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Protein

ADP-ribosylation factor-related protein 1

Gene

Arfrp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 318GTPBy similarity
Nucleotide bindingi75 – 795GTPBy similarity
Nucleotide bindingi134 – 1374GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor-related protein 1
Short name:
ARF-related protein 1
Gene namesi
Name:Arfrp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1923938. Arfrp1.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: MGI
  • membrane Source: MGI
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

Pathology & Biotechi

Disruption phenotypei

Disruption of the gene leads to embryonic lethality during early gastrulation. Intestine-specific knockout mice display severe growth retardation due to reduced fat absorbtion and decrease in lipid release from the intestinal epithelium to the lymph and blood. Liver-specific knockout mice display impaired VLDL lipidation leading to reduced plasma triglyceride levels in the fasted state. Liver-specific knockout mice also display a disturbed glucose metabolism caused by a reduced plasma membrane localization of the glucose transporter GLUT2.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201ADP-ribosylation factor-related protein 1PRO_0000207488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BXL7.
PaxDbiQ8BXL7.
PRIDEiQ8BXL7.

PTM databases

PhosphoSiteiQ8BXL7.

Expressioni

Gene expression databases

BgeeiQ8BXL7.
CleanExiMM_ARFRP1.
ExpressionAtlasiQ8BXL7. baseline and differential.
GenevisibleiQ8BXL7. MM.

Interactioni

Subunit structurei

Interacts with SYS1.By similarity

Protein-protein interaction databases

BioGridi218262. 1 interaction.
STRINGi10090.ENSMUSP00000104436.

Structurei

3D structure databases

ProteinModelPortaliQ8BXL7.
SMRiQ8BXL7. Positions 17-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Arf family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00550000074639.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiQ8BXL7.
KOiK07952.
OMAiRDCLVQP.
OrthoDBiEOG76473Q.
PhylomeDBiQ8BXL7.
TreeFamiTF105788.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BXL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTLLSGLYK YMFQKDEYCI LILGLDNAGK TTFLEQSKTR FNKNYKGMSL
60 70 80 90 100
SKITTTVGLN IGTVDVGKAR LMFWDLGGQE ELQSLWDKYY AECHGVIYVI
110 120 130 140 150
DSTDEERLSE SKEAFEKVVS SEALDGVPIL VLANKQDVET CLSIPDIKTA
160 170 180 190 200
FSDCTCKIGR RDCLTQACSA LTGKGVREGI EWMVKCVVRN VHRPPRQRDI

T
Length:201
Mass (Da):22,659
Last modified:May 10, 2004 - v2
Checksum:i7BB6D213946F597E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411F → L in BAC32069 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ413952 Genomic DNA. Translation: CAC88691.1.
AJ413953 mRNA. Translation: CAC88692.1.
AK005174 mRNA. Translation: BAB23861.1.
AK044759 mRNA. Translation: BAC32069.1.
BC010713 mRNA. Translation: AAH10713.1.
CCDSiCCDS17209.1.
RefSeqiNP_001159463.1. NM_001165991.1.
NP_001159464.1. NM_001165992.1.
NP_083978.3. NM_029702.4.
XP_011238267.1. XM_011239965.1.
UniGeneiMm.87720.

Genome annotation databases

EnsembliENSMUST00000108808; ENSMUSP00000104436; ENSMUSG00000038671.
ENSMUST00000127988; ENSMUSP00000122066; ENSMUSG00000038671.
GeneIDi76688.
KEGGimmu:76688.
UCSCiuc008oly.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ413952 Genomic DNA. Translation: CAC88691.1.
AJ413953 mRNA. Translation: CAC88692.1.
AK005174 mRNA. Translation: BAB23861.1.
AK044759 mRNA. Translation: BAC32069.1.
BC010713 mRNA. Translation: AAH10713.1.
CCDSiCCDS17209.1.
RefSeqiNP_001159463.1. NM_001165991.1.
NP_001159464.1. NM_001165992.1.
NP_083978.3. NM_029702.4.
XP_011238267.1. XM_011239965.1.
UniGeneiMm.87720.

3D structure databases

ProteinModelPortaliQ8BXL7.
SMRiQ8BXL7. Positions 17-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218262. 1 interaction.
STRINGi10090.ENSMUSP00000104436.

PTM databases

PhosphoSiteiQ8BXL7.

Proteomic databases

MaxQBiQ8BXL7.
PaxDbiQ8BXL7.
PRIDEiQ8BXL7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108808; ENSMUSP00000104436; ENSMUSG00000038671.
ENSMUST00000127988; ENSMUSP00000122066; ENSMUSG00000038671.
GeneIDi76688.
KEGGimmu:76688.
UCSCiuc008oly.2. mouse.

Organism-specific databases

CTDi10139.
MGIiMGI:1923938. Arfrp1.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00550000074639.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiQ8BXL7.
KOiK07952.
OMAiRDCLVQP.
OrthoDBiEOG76473Q.
PhylomeDBiQ8BXL7.
TreeFamiTF105788.

Miscellaneous databases

NextBioi345635.
PROiQ8BXL7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BXL7.
CleanExiMM_ARFRP1.
ExpressionAtlasiQ8BXL7. baseline and differential.
GenevisibleiQ8BXL7. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Embryonic lethality caused by apoptosis during gastrulation in mice lacking the gene of the ADP-ribosylation factor-related protein 1."
    Mueller A.G., Moser M., Kluge R., Leder S., Blum M., Buttner R., Joost H.-G., Schurmann A.
    Mol. Cell. Biol. 22:1488-1494(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  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: Cerebellum and Retina.
  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].
    Strain: 129.
    Tissue: Mammary tumor.
  4. "Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to the trans-Golgi in mouse embryos and HeLa cells."
    Zahn C., Hommel A., Lu L., Hong W., Walther D.J., Florian S., Joost H.G., Schurmann A.
    Mol. Membr. Biol. 23:475-485(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION; FUNCTION AND DISRUPTION PHENOTYPE.
  5. "GTPase ARFRP1 is essential for normal hepatic glycogen storage and insulin-like growth factor 1 secretion."
    Hesse D., Jaschke A., Kanzleiter T., Witte N., Augustin R., Hommel A., Puschel G.P., Petzke K.J., Joost H.G., Schupp M., Schurmann A.
    Mol. Cell. Biol. 32:4363-4374(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNTION AND DISRUPTION PHENOTYPE.
  6. "The GTPase ARFRP1 controls the lipidation of chylomicrons in the Golgi of the intestinal epithelium."
    Jaschke A., Chung B., Hesse D., Kluge R., Zahn C., Moser M., Petzke K.J., Brigelius-Flohe R., Puchkov D., Koepsell H., Heeren J., Joost H.G., Schurmann A.
    Hum. Mol. Genet. 21:3128-3142(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AND DISRUPTION PHENOTYPE.
  7. "Trans-Golgi proteins participate in the control of lipid droplet and chylomicron formation."
    Hesse D., Jaschke A., Chung B., Schuermann A.
    Biosci. Rep. 33:1-9(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNTION AND DISRUPTION PHENOTYPE.
  8. "Hepatic trans-Golgi action coordinated by the GTPase ARFRP1 is crucial for lipoprotein lipidation and assembly."
    Hesse D., Radloff K., Jaschke A., Lagerpusch M., Chung B., Tailleux A., Staels B., Schurmann A.
    J. Lipid Res. 55:41-52(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AND DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiARFRP_MOUSE
AccessioniPrimary (citable) accession number: Q8BXL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 22, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.