ID   ARF2_RAT                Reviewed;         181 AA.
AC   P84082; P10947; P16500; Q4KM00;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=ADP-ribosylation factor 2;
GN   Name=Arf2;
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=Placenta;
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.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; L12381; AAA40686.1; -; mRNA.
DR   EMBL; BC098915; AAH98915.1; -; mRNA.
DR   RefSeq; NP_077064.1; NM_024150.2.
DR   AlphaFoldDB; P84082; -.
DR   SMR; P84082; -.
DR   BioGRID; 249403; 3.
DR   IntAct; P84082; 2.
DR   MINT; P84082; -.
DR   STRING; 10116.ENSRNOP00000006483; -.
DR   iPTMnet; P84082; -.
DR   PhosphoSitePlus; P84082; -.
DR   jPOST; P84082; -.
DR   PaxDb; P84082; -.
DR   PRIDE; P84082; -.
DR   Ensembl; ENSRNOT00000006483; ENSRNOP00000006483; ENSRNOG00000004807.
DR   GeneID; 79119; -.
DR   KEGG; rno:79119; -.
DR   UCSC; RGD:621271; rat.
DR   CTD; 11841; -.
DR   RGD; 621271; Arf2.
DR   eggNOG; KOG0070; Eukaryota.
DR   GeneTree; ENSGT00950000183080; -.
DR   HOGENOM; CLU_040729_9_3_1; -.
DR   InParanoid; P84082; -.
DR   OMA; CETISIS; -.
DR   OrthoDB; 1362554at2759; -.
DR   PhylomeDB; P84082; -.
DR   TreeFam; TF300808; -.
DR   PRO; PR:P84082; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000004807; Expressed in heart and 20 other tissues.
DR   Genevisible; P84082; RN.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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; Myristate;
KW   Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..181
FT                   /note="ADP-ribosylation factor 2"
FT                   /id="PRO_0000207385"
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:0000255"
SQ   SEQUENCE   181 AA;  20746 MW;  95BE17A962B83016 CRC64;
     MGNVFEKLFK SLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELTRM LAEDELRDAV
     LLVFVNKQDL PNAMNAAEIT DKLGLHSLRQ RNWYIQATCA TSGDGLYEGL DWLSNQLKNQ
     K