ID   ARF2_MOUSE              Reviewed;         181 AA.
AC   Q8BSL7; P10947; P16500; Q3TJ37; Q91VR9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=ADP-ribosylation factor 2;
GN   Name=Arf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=8947846; DOI=10.1093/oxfordjournals.jbchem.a021484;
RA   Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT   "Structure and intracellular localization of mouse ADP-ribosylation factors
RT   type 1 to type 6 (ARF1-ARF6).";
RL   J. Biochem. 120:813-819(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Cerebellum, Embryo, Forelimb, Heart, Lung, and
RC   Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [4]
RP   PROTEIN SEQUENCE OF 39-59 AND 80-97, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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; D87899; BAA13491.1; -; mRNA.
DR   EMBL; AK031259; BAC27325.1; -; mRNA.
DR   EMBL; AK042977; BAC31426.1; -; mRNA.
DR   EMBL; AK053123; BAC35273.1; -; mRNA.
DR   EMBL; AK077591; BAC36882.1; -; mRNA.
DR   EMBL; AK167133; BAE39279.1; -; mRNA.
DR   EMBL; AK167601; BAE39658.1; -; mRNA.
DR   EMBL; AK167653; BAE39704.1; -; mRNA.
DR   EMBL; AK169094; BAE40877.1; -; mRNA.
DR   EMBL; AK169412; BAE41158.1; -; mRNA.
DR   EMBL; BC010487; AAH10487.1; -; mRNA.
DR   CCDS; CCDS25525.1; -.
DR   PIR; JC4946; JC4946.
DR   RefSeq; NP_001291503.1; NM_001304574.1.
DR   RefSeq; NP_031503.1; NM_007477.5.
DR   PDB; 1J2J; X-ray; 1.60 A; A=18-181.
DR   PDBsum; 1J2J; -.
DR   AlphaFoldDB; Q8BSL7; -.
DR   SMR; Q8BSL7; -.
DR   BioGRID; 198185; 33.
DR   IntAct; Q8BSL7; 1.
DR   STRING; 10090.ENSMUSP00000102622; -.
DR   GlyGen; Q8BSL7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BSL7; -.
DR   PhosphoSitePlus; Q8BSL7; -.
DR   SwissPalm; Q8BSL7; -.
DR   EPD; Q8BSL7; -.
DR   jPOST; Q8BSL7; -.
DR   MaxQB; Q8BSL7; -.
DR   PaxDb; 10090-ENSMUSP00000102622; -.
DR   PeptideAtlas; Q8BSL7; -.
DR   ProteomicsDB; 277272; -.
DR   Pumba; Q8BSL7; -.
DR   DNASU; 11841; -.
DR   Ensembl; ENSMUST00000057921.10; ENSMUSP00000051814.4; ENSMUSG00000062421.14.
DR   Ensembl; ENSMUST00000063347.12; ENSMUSP00000102622.3; ENSMUSG00000062421.14.
DR   GeneID; 11841; -.
DR   KEGG; mmu:11841; -.
DR   UCSC; uc007lvx.2; mouse.
DR   AGR; MGI:99595; -.
DR   CTD; 11841; -.
DR   MGI; MGI:99595; Arf2.
DR   VEuPathDB; HostDB:ENSMUSG00000062421; -.
DR   eggNOG; KOG0070; Eukaryota.
DR   GeneTree; ENSGT00950000183080; -.
DR   HOGENOM; CLU_040729_9_3_1; -.
DR   InParanoid; Q8BSL7; -.
DR   OMA; QEVRIVM; -.
DR   OrthoDB; 5474610at2759; -.
DR   PhylomeDB; Q8BSL7; -.
DR   TreeFam; TF300808; -.
DR   BioGRID-ORCS; 11841; 1 hit in 62 CRISPR screens.
DR   ChiTaRS; Arf2; mouse.
DR   EvolutionaryTrace; Q8BSL7; -.
DR   PRO; PR:Q8BSL7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8BSL7; Protein.
DR   Bgee; ENSMUSG00000062421; Expressed in placenta labyrinth and 254 other cell types or tissues.
DR   ExpressionAtlas; Q8BSL7; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; TAS:MGI.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; TAS:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd04150; Arf1_5_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045872; Arf1-5-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR   PANTHER; PTHR11711:SF449; ADP-RIBOSYLATION FACTOR 2; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51417; ARF; 1.
DR   Genevisible; Q8BSL7; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; ER-Golgi transport;
KW   Golgi apparatus; GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   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_0000207384"
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"
FT   CONFLICT        54..55
FT                   /note="ET -> GH (in Ref. 3; AAH10487)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="Y -> N (in Ref. 2; BAC27325)"
FT                   /evidence="ECO:0000305"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   STRAND          49..58
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           100..111
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:1J2J"
FT   HELIX           166..178
FT                   /evidence="ECO:0007829|PDB:1J2J"
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
//