ARF2_MOUSE
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 03-AUG-2022, entry version 146.
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 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, Spleen,
RC 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 iPTMnet; Q8BSL7; -.
DR PhosphoSitePlus; Q8BSL7; -.
DR SwissPalm; Q8BSL7; -.
DR EPD; Q8BSL7; -.
DR jPOST; Q8BSL7; -.
DR MaxQB; Q8BSL7; -.
DR PaxDb; Q8BSL7; -.
DR PeptideAtlas; Q8BSL7; -.
DR PRIDE; Q8BSL7; -.
DR ProteomicsDB; 277272; -.
DR DNASU; 11841; -.
DR Ensembl; ENSMUST00000057921; ENSMUSP00000051814; ENSMUSG00000062421.
DR Ensembl; ENSMUST00000063347; ENSMUSP00000102622; ENSMUSG00000062421.
DR GeneID; 11841; -.
DR KEGG; mmu:11841; -.
DR UCSC; uc007lvx.2; mouse.
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; CETISIS; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; Q8BSL7; -.
DR TreeFam; TF300808; -.
DR BioGRID-ORCS; 11841; 1 hit in 59 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 251 other tissues.
DR ExpressionAtlas; Q8BSL7; baseline and differential.
DR Genevisible; Q8BSL7; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
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; -; 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; 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
