Q8BSL7 (ARF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor 2

Gene names

Name:

Arf2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location	Golgi apparatus.
Sequence similarities	Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Golgi apparatus
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Myristate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein transport Traceable author statement Ref.1. Source: MGI small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro vesicle-mediated transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay Ref.1. Source: MGI
Molecular_function	GTP binding Traceable author statement Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Potential

Chain

2 – 181

180

ADP-ribosylation factor 2

PRO_0000207384

Regions

Nucleotide binding

24 – 31

8

GTP By similarity

Nucleotide binding

67 – 71

5

GTP By similarity

Nucleotide binding

126 – 129

4

GTP By similarity

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine Potential

Experimental info

Sequence conflict

54 – 55

2

ET → GH in AAH10487. Ref.3

Sequence conflict

154

1

Y → N in BAC27325. Ref.2

Secondary structure

1

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181

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Helix

30 – 39

10

Beta strand

49 – 58

10

Beta strand

61 – 68

8

Helix

72 – 81

10

Beta strand

87 – 93

7

Helix

97 – 99

3

Helix

100 – 111

12

Helix

114 – 116

3

Beta strand

120 – 126

7

Helix

136 – 143

8

Helix

145 – 147

3

Beta strand

153 – 157

5

Turn

160 – 163

4

Helix

166 – 178

13

Sequences

	Sequence		Length	Mass (Da)
	Q8BSL7 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 95BE17A962B83016	FASTA	181	20,746
	10 20 30 40 50 60 MGNVFEKLFK SLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 70 80 90 100 110 120 ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELTRM LAEDELRDAV 130 140 150 160 170 180 LLVFVNKQDL PNAMNAAEIT DKLGLHSLRQ RNWYIQATCA TSGDGLYEGL DWLSNQLKNQ K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6)." Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K. J. Biochem. 120:813-819(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion, Cerebellum, Embryo, Forelimb, Heart, Lung and Placenta.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[4]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 39-59 AND 80-97, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D87899 mRNA. Translation: BAA13491.1.
AK031259 mRNA. Translation: BAC27325.1.
AK042977 mRNA. Translation: BAC31426.1.
AK053123 mRNA. Translation: BAC35273.1.
AK077591 mRNA. Translation: BAC36882.1.
AK167133 mRNA. Translation: BAE39279.1.
AK167601 mRNA. Translation: BAE39658.1.
AK167653 mRNA. Translation: BAE39704.1.
AK169094 mRNA. Translation: BAE40877.1.
AK169412 mRNA. Translation: BAE41158.1.
BC010487 mRNA. Translation: AAH10487.1.

IPI

IPI00135730.

PIR

JC4946.

RefSeq

NP_031503.1. NM_007477.4.

UniGene

Mm.5061.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J2J	X-ray	1.60	A	18-181	[»]

ProteinModelPortal

Q8BSL7.

SMR

Q8BSL7. Positions 18-177.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8BSL7. 1 interaction.

PTM databases

PhosphoSite

Q8BSL7.

Proteomic databases

PaxDb

Q8BSL7.

PRIDE

Q8BSL7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000057921; ENSMUSP00000051814; ENSMUSG00000062421.
ENSMUST00000063347; ENSMUSP00000102622; ENSMUSG00000062421.

GeneID

11841.

KEGG

mmu:11841.

Organism-specific databases

CTD

11841.

MGI

MGI:99595. Arf2.

Phylogenomic databases

eggNOG

COG1100.

GeneTree

ENSGT00650000093078.

HOGENOM

HOG000163691.

HOVERGEN

HBG002073.

InParanoid

Q8BSL7.

KO

K06883.

OMA

EACDELQ.

OrthoDB

EOG4PZJ7Q.

Gene expression databases

ArrayExpress

Q8BSL7.

Bgee

Q8BSL7.

CleanEx

MM_ARF2.

Genevestigator

Q8BSL7.

GermOnline

ENSMUSG00000062421. Mus musculus.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]

Pfam

PF00025. Arf. 1 hit.
[Graphical view]

PRINTS

PR00328. SAR1GTPBP.

SMART

SM00177. ARF. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51417. ARF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARF2. mouse.

EvolutionaryTrace

Q8BSL7.

NextBio

20806307.

SOURCE

Search...

Entry information

Entry name

ARF2_MOUSE

Accession

Primary (citable) accession number: Q8BSL7
Secondary accession number(s): P10947 , P16500, Q3TJ37, Q91VR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program