor 4;
GN Name=Arf4;
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=Testis;
RX PubMed=1358888; DOI=10.1016/s0021-9258(18)35953-2;
RA Mishima K., Price S.R., Nightingale M.S., Kousvelari E., Moss J.,
RA Vaughan M.;
RT "Regulation of ADP-ribosylation factor (ARF) expression. Cross-species
RT conservation of the developmental and tissue-specific alternative
RT polyadenylation of ARF 4 mRNA.";
RL J. Biol. Chem. 267:24109-24116(1992).
RN [2]
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 [3]
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).
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; may modulate vesicle budding and
CC uncoating within the Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Membrane
CC {ECO:0000250|UniProtKB:P18085}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P18085}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; L12383; AAA40688.1; -; mRNA.
DR EMBL; BC063167; AAH63167.1; -; mRNA.
DR PIR; I55371; I55371.
DR RefSeq; NP_077065.1; NM_024151.1.
DR AlphaFoldDB; P61751; -.
DR SMR; P61751; -.
DR BioGRID; 249404; 3.
DR IntAct; P61751; 3.
DR MINT; P61751; -.
DR STRING; 10116.ENSRNOP00000017692; -.
DR iPTMnet; P61751; -.
DR PhosphoSitePlus; P61751; -.
DR SwissPalm; P61751; -.
DR jPOST; P61751; -.
DR PaxDb; P61751; -.
DR PRIDE; P61751; -.
DR Ensembl; ENSRNOT00000017692; ENSRNOP00000017692; ENSRNOG00000012623.
DR GeneID; 79120; -.
DR KEGG; rno:79120; -.
DR UCSC; RGD:621275; rat.
DR CTD; 378; -.
DR RGD; 621275; Arf4.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000156297; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P61751; -.
DR OMA; CATQGEG; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P61751; -.
DR TreeFam; TF300808; -.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P61751; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000012623; Expressed in jejunum and 20 other tissues.
DR Genevisible; P61751; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0031584; P:activation of phospholipase D activity; ISO:RGD.
DR GO; GO:0045176; P:apical protein localization; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0060996; P:dendritic spine development; ISO:RGD.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:RGD.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:RGD.
DR GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
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 2: Evidence at transcript level;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P18085"
FT CHAIN 2..180
FT /note="ADP-ribosylation factor 4"
FT /id="PRO_0000207394"
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 MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18085"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P18085"
SQ SEQUENCE 180 AA; 20397 MW; 09112917D8CE15D6 CRC64;
MGLTISSLFS RLFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERI QEGAAVLQKM LLEDELQDAV
LLLFANKQDL PNAMAISEMT DKLGLQSLRN RTWYVQATCA TQGTGLYEGL DWLSNELSKR
